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1. Differential and shared genetic effects on kidney function between diabetic and non-diabetic individuals

Author: Winkler, Thomas W., Rasheed, Humaira, Teumer, Alexander, Gorski, Mathias, Rowan, Bryce X., Stanzick, Kira J., Thomas, Laurent F., Tin, Adrienne, Hoppmann, Anselm, Chu, Audrey Y., Tayo, Bamidele, Thio, Chris H. L., Cusi, Daniele, Chai, Jin-Fang, Sieber, Karsten B., Horn, Katrin, Li, Man, Scholz, Markus, Cocca, Massimiliano, Wuttke, Matthias, van der Most, Peter J., Yang, Qiong, Ghasemi, Sahar, Nutile, Teresa, Li, Yong, Pontali, Giulia, Günther, Felix, Dehghan, Abbas, Correa, Adolfo, Parsa, Afshin, Feresin, Agnese, de Vries, Aiko P. J., Zonderman, Alan B., Smith, Albert V., Oldehinkel, Albertine J., De Grandi, Alessandro, Rosenkranz, Alexander R., Franke, Andre, Teren, Andrej, Metspalu, Andres, Hicks, Andrew A., Morris, Andrew P., Tönjes, Anke, Morgan, Anna, Podgornaia, Anna I., Peters, Annette, Körner, Antje, Mahajan, Anubha, Campbell, Archie, Freedman, Barry I., Spedicati, Beatrice, Ponte, Belen, Schöttker, Ben, Brumpton, Ben, Banas, Bernhard, Krämer, Bernhard K., Jung, Bettina, Åsvold, Bjørn Olav, Smith, Blair H., Ning, Boting, Penninx, Brenda W. J. H., Vanderwerff, Brett R., Psaty, Bruce M., Kammerer, Candace M., Langefeld, Carl D., Hayward, Caroline, Spracklen, Cassandra N., Robinson-Cohen, Cassianne, Hartman, Catharina A., Lindgren, Cecilia M., Wang, Chaolong, Sabanayagam, Charumathi, Heng, Chew-Kiat, Lanzani, Chiara, Khor, Chiea-Chuen, Cheng, Ching-Yu, Fuchsberger, Christian, Gieger, Christian, Shaffer, Christian M., Schulz, Christina-Alexandra, Willer, Cristen J., Chasman, Daniel I., Gudbjartsson, Daniel F., Ruggiero, Daniela, Toniolo, Daniela, Czamara, Darina, Porteous, David J., Waterworth, Dawn M., Mascalzoni, Deborah, Mook-Kanamori, Dennis O., Reilly, Dermot F., Daw, E. Warwick, Hofer, Edith, Boerwinkle, Eric, Salvi, Erika, Bottinger, Erwin P., Tai, E-Shyong, Catamo, Eulalia, Rizzi, Federica, Guo, Feng, Rivadeneira, Fernando, Guilianini, Franco, Sveinbjornsson, Gardar, Ehret, Georg, Waeber, Gerard, Biino, Ginevra, Girotto, Giorgia, Pistis, Giorgio, Nadkarni, Girish N., Delgado, Graciela E., Montgomery, Grant W., Snieder, Harold, Campbell, Harry, White, Harvey D., Gao, He, Stringham, Heather M., Schmidt, Helena, Li, Hengtong, Brenner, Hermann, Holm, Hilma, Kirsten, Holger, Kramer, Holly, Rudan, Igor, Nolte, Ilja M., Tzoulaki, Ioanna, Olafsson, Isleifur, Martins, Jade, Cook, James P., Wilson, James F., Halbritter, Jan, Felix, Janine F., Divers, Jasmin, Kooner, Jaspal S., Lee, Jeannette Jen-Mai, O’Connell, Jeffrey, Rotter, Jerome I., Liu, Jianjun, Xu, Jie, Thiery, Joachim, Ärnlöv, Johan, Kuusisto, Johanna, Jakobsdottir, Johanna, Tremblay, Johanne, Chambers, John C., Whitfield, John B., Gaziano, John M., Marten, Jonathan, Coresh, Josef, Jonas, Jost B., Mychaleckyj, Josyf C., Christensen, Kaare, Eckardt, Kai-Uwe, Mohlke, Karen L., Endlich, Karlhans, Dittrich, Katalin, Ryan, Kathleen A., Rice, Kenneth M., Taylor, Kent D., Ho, Kevin, Nikus, Kjell, Matsuda, Koichi, Strauch, Konstantin, Miliku, Kozeta, Hveem, Kristian, Lind, Lars, Wallentin, Lars, Yerges-Armstrong, Laura M., Raffield, Laura M., Phillips, Lawrence S., Launer, Lenore J., Lyytikäinen, Leo-Pekka, Lange, Leslie A., Citterio, Lorena, Klaric, Lucija, Ikram, M. Arfan, Ising, Marcus, Kleber, Marcus E., Francescatto, Margherita, Concas, Maria Pina, Ciullo, Marina, Piratsu, Mario, Orho-Melander, Marju, Laakso, Markku, Loeffler, Markus, Perola, Markus, de Borst, Martin H., Gögele, Martin, Bianca, Martina La, Lukas, Mary Ann, Feitosa, Mary F., Biggs, Mary L., Wojczynski, Mary K., Kavousi, Maryam, Kanai, Masahiro, Akiyama, Masato, Yasuda, Masayuki, Nauck, Matthias, Waldenberger, Melanie, Chee, Miao-Li, Chee, Miao-Ling, Boehnke, Michael, Preuss, Michael H., Stumvoll, Michael, Province, Michael A., Evans, Michele K., O’Donoghue, Michelle L., Kubo, Michiaki, Kähönen, Mika, Kastarinen, Mika, Nalls, Mike A., Kuokkanen, Mikko, Ghanbari, Mohsen, Bochud, Murielle, Josyula, Navya Shilpa, Martin, Nicholas G., Tan, Nicholas Y. Q., Palmer, Nicholette D., Pirastu, Nicola, Schupf, Nicole, Verweij, Niek, Hutri-Kähönen, Nina, Mononen, Nina, Bansal, Nisha, Devuyst, Olivier, Melander, Olle, Raitakari, Olli T., Polasek, Ozren, Manunta, Paolo, Gasparini, Paolo, Mishra, Pashupati P., Sulem, Patrick, Magnusson, Patrik K. E., Elliott, Paul, Ridker, Paul M., Hamet, Pavel, Svensson, Per O., Joshi, Peter K., Kovacs, Peter, Pramstaller, Peter P., Rossing, Peter, Vollenweider, Peter, van der Harst, Pim, Dorajoo, Rajkumar, Sim, Ralene Z. H., Burkhardt, Ralph, Tao, Ran, Noordam, Raymond, Mägi, Reedik, Schmidt, Reinhold, de Mutsert, Renée, Rueedi, Rico, van Dam, Rob M., Carroll, Robert J., Gansevoort, Ron T., Loos, Ruth J. F., Felicita, Sala Cinzia, Sedaghat, Sanaz, Padmanabhan, Sandosh, Freitag-Wolf, Sandra, Pendergrass, Sarah A., Graham, Sarah E., Gordon, Scott D., Hwang, Shih-Jen, Kerr, Shona M., Vaccargiu, Simona, Patil, Snehal B., Hallan, Stein, Bakker, Stephan J. L., Lim, Su-Chi, Lucae, Susanne, Vogelezang, Suzanne, Bergmann, Sven, Corre, Tanguy, Ahluwalia, Tarunveer S., Lehtimäki, Terho, Boutin, Thibaud S., Meitinger, Thomas, Wong, Tien-Yin, Bergler, Tobias, Rabelink, Ton J., Esko, Tõnu, Haller, Toomas, Thorsteinsdottir, Unnur, Völker, Uwe, Foo, Valencia Hui Xian, Salomaa, Veikko, Vitart, Veronique, Giedraitis, Vilmantas, Gudnason, Vilmundur, Jaddoe, Vincent W. V., Huang, Wei, Zhang, Weihua, Wei, Wen Bin, Kiess, Wieland, März, Winfried, Koenig, Wolfgang, Lieb, Wolfgang, Gao, Xin, Sim, Xueling, Wang, Ya Xing, Friedlander, Yechiel, Tham, Yih-Chung, Kamatani, Yoichiro, Okada, Yukinori, Milaneschi, Yuri, Yu, Zhi, Hung, Adriana M., Stark, Klaus J., Stefansson, Kari, Böger, Carsten A., Kronenberg, Florian, Köttgen, Anna, Pattaro, Cristian, Heid, Iris M., Psychiatry, APH - Mental Health, Amsterdam Neuroscience - Complex Trait Genetics, Amsterdam Neuroscience - Mood, Anxiety, Psychosis, Stress & Sleep, APH - Digital Health, University of Helsinki, CAMM - Research Program for Clinical and Molecular Metabolism, Faculty of Medicine, Research Programs Unit, Tampere University, Clinical Medicine, TAYS Heart Centre, Department of Clinical Chemistry, Department of Clinical Physiology and Nuclear Medicine, Internal Medicine, Pediatrics, Epidemiology, Radiology & Nuclear Medicine, Erasmus MC other, Home Office, Imperial College Healthcare NHS Trust- BRC Funding, Medical Research Council (MRC), UK DRI Ltd, Interdisciplinary Centre Psychopathology and Emotion regulation (ICPE), Life Course Epidemiology (LCE), Groningen Institute for Organ Transplantation (GIOT), Groningen Kidney Center (GKC), Cardiovascular Centre (CVC), Winkler, Thomas W, Rasheed, Humaira, Teumer, Alexander, Gorski, Mathia, Rowan, Bryce X, Stanzick, Kira J, Thomas, Laurent F, Tin, Adrienne, Hoppmann, Anselm, Chu, Audrey Y, Tayo, Bamidele, Thio, Chris H L, Cusi, Daniele, Chai, Jin-Fang, Sieber, Karsten B, Horn, Katrin, Li, Man, Scholz, Marku, Cocca, Massimiliano, Wuttke, Matthia, van der Most, Peter J, Yang, Qiong, Ghasemi, Sahar, Nutile, Teresa, Li, Yong, Pontali, Giulia, Günther, Felix, Dehghan, Abba, Correa, Adolfo, Parsa, Afshin, Feresin, Agnese, de Vries, Aiko P J, Zonderman, Alan B, Smith, Albert V, Oldehinkel, Albertine J, De Grandi, Alessandro, Rosenkranz, Alexander R, Franke, Andre, Teren, Andrej, Metspalu, Andre, Hicks, Andrew A, Morris, Andrew P, Tönjes, Anke, Morgan, Anna, Podgornaia, Anna I, Peters, Annette, Körner, Antje, Mahajan, Anubha, Campbell, Archie, Freedman, Barry I, Spedicati, Beatrice, Ponte, Belen, Schöttker, Ben, Brumpton, Ben, Banas, Bernhard, Krämer, Bernhard K, Jung, Bettina, Åsvold, Bjørn Olav, Smith, Blair H, Ning, Boting, Penninx, Brenda W J H, Vanderwerff, Brett R, Psaty, Bruce M, Kammerer, Candace M, Langefeld, Carl D, Hayward, Caroline, Spracklen, Cassandra N, Robinson-Cohen, Cassianne, Hartman, Catharina A, Lindgren, Cecilia M, Wang, Chaolong, Sabanayagam, Charumathi, Heng, Chew-Kiat, Lanzani, Chiara, Khor, Chiea-Chuen, Cheng, Ching-Yu, Fuchsberger, Christian, Gieger, Christian, Shaffer, Christian M, Schulz, Christina-Alexandra, Willer, Cristen J, Chasman, Daniel I, Gudbjartsson, Daniel F, Ruggiero, Daniela, Toniolo, Daniela, Czamara, Darina, Porteous, David J, Waterworth, Dawn M, Mascalzoni, Deborah, Mook-Kanamori, Dennis O, Reilly, Dermot F, Daw, E Warwick, Hofer, Edith, Boerwinkle, Eric, Salvi, Erika, Bottinger, Erwin P, Tai, E-Shyong, Catamo, Eulalia, Rizzi, Federica, Guo, Feng, Rivadeneira, Fernando, Guilianini, Franco, Sveinbjornsson, Gardar, Ehret, Georg, Waeber, Gerard, Biino, Ginevra, Girotto, Giorgia, Pistis, Giorgio, Nadkarni, Girish N, Delgado, Graciela E, Montgomery, Grant W, Snieder, Harold, Campbell, Harry, White, Harvey D, Gao, He, Stringham, Heather M, Schmidt, Helena, Li, Hengtong, Brenner, Hermann, Holm, Hilma, Kirsten, Holgen, Kramer, Holly, Rudan, Igor, Nolte, Ilja M, Tzoulaki, Ioanna, Olafsson, Isleifur, Martins, Jade, Cook, James P, Wilson, James F, Halbritter, Jan, Felix, Janine F, Divers, Jasmin, Kooner, Jaspal S, Lee, Jeannette Jen-Mai, O'Connell, Jeffrey, Rotter, Jerome I, Liu, Jianjun, Xu, Jie, Thiery, Joachim, Ärnlöv, Johan, Kuusisto, Johanna, Jakobsdottir, Johanna, Tremblay, Johanne, Chambers, John C, Whitfield, John B, Gaziano, John M, Marten, Jonathan, Coresh, Josef, Jonas, Jost B, Mychaleckyj, Josyf C, Christensen, Kaare, Eckardt, Kai-Uwe, Mohlke, Karen L, Endlich, Karlhan, Dittrich, Katalin, Ryan, Kathleen A, Rice, Kenneth M, Taylor, Kent D, Ho, Kevin, Nikus, Kjell, Matsuda, Koichi, Strauch, Konstantin, Miliku, Kozeta, Hveem, Kristian, Lind, Lar, Wallentin, Lar, Yerges-Armstrong, Laura M, Raffield, Laura M, Phillips, Lawrence S, Launer, Lenore J, Lyytikäinen, Leo-Pekka, Lange, Leslie A, Citterio, Lorena, Klaric, Lucija, Ikram, M Arfan, Ising, Marcu, Kleber, Marcus E, Francescatto, Margherita, Concas, Maria Pina, Ciullo, Marina, Piratsu, Mario, Orho-Melander, Marju, Laakso, Markku, Loeffler, Marku, Perola, Marku, de Borst, Martin H, Gögele, Martin, Bianca, Martina La, Lukas, Mary Ann, Feitosa, Mary F, Biggs, Mary L, Wojczynski, Mary K, Kavousi, Maryam, Kanai, Masahiro, Akiyama, Masato, Yasuda, Masayuki, Nauck, Matthia, Waldenberger, Melanie, Chee, Miao-Li, Chee, Miao-Ling, Boehnke, Michael, Preuss, Michael H, Stumvoll, Michael, Province, Michael A, Evans, Michele K, O'Donoghue, Michelle L, Kubo, Michiaki, Kähönen, Mika, Kastarinen, Mika, Nalls, Mike A, Kuokkanen, Mikko, Ghanbari, Mohsen, Bochud, Murielle, Josyula, Navya Shilpa, Martin, Nicholas G, Tan, Nicholas Y Q, Palmer, Nicholette D, Pirastu, Nicola, Schupf, Nicole, Verweij, Niek, Hutri-Kähönen, Nina, Mononen, Nina, Bansal, Nisha, Devuyst, Olivier, Melander, Olle, Raitakari, Olli T, Polasek, Ozren, Manunta, Paolo, Gasparini, Paolo, Mishra, Pashupati P, Sulem, Patrick, Magnusson, Patrik K E, Elliott, Paul, Ridker, Paul M, Hamet, Pavel, Svensson, Per O, Joshi, Peter K, Kovacs, Peter, Pramstaller, Peter P, Rossing, Peter, Vollenweider, Peter, van der Harst, Pim, Dorajoo, Rajkumar, Sim, Ralene Z H, Burkhardt, Ralph, Tao, Ran, Noordam, Raymond, Mägi, Reedik, Schmidt, Reinhold, de Mutsert, Renée, Rueedi, Rico, van Dam, Rob M, Carroll, Robert J, Gansevoort, Ron T, Loos, Ruth J F, Felicita, Sala Cinzia, Sedaghat, Sanaz, Padmanabhan, Sandosh, Freitag-Wolf, Sandra, Pendergrass, Sarah A, Graham, Sarah E, Gordon, Scott D, Hwang, Shih-Jen, Kerr, Shona M, Vaccargiu, Simona, Patil, Snehal B, Hallan, Stein, Bakker, Stephan J L, Lim, Su-Chi, Lucae, Susanne, Vogelezang, Suzanne, Bergmann, Sven, Corre, Tanguy, Ahluwalia, Tarunveer S, Lehtimäki, Terho, Boutin, Thibaud S, Meitinger, Thoma, Wong, Tien-Yin, Bergler, Tobia, Rabelink, Ton J, Esko, Tõnu, Haller, Tooma, Thorsteinsdottir, Unnur, Völker, Uwe, Foo, Valencia Hui Xian, Salomaa, Veikko, Vitart, Veronique, Giedraitis, Vilmanta, Gudnason, Vilmundur, Jaddoe, Vincent W V, Huang, Wei, Zhang, Weihua, Wei, Wen Bin, Kiess, Wieland, März, Winfried, Koenig, Wolfgang, Lieb, Wolfgang, Gao, Xin, Sim, Xueling, Wang, Ya Xing, Friedlander, Yechiel, Tham, Yih-Chung, Kamatani, Yoichiro, Okada, Yukinori, Milaneschi, Yuri, Yu, Zhi, Stark, Klaus J, Stefansson, Kari, Böger, Carsten A, Hung, Adriana M, Kronenberg, Florian, Köttgen, Anna, Pattaro, Cristian, Heid, Iris M, and Lee Kong Chian School of Medicine (LKCMedicine)
Subjects: Life Sciences & Biomedicine - Other Topics, EXPRESSION, Diabetic Nephropathies/genetics, 610 Medizin, LOCI, Medicine (miscellaneous), EFFICIENT, Lifelines cohort study, Kidney, General Biochemistry, Genetics and Molecular Biology, DISEASE, QUALITY-CONTROL, SDG 3 - Good Health and Well-being, Diabetic Nephropathy, Diabetes Mellitus, Humans, Medicine [Science], Diabetic Nephropathies, GENOME-WIDE ASSOCIATION, Biology, DiscovEHR/MyCode study, METAANALYSIS, Glomerular Filtration Rate/genetics, Medicinsk genetik, ddc:610, Science & Technology, genetic, effects, kidney, diabetic, JOINT, Klinisk medicin, Diabetes Mellitu, 3126 Surgery, anesthesiology, intensive care, radiology, Multidisciplinary Sciences, ENVIRONMENT INTERACTION, Creatinine, VA Million Veteran Program, Science & Technology - Other Topics, 3111 Biomedicine, Clinical Medicine, SMOKING, General Agricultural and Biological Sciences, Life Sciences & Biomedicine, Medical Genetics, Human, Genome-Wide Association Study, Glomerular Filtration Rate
Abstract: Reduced glomerular filtration rate (GFR) can progress to kidney failure. Risk factors include genetics and diabetes mellitus (DM), but little is known about their interaction. We conducted genome-wide association meta-analyses for estimated GFR based on serum creatinine (eGFR), separately for individuals with or without DM (nDM = 178,691, nnoDM = 1,296,113). Our genome-wide searches identified (i) seven eGFR loci with significant DM/noDM-difference, (ii) four additional novel loci with suggestive difference and (iii) 28 further novel loci (including CUBN) by allowing for potential difference. GWAS on eGFR among DM individuals identified 2 known and 27 potentially responsible loci for diabetic kidney disease. Gene prioritization highlighted 18 genes that may inform reno-protective drug development. We highlight the existence of DM-only and noDM-only effects, which can inform about the target group, if respective genes are advanced as drug targets. Largely shared effects suggest that most drug interventions to alter eGFR should be effective in DM and noDM. Published version The Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) supported the meta-analysis—Project-ID 387509280—SFB1350 (Subproject C6 to I.M.H.). A.M.H., B.R., and R.T. were supported by VACSR&D MVP grant CX001897. This research is based on data from the Million Veteran Program, Office of Research and Development, Veterans Health Administration, and was supported by VACSR&D MVP grant CX001897 (A.M.H.). This publication does not represent the views of the Department of Veteran Affairs or the United States Government. We conducted this research using the UK Biobank resource under the application number 20272.
Published: 2022
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2. SMC-Derived Hyaluronan Modulates Vascular SMC Phenotype in Murine Atherosclerosis

Author: Katherine Owsiany, Daniel J. Gorski, Gary K. Owens, Susanne Homann, Vlad Serbulea, Jens W. Fischer, Felicia Hartmann, Anne Petz, Rebecca A. Deaton, Michelle P. Bendeck, Alexandra A. C. Newman, and Yu-Qing Zhou
Subjects: Physiology, Galectin 3, Myocytes, Smooth Muscle, Phenotypic switching, Article, Muscle, Smooth, Vascular, Extracellular matrix, Mice, Gene expression, medicine, Animals, Hyaluronic Acid, Receptor, biology, Chemistry, Fibrous cap, Phenotype, Actins, Plaque, Atherosclerotic, Cell biology, Mice, Inbred C57BL, Hyaluronan Receptors, medicine.anatomical_structure, Galectin-3, biology.protein, Collagen, ACTA2, Cardiology and Cardiovascular Medicine, Hyaluronan Synthases, Gene Deletion
Abstract: Rationale: Plaque instability remains poorly understood and new therapeutic approaches to reduce plaque rupture and subsequent clinical events are of great interest. Recent studies revealed an important role of phenotypic switching of smooth muscle cells (SMC) in controlling plaque stability, including ECM (extracellular matrix) deposition. Objective: The aim of this study was to elucidate the role of hyaluronan derived from SMC–hyaluronan synthase 3 ( Has3 ), in phenotypic switching and plaque stability in an animal model of atherosclerosis. Methods and Results: A mouse line with SMC-specific deletion of Has3 and simultaneous SMC-lineage tracing ( e YFP [enhanced yellow fluorescent protein]) on an Apoe −/− background was used. Lineage tracing of SMC with e YFP revealed that SMC-specific deletion of Has3 significantly increased the number of LGALS3 + (galectin-3) transition state SMC and decreased ACTA2 + (alpha-smooth muscle actin) SMC. Notably, SMC- Has3 deletion led to significantly increased collagen deposition and maturation within the fibrous cap and the whole lesion, as evidenced by picrosirius red staining and LC-PolScope analysis. Single-cell RNA sequencing of brachiocephalic artery lesions demonstrated that the loss of SMC- Has3 enhanced the transition of SMC to a Lgals3 + , ECM-producing phenotype with elevated acute-phase response gene expression. Experiments using cultured murine aortic SMC revealed that blocking CD44 (cluster of differentiation-44), an important hyaluronan binding receptor, recapitulated the enhanced acute-phase response, and synthesis of fibrous ECM. Conclusions: These studies provide evidence that the deletion of SMC- Has3 results in an ECM-producing transition state SMC phenotype (characterized by LGALS3 + expression), likely via reduced CD44 signaling, resulting in increased collagen formation and maturation, an index consistent with increased plaque stability.
Published: 2021
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3. Geographical variation in pace-of-life in a long-distance migratory bird: implications for population management

Author: A Gorski, Aurélien Besnard, Laimonas Sniauksta, Orsolya Kiss, Teresa Catry, Jesús M. Avilés, Deseada Parejo, Milda Šniaukštienė, Edmunds Račinskis, Timothée Schwartz, Inês Catry, and Otto Szekeres
Subjects: Avian clutch size, Reproductive success, Ecology, Range (biology), media_common.quotation_subject, Tropics, Biology, biology.organism_classification, Latitude, Life history theory, Coracias garrulus, Reproduction, Ecology, Evolution, Behavior and Systematics, media_common
Abstract: Life-history theory predicts that animals should develop adaptive trade-offs between survival and reproduction to maximize their fitness. This results in a continuum of life-history strategies among species, ranging from slow to fast paces-of-life. The optimal pace-of-life has been shown to vary within environmental gradients, with a commonly observed pattern of a slow-to-fast continuum from the tropics to the poles. Within species, pace-of-life variability has however received much less attention. In this study, we investigated whether or not the pace-of-life of populations within a species follows the expected slow–fast continuum associated with latitude. We analysed the variability of life-history strategies among populations of the European roller Coracias garrulus, a long-distance migratory species, comparing breeding parameters and adult survival between populations across a latitudinal gradient. The findings showed a negative correlation between survival and clutch size in roller populations, with a slower pace-of-life in the northern populations and a faster pace-of-life in the southern populations: a reverse gradient to what might be expected from inter-specific studies. These results suggest that northern populations would benefit from measures enhancing adult survival probability, such as reduction in harvesting rates, while southern populations would respond better to actions favouring reproductive success, such as nesting site provisioning. This study highlights that life-history traits can vary substantially between populations of a single species with a large latitudinal breeding range, and pinpoint how knowledge about this variability may be key in anticipating different populations’ responses to threats as well as to conservation strategies.
Published: 2021
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4. The Use of Simulated Patients Is more Effective than Student Role Playing in Fostering Patient-Centred Attitudes during Communication Skills Training: A Mixed Method Study

Author: Stanislaw Gorski, Anna Prokop-Dorner, Michal Pers, Agata Stalmach-Przygoda, Łukasz Malecki, Grzegorz Cebula, and Katrien Bombeke
Subjects: General Immunology and Microbiology, Article Subject, General Medicine, Human medicine, Biology, General Biochemistry, Genetics and Molecular Biology
Abstract: Objective. While simulated patients (SPs) are considered a standard tool in communication skills training, there is no evidence thus far of their comparative benefit to the more cost-effective option of student role playing. We compared the effectiveness of both approaches in developing patient-centred attitudes in students. Methods. We retrospectively compared students who participated in the clinical communication course (CCC), based on student role playing (CCCsp-, n = 160 ), to students who participated in the CCC with SPs (CCCsp+, n = 146 ), and students with no formal CCC (CCC-, n = 122 ). We used validated questionnaires to assess patient centredness. We also conducted focus group interviews (FGI) to better understand the impact of CCC with sp. Results. Students after the CCC with simulated patients achieved a significantly higher score in the patient-practitioner orientation scale than other groups ( p < 0.001 ). Conclusions. There is a strong positive correlation between the implementation of simulated patients and patient-centred attitudes among students. Data from the FGI revealed that students perceived training with SP as more realistic, safe, and engaging than student role playing. Practice Implications. Our research provides evidence to justify costs and resources invested in simulated patient programs.
Published: 2022

5. Discovery and prioritization of variants and genes for kidney function in >1.2 million individuals

Author: John Michael Gaziano, Snehal Patil, Cassiane Robinson-Cohen, Thomas W. Winkler, Humaira Rasheed, Anna Köttgen, Christopher J. O'Donnell, Sarah E. Graham, Stein Hallan, Brett R Vanderweff, Kira J Stanzick, Cristian Pattaro, Matthias Wuttke, Bjørn Olav Åsvold, Iris M. Heid, Adriana M. Hung, Bryce X Rowan, Pascal Schlosser, Klaus Stark, VA Million Veteran Program, Cristen J. Willer, André Gessner, Yong Li, Mathias Gorski, and Laurent F. Thomas
Subjects: 0301 basic medicine, Science, Quantitative Trait Loci, 610 Medizin, General Physics and Astronomy, Renal function, Genome-wide association study, RNA-Seq, Computational biology, Biology, Quantitative trait locus, Kidney, Genome-wide association studies, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, 0302 clinical medicine, Risk Factors, Chronic kidney disease, Genetics research, Databases, Genetic, medicine, Humans, Genetic Predisposition to Disease, Renal Insufficiency, Chronic, Gene, Genetic association, ddc:610, Multidisciplinary, Kidney metabolism, General Chemistry, medicine.disease, Cystatins, Europe, 030104 developmental biology, Gene Expression Regulation, Organ Specificity, Creatinine, Single-Cell Analysis, Biomarkers, 030217 neurology & neurosurgery, Genome-Wide Association Study, Glomerular Filtration Rate, Kidney disease
Abstract: Genes underneath signals from genome-wide association studies (GWAS) for kidney function are promising targets for functional studies, but prioritizing variants and genes is challenging. By GWAS meta-analysis for creatinine-based estimated glomerular filtration rate (eGFR) from the Chronic Kidney Disease Genetics Consortium and UK Biobank (n = 1,201,909), we expand the number of eGFRcrea loci (424 loci, 201 novel; 9.8% eGFRcrea variance explained by 634 independent signal variants). Our increased sample size in fine-mapping (n = 1,004,040, European) more than doubles the number of signals with resolved fine-mapping (99% credible sets down to 1 variant for 44 signals, ≤5 variants for 138 signals). Cystatin-based eGFR and/or blood urea nitrogen association support 348 loci (n = 460,826 and 852,678, respectively). Our customizable tool for Gene PrioritiSation reveals 23 compelling genes including mechanistic insights and enables navigation through genes and variants likely relevant for kidney function in human to help select targets for experimental follow-up., Identifying causal variants and genes in genome-wide association studies remains a challenge, an issue that is ameliorated with larger sample sizes. Here the authors meta-analyze kidney function genome-wide association studies to identify new loci and fine-map loci to home in on variants and genes involved in kidney function.
Published: 2021

6. Janus-faced EPHB4-associated disorders: novel pathogenic variants and unreported intrafamilial overlapping phenotypes

Author: Noeline Nadarajah, Mark D. Kilby, Maja Hempel, Stephanie E. Vallee, Silvia Martin-Almedina, Rhiannon Mellis, Dionysios Grigoriadis, Sarah Robart, Sahar Mansour, Mary Beth Dinulos, Ege Sackey, Giles Atton, Wolf-Henning Becker, Christina Karapouliou, Kazim Ogmen, Fanny Kortuem, Katherine S. Josephs, Gunnar Houge, Cathrine Ebbing, Pia Ostergaard, Kristiana Gordon, Steve Jeffery, Peter S. Mortimer, Jerome L. Gorski, Axel von der Wense, Alexandra Robinson, Cassandra Polun, Siren Berland, Jenny Lord, Hallvard Reigstad, and Sherri J. Bale
Subjects: 0301 basic medicine, Genetics, Hydrops Fetalis, Receptor, EphB4, Correction, Biology, Subcellular localization, Phenotype, Article, Human genetics, Pathogenesis, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, Lymphatic system, Humans, Ephrin, Functional studies, Phosphorylation, Receptor, Genetic Association Studies, 030217 neurology & neurosurgery, Genetics (clinical)
Abstract: PurposeSeveral clinical phenotypes including fetal hydrops, central conducting lymphatic anomaly or capillary malformations with arteriovenous malformations 2 (CM-AVM2) have been associated with EPHB4 (Ephrin type B receptor 4) variants, demanding new approaches for deciphering pathogenesis of novel variants of uncertain significance (VUS) identified in EPHB4, and for the identification of differentiated disease mechanisms at the molecular level.MethodsTen index cases with various phenotypes, either fetal hydrops, CM-AVM2, or peripheral lower limb lymphedema, whose distinct clinical phenotypes are described in detail in this study, presented with a variant in EPHB4. In vitro functional studies were performed to confirm pathogenicity.ResultsPathogenicity was demonstrated for six of the seven novel EPHB4 VUS investigated. A heterogeneity of molecular disease mechanisms was identified, from loss of protein production or aberrant subcellular localization to total reduction of the phosphorylation capability of the receptor. There was some phenotype–genotype correlation; however, previously unreported intrafamilial overlapping phenotypes such as lymphatic-related fetal hydrops (LRFH) and CM-AVM2 in the same family were observed.ConclusionThis study highlights the usefulness of protein expression and subcellular localization studies to predict EPHB4 variant pathogenesis. Our accurate clinical phenotyping expands our interpretation of the Janus-faced spectrum of EPHB4-related disorders, introducing the discovery of cases with overlapping phenotypes.
Published: 2021
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7. Role of the GLUT1 Glucose Transporter in Postnatal CNS Angiogenesis and Blood-Brain Barrier Integrity

Author: Cindy Casteels, Tatiane Gorski, E. Dale Abel, Paola Gilardoni, Koen Van Laere, Melissa García-Caballero, Johanna Schaffenrath, Zheng Fan, Koen Veys, Joanna Kalucka, Annika Keller, Nadine V. Conchinha, Moheb Ghobrial, Gino De Smet, Thomas Wälchli, Peter Carmeliet, Anna Rita Cantelmo, Aline Seuwen, Sarah-Maria Fendt, Aileen Schroeter, Ann Bouché, Felix Schlegel, Katrien De Bock, Kim Vriens, Raphaela Ardicoglu, Melissa Crabbé, Ilse Julia Smolders, University of Zurich, Pharmaceutical and Pharmacological Sciences, Alliance for Modulation in Epilepsy, Experimental Pharmacology, and Pathologic Biochemistry and Physiology
Subjects: 0301 basic medicine, HOMEOSTASIS, Physiology, Angiogenesis, AMP-Activated Protein Kinases, Glucose transport, Endothelium, Metabolism, Blood-brain barrier, Vascular biology, Mice, 0302 clinical medicine, Cell Movement, homeostasis, Glycolysis, Original Research, Glucose Transporter Type 1, biology, Chemistry, Brain, glycolysis, 3. Good health, Cell biology, medicine.anatomical_structure, ComputingMethodologies_DOCUMENTANDTEXTPROCESSING, Cardiology and Cardiovascular Medicine, endothelium, Neuroscience(all), extracellular matrix, Neovascularization, Physiologic, 610 Medicine & health, Blood–brain barrier, Retina, 10180 Clinic for Neurosurgery, 03 medical and health sciences, medicine, Animals, Humans, Cell Proliferation, Glucose transporter, Endothelial Cells, Retinal Vessels, glucose transport, blood-brain barrier, Glucose, 030104 developmental biology, biology.protein, GLUT1, Endothelium, Vascular, Energy Metabolism, 030217 neurology & neurosurgery, Homeostasis
Abstract: Supplemental Digital Content is available in the text., Rationale: Endothelial cells (ECs) are highly glycolytic and generate the majority of their energy via the breakdown of glucose to lactate. At the same time, a main role of ECs is to allow the transport of glucose to the surrounding tissues. GLUT1 (glucose transporter isoform 1/Slc2a1) is highly expressed in ECs of the central nervous system (CNS) and is often implicated in blood-brain barrier (BBB) dysfunction, but whether and how GLUT1 controls EC metabolism and function is poorly understood. Objective: We evaluated the role of GLUT1 in endothelial metabolism and function during postnatal CNS development as well as at the adult BBB. Methods and Results: Inhibition of GLUT1 decreases EC glucose uptake and glycolysis, leading to energy depletion and the activation of the cellular energy sensor AMPK (AMP-activated protein kinase), and decreases EC proliferation without affecting migration. Deletion of GLUT1 from the developing postnatal retinal endothelium reduces retinal EC proliferation and lowers vascular outgrowth, without affecting the number of tip cells. In contrast, in the brain, we observed a lower number of tip cells in addition to reduced brain EC proliferation, indicating that within the CNS, organotypic differences in EC metabolism exist. Interestingly, when ECs become quiescent, endothelial glycolysis is repressed, and GLUT1 expression increases in a Notch-dependent fashion. GLUT1 deletion from quiescent adult ECs leads to severe seizures, accompanied by neuronal loss and CNS inflammation. Strikingly, this does not coincide with BBB leakiness, altered expression of genes crucial for BBB barrier functioning nor reduced vascular function. Instead, we found a selective activation of inflammatory and extracellular matrix related gene sets. Conclusions: GLUT1 is the main glucose transporter in ECs and becomes uncoupled from glycolysis during quiescence in a Notch-dependent manner. It is crucial for developmental CNS angiogenesis and adult CNS homeostasis but does not affect BBB barrier function.
Published: 2020
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8. Puncta intended: connecting the dots between autophagy and cell stress networks

Author: Emily Leung, Xiaoyan Jiang, Sharon M. Gorski, Cally J Ho, Gayathri Samarasekera, Michelle Chan, Jing Xu, Kevin C. Yang, and Katharina Rothe
Subjects: Proteomics, 0301 basic medicine, Proteome, Reticulophagy, Autophagy-Related Proteins, Meeting Report, 03 medical and health sciences, Stress granule, Sequestosome 1, Stress, Physiological, Autophagy, Animals, Humans, Disease, Integrin-linked kinase, EIF2AK3, education, Molecular Biology, Mechanistic target of rapamycin, education.field_of_study, 030102 biochemistry & molecular biology, biology, Cell Biology, Cell biology, 030104 developmental biology, biology.protein, EIF2S1
Abstract: Proteome profiling and global protein-interaction approaches have significantly improved our knowledge of the protein interactomes of autophagy and other cellular stress-response pathways. New discoveries regarding protein complexes, interaction partners, interaction domains, and biological roles of players that are part of these pathways are emerging. The fourth Vancouver Autophagy Symposium showcased research that expands our understanding of the protein interaction networks and molecular mechanisms underlying autophagy and other cellular stress responses in the context of distinct stressors. In the keynote presentation, Dr. Wade Harper described his team’s recent discovery of a novel reticulophagy receptor for selective autophagic degradation of the endoplasmic reticulum, and discussed molecular mechanisms involved in ribophagy and non-autophagic ribosomal turnover. In other presentations, both omic and targeted approaches were used to reveal molecular players of other cellular stress responses including amyloid body and stress granule formation, anastasis, and extracellular vesicle biogenesis. Additional topics included the roles of autophagy in disease pathogenesis, autophagy regulatory mechanisms, and crosstalk between autophagy and cellular metabolism in anti-tumor immunity. The relationship between autophagy and other cell stress responses remains a relatively unexplored area in the field, with future investigations required to understand how the various processes are coordinated and connected in cells and tissues. Abbreviations: A-bodies: amyloid bodies; ACM: amyloid-converting motif; AMFR/gp78: autocrine motility factor receptor; ATG: autophagy-related; ATG4B: autophagy related 4B cysteine peptidase; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; CAR T: chimeric antigen receptor T; CASP3: caspase 3; CCPG1: cell cycle progression 1; CAR: chimeric antigen receptor; CML: chronic myeloid leukemia; CCOCs: clear cell ovarian cancers; CVB3: coxsackievirus B3; CRISPR-Cas9: clustered regularly interspaced short palindromic repeats-CRISPR associated protein 9; DDXs: DEAD-box helicases; EIF2S1/EIF-2alpha: eukaryotic translation initiation factor 2 subunit alpha; EIF2AK3: eukaryotic translation initiation factor 2 alpha kinase 3; ER: endoplasmic reticulum; EV: extracellular vesicle; FAO: fatty acid oxidation; GABARAP: GABA type A receptor-associated protein; ILK: integrin linked kinase; ISR: integrated stress response; MTOR: mechanistic target of rapamycin kinase; MPECs: memory precursory effector T cells; MAVS: mitochondrial antiviral signaling protein; NBR1: NBR1 autophagy cargo receptor; PI4KB/PI4KIIIβ: phosphatidylinositol 4-kinase beta; PLEKHM1: pleckstrin homology and RUN domain containing M1; RB1CC1: RB1 inducible coiled-coil 1; RTN3: reticulon 3; rIGSRNAs: ribosomal intergenic noncoding RNAs; RPL29: ribosomal protein L29; RPS3: ribosomal protein S3; S. cerevisiae: Saccharomyces cerevisiae; sEV: small extracellular vesicles; S. pombe: Schizosaccharomyces pombe; SQSTM1: sequestosome 1; SF3B1: splicing factor 3b subunit 1; SILAC-MS: stable isotope labeling with amino acids in cell culture-mass spectrometry; SNAP29: synaptosome associated protein 29; TEX264: testis expressed 264, ER-phagy receptor; TNBC: triple-negative breast cancer; ULK1: unc-51 like autophagy activating kinase 1; VAS: Vancouver Autophagy Symposium
Published: 2020
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9. Basic Biology of Extracellular Matrix in the Cardiovascular System, Part 1/4

Author: Richard P. Harvey, Daniel J. Gorski, Jason C. Kovacic, Gonzalo del Monte-Nieto, and Jens W. Fischer
Subjects: Extracellular matrix, 03 medical and health sciences, 0302 clinical medicine, 030212 general & internal medicine, 030204 cardiovascular system & hematology, Matrix (biology), Biology, Cardiology and Cardiovascular Medicine, Proteomics, Neuroscience
Abstract: Highlights •The ECM is the noncellular component of tissues throughout the body and is formed of filamentous proteins, proteoglycans, and glycosaminoglycans, which extensively interact and whose structure and dynamics are modified by cross-linking. •Whereas historically ECM was thought to be static, thereby providing the “mortar” for cells, on the contrary, it is now recognized that the ECM is highly dynamic during development and in response to physiologic and pathophysiologic stimuli, conferring very specific signaling and mechanical functions. •By leveraging novel tools such as scRNAseq and high-throughput proteomics, it is anticipated that a great deal more remains to be discovered, which may lead to future novel therapeutic opportunities.
Published: 2020
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10. Differential and shared genetic effects on kidney function between diabetic and non-diabetic individuals

Author: Winkler, Thomas W, Rasheed, Humaira, Teumer, Alexander, Gorski, Mathias, Rowan, Bryce X, Stanzick, Kira J, Thomas, Laurent F, Tin, Adrienne, Hoppmann, Anselm, Chu, Audrey Y, Tayo, Bamidele, Thio, Chris H L, Cusi, Daniele, Chai, Jin-Fang, Sieber, Karsten B, Horn, Katrin, Li, Man, Scholz, Markus, Cocca, Massimiliano, Wuttke, Matthias, van der Most, Peter J, Yang, Qiong, Ghasemi, Sahar, Nutile, Teresa, Li, Yong, Pontali, Giulia, Günther, Felix, Dehghan, Abbas, Correa, Adolfo, Parsa, Afshin, et al, University of Zurich, and Winkler, Thomas W
Subjects: 1300 General Biochemistry, Genetics and Molecular Biology, 570 Life sciences, biology, 610 Medicine & health, 2701 Medicine (miscellaneous), 1100 General Agricultural and Biological Sciences, 10052 Institute of Physiology
Published: 2022
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11. The structure of the Physcomitrium Patens Photosystem I Reveals a Unique Lhca2 Paralogue replacing Lhca4

Author: C. Gorski, Dewight Williams, R. Riddle, Z. Dobson, Yuval Mazor, H. Toporik, and Z. Da
Subjects: Cyanobacteria, Chlorophyll b, biology, Lineage (evolution), Physcomitrium, Plant Science, biology.organism_classification, Photosystem I, Photosynthesis, Light-harvesting complex, chemistry.chemical_compound, chemistry, Botany, Green algae
Abstract: The moss Physcomitrium patens diverged from green algae shortly after the colonization of land by ancient plants. This colonization posed new environmental challenges which drove evolutionary processes. The photosynthetic machinery of modern flowering plants is adapted to the high light conditions on land. Red shifted Lhca4 antennae are present in the photosystem I light harvesting complex of many green lineage plants but absent from P. patens. The Cryo-EM structure of the P. patens photosystem I light harvesting complex I supercomplex (PSI-LHCI) at 2.8 Å reveals that Lhca4 is replaced by a unique Lhca2 paralogue in moss. This PSI-LHCI supercomplex also retains the PsaM subunit, present in cyanobacteria and several algal species but lost in higher plants, and the PsaO subunit responsible for binding light harvesting complex II. The blue shifted Lhca2 paralogue and chlorophyll b enrichment relative to higher plants make the P. patens PSI-LHCI spectroscopically unique among other green lineage supercomplexes. Overall, the structure represents an evolutionary intermediate PSI with the crescent shaped LHCI common in higher plants and contains a unique Lhca2 paralogue which facilitates the mosses adaptation to low light niches.
Published: 2021
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12. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Author: Klionsky, Daniel, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis, Adeli, Khosrow, Adolph, Timon, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed, Agrotis, Alexander, Aguilar, Patricia, Ahmad, S Tariq, Ahmed, Zubair, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay, Alberti, Simon, Alcocer-Gómez, Elísabet, Alessandri, Cristiano, Ali, Muhammad, Alim Al-Bari, M Abdul, Aliwaini, Saeb, Alizadeh, Javad, Almacellas, Eugènia, Almasan, Alexandru, Alonso, Alicia, Alonso, Guillermo, Altan-Bonnet, Nihal, Altieri, Dario, Álvarez, Élida, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal, Ammanathan, Veena, An, Zhenyi, Andersen, Stig, Andrabi, Shaida, Andrade-Silva, Magaiver, Andres, Allen, Angelini, Sabrina, Ann, David, Anozie, Uche, Ansari, Mohammad, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas, Au, Alicia, Auberger, Patrick, Auner, Holger, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, Yucel, Ayton, Scott, Ayyadevara, Srinivas, Azzopardi, Maria, Baba, Misuzu, Backer, Jonathan, Backues, Steven, Bae, Dong-Hun, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric, Baek, Ahruem, Baek, Seung-Hoon, Baek, Sung Hee, Bagetta, Giacinto, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xiyuan, Bai, Yidong, Bairagi, Nandadulal, Baksi, Shounak, Balbi, Teresa, Baldari, Cosima, Balduini, Walter, Ballabio, Andrea, Ballester, Maria, Balazadeh, Salma, Balzan, Rena, Bandopadhyay, Rina, Banerjee, Sreeparna, Banerjee, Sulagna, Bánréti, Ágnes, Bao, Yan, Baptista, Mauricio, Baracca, Alessandra, Barbati, Cristiana, Bargiela, Ariadna, Barilà, Daniela, Barlow, Peter, Barmada, Sami, Barreiro, Esther, Barreto, George, Bartek, Jiri, Bartel, Bonnie, Bartolome, Alberto, Barve, Gaurav, Basagoudanavar, Suresh, Bassham, Diane, Bast, Robert, Basu, Alakananda, Batoko, Henri, Batten, Isabella, Baulieu, Etienne, Baumgarner, Bradley, Bayry, Jagadeesh, Beale, Rupert, Beau, Isabelle, Beaumatin, Florian, Bechara, Luiz, Beck, George, Beers, Michael, Begun, Jakob, Behrends, Christian, Behrens, Georg, Bei, Roberto, Bejarano, Eloy, Bel, Shai, Behl, Christian, Belaid, Amine, Belgareh-Touzé, Naïma, Bellarosa, Cristina, Belleudi, Francesca, Belló Pérez, Melissa, Bello-Morales, Raquel, Beltran, Jackeline Soares de Oliveira, Beltran, Sebastián, Benbrook, Doris Mangiaracina, Bendorius, Mykolas, Benitez, Bruno, Benito-Cuesta, Irene, Bensalem, Julien, Berchtold, Martin, Berezowska, Sabina, Bergamaschi, Daniele, Bergami, Matteo, Bergmann, Andreas, Berliocchi, Laura, Berlioz-Torrent, Clarisse, Bernard, Amélie, Berthoux, Lionel, Besirli, Cagri, Besteiro, Sebastien, Betin, Virginie, Beyaert, Rudi, Bezbradica, Jelena, Bhaskar, Kiran, Bhatia-Kissova, Ingrid, Bhattacharya, Resham, Bhattacharya, Sujoy, Bhattacharyya, Shalmoli, Bhuiyan, Md Shenuarin, Bhutia, Sujit Kumar, Bi, Lanrong, Bi, Xiaolin, Biden, Trevor, Bijian, Krikor, Billes, Viktor, Binart, Nadine, Bincoletto, Claudia, Birgisdottir, Asa, Bjorkoy, Geir, Blanco, Gonzalo, Blas-Garcia, Ana, Blasiak, Janusz, Blomgran, Robert, Blomgren, Klas, Blum, Janice, Boada-Romero, Emilio, Boban, Mirta, Boesze-Battaglia, Kathleen, Boeuf, Philippe, Boland, Barry, Bomont, Pascale, Bonaldo, Paolo, Bonam, Srinivasa Reddy, Bonfili, Laura, Bonifacino, Juan, Boone, Brian, Bootman, Martin, Bordi, Matteo, Borner, Christoph, Bornhauser, Beat, Borthakur, Gautam, Bosch, Jürgen, Bose, Santanu, botana, luis, Botas, Juan, Boulanger, Chantal, Boulton, Michael, Bourdenx, Mathieu, Bourgeois, Benjamin, Bourke, Nollaig, Bousquet, Guilhem, Boya, Patricia, Bozhkov, Peter, Bozi, Luiz, Bozkurt, Tolga, Brackney, Doug, Brandts, Christian, Braun, Ralf, Braus, Gerhard, Bravo-Sagua, Roberto, Bravo-San Pedro, José, Brest, Patrick, Bringer, Marie-Agnès, Briones-Herrera, Alfredo, Broaddus, V Courtney, Brodersen, Peter, Brodsky, Jeffrey, Brody, Steven, Bronson, Paola, Bronstein, Jeff, Brown, Carolyn, Brown, Rhoderick, Brum, Patricia, Brumell, John, Brunetti-Pierri, Nicola, Bruno, Daniele, Bryson-Richardson, Robert, Bucci, Cecilia, Buchrieser, Carmen, Bueno, Marta, Buitrago-Molina, Laura Elisa, Buraschi, Simone, Buch, Shilpa, Buchan, J Ross, Buckingham, Erin, Budak, Hikmet, Budini, Mauricio, Bultynck, Geert, Burada, Florin, Burgoyne, Joseph, Burón, M Isabel, Bustos, Victor, Büttner, Sabrina, Butturini, Elena, Byrd, Aaron, Cabas, Isabel, Cabrera-Benitez, Sandra, Cadwell, Ken, Cai, Jingjing, Cai, Lu, Cai, Qian, Cairó, Montserrat, Calbet, Jose, Caldwell, Guy, Caldwell, Kim, Call, Jarrod, Calvani, Riccardo, Calvo, Ana, Calvo-Rubio Barrera, Miguel, Camara, Niels OS, Camonis, Jacques, Camougrand, Nadine, Campanella, Michelangelo, Campbell, Edward, Campbell-Valois, François-Xavier, Campello, Silvia, Campesi, Ilaria, Campos, Juliane, Camuzard, Olivier, Cancino, Jorge, Candido de Almeida, Danilo, Canesi, Laura, Caniggia, Isabella, Canonico, Barbara, Cantí, Carles, Cao, Bin, Caraglia, Michele, Caramés, Beatriz, Carchman, Evie, Cardenal-Muñoz, Elena, Cardenas, Cesar, Cardenas, Luis, Cardoso, Sandra, Carew, Jennifer, Carle, Georges, Carleton, Gillian, Carloni, Silvia, Carmona-Gutierrez, Didac, Carneiro, Leticia, Carnevali, Oliana, Carosi, Julian, Carra, Serena, Carrier, Alice, Carrier, Lucie, Carroll, Bernadette, Carter, A Brent, Carvalho, Andreia Neves, Casanova, Magali, Casas, Caty, Casas, Josefina, Cassioli, Chiara, Castillo, Eliseo, Castillo, Karen, Castillo-Lluva, Sonia, Castoldi, Francesca, Castori, Marco, Castro, Ariel, Castro-Caldas, Margarida, Castro-Hernandez, Javier, Castro-Obregon, Susana, Catz, Sergio, Cavadas, Claudia, Cavaliere, Federica, Cavallini, Gabriella, Cavinato, Maria, Cayuela, Maria, Cebollada Rica, Paula, Cecarini, Valentina, Cecconi, Francesco, Cechowska-Pasko, Marzanna, Cenci, Simone, Ceperuelo-Mallafré, Victòria, Cerqueira, João, Cerutti, Janete, Cervia, Davide, Cetintas, Vildan Bozok, Cetrullo, Silvia, Chae, Han-Jung, Chagin, Andrei, Chai, Chee-Yin, Chakrabarti, Gopal, Chakrabarti, Oishee, Chakraborty, Tapas, Chakraborty, Trinad, Chami, mounia, Chamilos, Georgios, Chan, David, Chan, Edmond, Chan, Edward, Chan, H.Y. Edwin, Chan, Helen, Chan, Hung, Chan, Matthew, Chan, Yau Sang, Chandra, Partha, Chang, Chih-Peng, Chang, Chunmei, Chang, Hao-Chun, Chang, Kai, Chao, Jie, Chapman, Tracey, Charlet-Berguerand, Nicolas, Chatterjee, Samrat, Chaube, Shail, Chaudhary, Anu, Chauhan, Santosh, Chaum, Edward, Checler, Frédéric, Cheetham, Michael, Chen, Chang-Shi, Chen, Guang-Chao, Chen, Jian-Fu, Chen, Liam, Chen, Leilei, Chen, Lin, Chen, Mingliang, Chen, Mu-Kuan, Chen, Ning, Chen, Quan, Chen, Ruey-Hwa, Chen, Shi, Chen, Wei, Chen, Weiqiang, Chen, Xin-Ming, Chen, Xiong-Wen, Chen, Xu, Chen, Yan, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Yue-Qin, Chen, Zhefan Stephen, Chen, Zhi, Chen, Zhi-Hua, Chen, Zhijian, Chen, Zhixiang, Cheng, Hanhua, Cheng, Jun, Cheng, Shi-Yuan, Cheng, Wei, Cheng, Xiaodong, Cheng, Xiu-Tang, Cheng, Yiyun, Cheng, Zhiyong, Chen, Zhong, Cheong, Heesun, Cheong, Jit Kong, Chernyak, Boris, Cherry, Sara, Cheung, Chi Fai Randy, Cheung, Chun Hei Antonio, Cheung, King-Ho, Chevet, Eric, Chi, Richard, Chiang, Alan Kwok Shing, Chiaradonna, Ferdinando, Chiarelli, Roberto, Chiariello, Mario, Chica, Nathalia, Chiocca, Susanna, Chiong, Mario, Chiou, Shih-Hwa, Chiramel, Abhilash, Chiurchiù, Valerio, Cho, Dong-Hyung, Choe, Seong-Kyu, Choi, Augustine, Choi, Mary, Choudhury, Kamalika Roy, Chow, Norman, Chu, Charleen, Chua, Jason, Chua, John Jia En, Chung, Hyewon, Chung, Kin Pan, Chung, Seockhoon, Chung, So-Hyang, Chung, Yuen-Li, Cianfanelli, Valentina, Ciechomska, Iwona, Cifuentes, Mariana, Cinque, Laura, Cirak, Sebahattin, Cirone, Mara, Clague, Michael, Clarke, Robert, Clementi, Emilio, Coccia, Eliana, Codogno, Patrice, Cohen, Ehud, Cohen, Mickael, Colasanti, Tania, Colasuonno, Fiorella, Colbert, Robert, Colell, Anna, Čolić, Miodrag, Coll, Nuria, Collins, Mark, Colombo, María, Colón-Ramos, Daniel, Combaret, Lydie, Comincini, Sergio, Cominetti, Márcia, Consiglio, Antonella, Conte, Andrea, Conti, Fabrizio, Contu, Viorica Raluca, Cookson, Mark, Coombs, Kevin, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corkery, Dale, Cordes, Nils, Cortese, Katia, Costa, Maria do Carmo, Costantino, Sarah, Costelli, Paola, Coto-Montes, Ana, Crack, Peter, Crespo, Jose, Criollo, Alfredo, Crippa, Valeria, Cristofani, Riccardo, Csizmadia, Tamas, Cuadrado, Antonio, Cui, Bing, Cui, Jun, Cui, Yixian, Cui, Yong, Culetto, Emmanuel, Cumino, Andrea, Cybulsky, Andrey, Czaja, Mark, Czuczwar, Stanislaw, D'Adamo, Stefania, D'Amelio, Marcello, D'Arcangelo, Daniela, D'Lugos, Andrew, D'Orazi, Gabriella, da Silva, James, Dafsari, Hormos Salimi, Dagda, Ruben, Dagdas, Yasin, Daglia, Maria, Dai, Xiaoxia, Dai, Yun, Dai, Yuyuan, Dal Col, Jessica, Dalhaimer, Paul, Dalla Valle, Luisa, Dallenga, Tobias, Dalmasso, Guillaume, Damme, Markus, Dando, Ilaria, Dantuma, Nico, Darling, April, Das, Hiranmoy, Dasarathy, Srinivasan, Dasari, Santosh, Dash, Srikanta, Daumke, Oliver, Dauphinee, Adrian, Davies, Jeffrey, Dávila, Valeria, Davis, Roger, Davis, Tanja, Dayalan Naidu, Sharadha, De Amicis, Francesca, De Bosscher, Karolien, De Felice, Francesca, De Franceschi, Lucia, De Leonibus, Chiara, de Mattos Barbosa, Mayara, De Meyer, Guido, De Milito, Angelo, De Nunzio, Cosimo, De Palma, Clara, De Santi, Mauro, De Virgilio, Claudio, De Zio, Daniela, Debnath, Jayanta, DeBosch, Brian, Decuypere, Jean-Paul, Deehan, Mark, Deflorian, Gianluca, DeGregori, James, Dehay, Benjamin, Del Rio, Gabriel, Delaney, Joe, Delbridge, Lea, Delorme-Axford, Elizabeth, Delpino, M Victoria, Demarchi, Francesca, Dembitz, Vilma, Demers, Nicholas, Deng, Hongbin, Deng, Zhiqiang, Dengjel, Joern, Dent, Paul, Denton, Donna, DePamphilis, Melvin, Der, Channing, Deretic, Vojo, Descoteaux, Albert, Devis, Laura, Devkota, Sushil, Devuyst, Olivier, Dewson, Grant, Dharmasivam, Mahendiran, Dhiman, Rohan, di Bernardo, Diego, Di Cristina, Manlio, Di Domenico, Fabio, Di Fazio, Pietro, Di Fonzo, Alessio, Di Guardo, Giovanni, Di Guglielmo, Gianni, Di Leo, Luca, Di Malta, Chiara, Di Nardo, Alessia, Di Rienzo, Martina, Di Sano, Federica, Diallinas, George, Diao, Jiajie, Diaz-Araya, Guillermo, Díaz-Laviada, Inés, Dickinson, Jared, Diederich, Marc, Dieudé, Mélanie, Dikic, Ivan, Ding, Shiping, Ding, Wen-Xing, Dini, Luciana, Dinić, Jelena, Dinic, Miroslav, Dinkova-Kostova, Albena, Dionne, Marc, Distler, Jörg, Diwan, Abhinav, Dixon, Ian, Djavaheri-Mergny, Mojgan, Dobrinski, Ina, Dobrovinskaya, Oxana, Dobrowolski, Radek, Dobson, Renwick, Đokić, Jelena, Dokmeci Emre, Serap, Donadelli, Massimo, Dong, Bo, Dong, Xiaonan, Dong, Zhiwu, Dorn Ii, Gerald, Dotsch, Volker, Dou, Huan, Dou, Juan, Dowaidar, Moataz, Dridi, Sami, Drucker, Liat, Du, Ailian, Du, Caigan, Du, Guangwei, Du, Hai-Ning, Du, Li-Lin, du Toit, André, Duan, Shao-Bin, Duan, Xiaoqiong, Duarte, Sónia, Dubrovska, Anna, Dunlop, Elaine, Dupont, Nicolas, Durán, Raúl, Dwarakanath, Bilikere, Dyshlovoy, Sergey, Ebrahimi-Fakhari, Darius, Eckhart, Leopold, Edelstein, Charles, Efferth, Thomas, Eftekharpour, Eftekhar, Eichinger, Ludwig, Eid, Nabil, Eisenberg, Tobias, Eissa, N Tony, Eissa, Sanaa, Ejarque, Miriam, El Andaloussi, Abdeljabar, El-Hage, Nazira, El-Naggar, Shahenda, Eleuteri, Anna Maria, El-Shafey, Eman, Elgendy, Mohamed, Eliopoulos, Aristides, Elizalde, María, Elks, Philip, Elsasser, Hans-Peter, Elsherbiny, Eslam, Emerling, Brooke, Emre, N., Eng, Christina, Engedal, Nikolai, Engelbrecht, Anna-Mart, Engelsen, Agnete, Enserink, Jorrit, Escalante, Ricardo, Esclatine, Audrey, Escobar-Henriques, Mafalda, Eskelinen, Eeva-Liisa, Espert, Lucile, Eusebio, Makandjou-Ola, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Facchiano, Francesco, Fadeel, Bengt, Fader, Claudio, Faesen, Alex, Fairlie, W Douglas, Falcó, Alberto, Falkenburger, Bjorn, Fan, Daping, Fan, Jie, Fan, Yanbo, Fang, Evandro, Fang, Yanshan, Fang, Yognqi, Fanto, Manolis, Farfel-Becker, Tamar, Faure, Mathias, Fazeli, Gholamreza, Fedele, Anthony, Feldman, Arthur, Feng, Du, Feng, Jiachun, Feng, Lifeng, Feng, Yibin, Feng, Yuchen, Feng, Wei, Fenz Araujo, Thais, Ferguson, Thomas, Fernández, Álvaro, Fernandez-Checa, Jose, Fernández-Veledo, Sonia, Fernie, Alisdair, Ferrante, Anthony, Ferraresi, Alessandra, Ferrari, Merari, Ferreira, Julio, Ferro-Novick, Susan, Figueras, Antonio, Filadi, Riccardo, Filigheddu, Nicoletta, Filippi-Chiela, Eduardo, Filomeni, Giuseppe, Fimia, Gian Maria, Fineschi, Vittorio, Finetti, Francesca, Finkbeiner, Steven, Fisher, Edward, Fisher, Paul, Flamigni, Flavio, Fliesler, Steven, Flo, Trude, Florance, Ida, Florey, Oliver, Florio, Tullio, Fodor, Erika, Follo, Carlo, Fon, Edward, Forlino, Antonella, Fornai, Francesco, Fortini, Paola, Fracassi, Anna, Fraldi, Alessandro, Franco, Brunella, Franco, Rodrigo, Franconi, Flavia, Frankel, Lisa, Friedman, Scott, Fröhlich, Leopold, Frühbeck, Gema, Fuentes, Jose, Fujiki, Yukio, Fujita, Naonobu, Fujiwara, Yuuki, Fukuda, Mitsunori, Fulda, Simone, Furic, Luc, Furuya, Norihiko, Fusco, Carmela, Gack, Michaela, Gaffke, Lidia, Galadari, Sehamuddin, Galasso, Alessia, Galindo, Maria, Gallolu Kankanamalage, Sachith, Galluzzi, Lorenzo, Galy, Vincent, Gammoh, Noor, Gan, Boyi, Ganley, Ian, Gao, Feng, Gao, Hui, Gao, Minghui, Gao, Ping, Gao, Shou-Jiang, Gao, Wentao, Gao, Xiaobo, Garcera, Ana, Garcia, Maria Noé, Garcia, Verónica, García-del Portillo, Francisco, Garcia-Escudero, Vega, Garcia-Garcia, Aracely, Garcia-Macia, Marina, García-Moreno, Diana, Garcia-Ruiz, Carmen, García-Sanz, Patricia, Garg, Abhishek, Gargini, Ricardo, Garofalo, Tina, Garry, Robert, Gassen, Nils, Gatica, Damian, Ge, Liang, Ge, Wanzhong, Geiss-Friedlander, Ruth, Gelfi, Cecilia, Genschik, Pascal, Gentle, Ian, Gerbino, Valeria, Gerhardt, Christoph, Germain, Kyla, Germain, Marc, Gewirtz, David, Ghasemipour Afshar, Elham, Ghavami, Saeid, Ghigo, Alessandra, Ghosh, Manosij, Giamas, Georgios, Giampietri, Claudia, Giatromanolaki, Alexandra, Gibson, Gary, Gibson, Spencer, Ginet, Vanessa, Giniger, Edward, Giorgi, Carlotta, Girao, Henrique, Girardin, Stephen, Giridharan, Mridhula, Giuliano, Sandy, Giulivi, Cecilia, Giuriato, Sylvie, Giustiniani, Julien, Gluschko, Alexander, Goder, Veit, Goginashvili, Alexander, Golab, Jakub, Goldstone, David, Golebiewska, Anna, Gomes, Luciana, Gomez, Rodrigo, Gómez-Sánchez, Rubén, Gomez-Puerto, Maria Catalina, Gomez-Sintes, Raquel, Gong, Qingqiu, Goni, Felix, González-Gallego, Javier, Gonzalez-Hernandez, Tomas, Gonzalez-Polo, Rosa, Gonzalez-Reyes, Jose, González-Rodríguez, Patricia, Goping, Ing Swie, Gorbatyuk, Marina, Gorbunov, Nikolai, Görgülü, Kıvanç, Gorojod, Roxana, Gorski, Sharon, Goruppi, Sandro, Gotor, Cecilia, Gottlieb, Roberta, Gozes, Illana, Gozuacik, Devrim, Graef, Martin, Gräler, Markus, Granatiero, Veronica, Grasso, Daniel, Gray, Joshua, Green, Douglas, Greenhough, Alexander, Gregory, Stephen, Griffin, Edward, Grinstaff, Mark, Gros, Frederic, Grose, Charles, Gross, Angelina, Gruber, Florian, Grumati, Paolo, Grune, Tilman, Gu, Xueyan, Guan, Jun-Lin, Guardia, Carlos, Guda, Kishore, Guerra, Flora, Guerri, Consuelo, Guha, Prasun, Guillén, Carlos, Gujar, Shashi, Gukovskaya, Anna, Gukovsky, Ilya, Gunst, Jan, Günther, Andreas, Guntur, Anyonya, Guo, Chuanyong, Guo, Chun, Guo, Hongqing, Guo, Lian-Wang, Guo, Ming, Gupta, Pawan, Gupta, Shashi Kumar, Gupta, Swapnil, Gupta, Veer Bala, Gupta, Vivek, Gustafsson, Asa, Gutterman, David, H B, Ranjitha, Haapasalo, Annakaisa, Haber, James, Hać, Aleksandra, Hadano, Shinji, Hafrén, Anders, Haidar, Mansour, Hall, Belinda, Halldén, Gunnel, Hamacher-Brady, Anne, Hamann, Andrea, Hamasaki, Maho, Han, Weidong, Hansen, Malene, Hanson, Phyllis, Hao, Zijian, Harada, Masaru, Harhaji-Trajkovic, Ljubica, Hariharan, Nirmala, Haroon, Nigil, Harris, James, Hasegawa, Takafumi, Hasima Nagoor, Noor, Haspel, Jeffrey, Haucke, Volker, Hawkins, Wayne, Hay, Bruce, Haynes, Cole, Hayrabedyan, Soren, Hays, Thomas, He, Congcong, He, Qin, He, Rong-Rong, He, You-Wen, He, Yu-Ying, Heakal, Yasser, Heberle, Alexander, Hejtmancik, J Fielding, Helgason, Gudmundur Vignir, Henkel, Vanessa, Herb, Marc, Hergovich, Alexander, Herman-Antosiewicz, Anna, Hernández, Agustín, Hernandez, Carlos, Hernandez-Diaz, Sergio, Hernandez-Gea, Virginia, Herpin, Amaury, Herreros, Judit, Hervás, Javier, Hesselson, Daniel, Hetz, Claudio, Heussler, Volker, Higuchi, Yujiro, Hilfiker, Sabine, Hill, Joseph, Hlavacek, William, Ho, Emmanuel, Ho, Idy, Ho, Philip Wing-Lok, Ho, Shu-Leong, Ho, Wan Yun, Hobbs, G Aaron, Hochstrasser, Mark, Hoet, Peter, Hofius, Daniel, Hofman, Paul, Höhn, Annika, Holmberg, Carina, Hombrebueno, Jose, Yi-Ren Hong, Chang-Won Hong, Hooper, Lora, Hoppe, Thorsten, Horos, Rastislav, Hoshida, Yujin, Hsin, I-Lun, Hsu, Hsin-Yun, Hu, Bing, Hu, Dong, Hu, Li-Fang, Hu, Ming Chang, Hu, Ronggui, Hu, Wei, Hu, Yu-Chen, Hu, Zhuo-Wei, Hua, Fang, Hua, Jinlian, Hua, Yingqi, Huan, Chongmin, Huang, Canhua, Huang, Chuanshu, Huang, Chuanxin, Huang, Chunling, Huang, Haishan, Huang, Kun, Huang, Michael, Huang, Rui, Huang, Shan, Huang, Tianzhi, Huang, Xing, Huang, Yuxiang Jack, Huber, Tobias, Hubert, Virginie, Hubner, Christian, Hughes, Stephanie, Hughes, William, Humbert, Magali, Hummer, Gerhard, Hurley, James, Hussain, Sabah, Hussain, Salik, Hussey, Patrick, Hutabarat, Martina, Hwang, Hui-Yun, Hwang, Seungmin, Ieni, Antonio, Ikeda, Fumiyo, Imagawa, Yusuke, Imai, Yuzuru, Imbriano, Carol, Imoto, Masaya, Inman, Denise, Inoki, Ken, Iovanna, Juan, Iozzo, Renato, Ippolito, Giuseppe, Irazoqui, Javier, Iribarren, Pablo, Ishaq, Mohd, ISHIKAWA, Makoto, Ishimwe, Nestor, Isidoro, Ciro, Ismail, Nahed, Issazadeh-Navikas, Shohreh, Itakura, Eisuke, Ito, Daisuke, Ivankovic, Davor, Ivanova, Saška, Iyer, Anand Krishnan V, Izquierdo, José, Izumi, Masanori, Jäättelä, Marja, Jabir, Majid Sakhi, Jackson, William, Jacobo-Herrera, Nadia, Jacomin, Anne-Claire, Jacquin, Elise, Jadiya, Pooja, Jaeschke, Hartmut, Jagannath, Chinnaswamy, Jakobi, Arjen, Jakobsson, Johan, Janji, Bassam, Jansen-Dürr, Pidder, Jansson, Patric, Jantsch, Jonathan, Januszewski, Sławomir, Jassey, Alagie, Jean, Steve, Jeltsch-David, Hélène, Jendelova, Pavla, Jenny, Andreas, Jensen, Thomas, Jessen, Niels, Jewell, Jenna, Ji, Jing, Jia, Lijun, Jia, Rui, Jiang, Liwen, Jiang, Qing, Jiang, Richeng, Jiang, Teng, Jiang, Xuejun, Jiang, Yu, Jimenez-Sanchez, Maria, Jin, Eun-Jung, Jin, Fengyan, Jin, Hongchuan, Jin, Li, Jin, Luqi, Jin, Meiyan, Jin, Si, Jo, Eun-Kyeong, Joffre, Carine, Johansen, Terje, Johnson, Gail, Johnston, Simon, Jokitalo, Eija, Jolly, Mohit Kumar, Joosten, Leo, Jordan, Joaquin, Joseph, Bertrand, Ju, Dianwen, Ju, Jeong-Sun, Ju, Jingfang, Juárez, Esmeralda, Judith, Delphine, Juhász, Gábor, Jun, Youngsoo, Jung, Chang Hwa, Jung, Sung-Chul, Jung, Yong Keun, Jungbluth, Heinz, Jungverdorben, Johannes, Just, Steffen, Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kaganovich, Daniel, Kahana, Alon, Kain, Renate, Kajimura, Shinjo, Kalamvoki, Maria, Kalia, Manjula, Kalinowski, Danuta, Kaludercic, Nina, Kalvari, Ioanna, Kaminska, Joanna, Kaminskyy, Vitaliy, Kanamori, Hiromitsu, Kanasaki, Keizo, Kang, Chanhee, Kang, Rui, Kang, Sang Sun, Kaniyappan, Senthilvelrajan, Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanthasamy, Anumantha, Kanthasamy, Arthi, Kantorow, Marc, Kapuy, Orsolya, Karamouzis, Michalis, Karim, Md Razaul, Karmakar, Parimal, Katare, Rajesh, Kato, Masaru, Kaufmann, Stefan, Kauppinen, Anu, Kaushal, Gur, Kaushik, Susmita, Kawasaki, Kiyoshi, Kazan, Kemal, Ke, Po-Yuan, Keating, Damien, Keber, Ursula, Kehrl, John, Keller, Kate, Keller, Christian, Kemper, Jongsook Kim, Kenific, Candia, Kepp, Oliver, Kermorgant, Stephanie, Kern, Andreas, Ketteler, Robin, Keulers, Tom, Khalfin, Boris, Khalil, Hany, Khambu, Bilon, Khan, Shahid, Khandelwal, Vinoth Kumar Megraj, Khandia, Rekha, Kho, Widuri, Khobrekar, Noopur, Khuansuwan, Sataree, Khundadze, Mukhran, Killackey, Samuel, Kim, Dasol, Kim, Deok Ryong, Kim, Do-Hyung, Kim, Dong-Eun, Kim, Eun Young, Kim, Eun-Kyoung, Kim, Hak-Rim, Kim, Hee-Sik, Kim, Hyung Ryong, Kim, Jeong Hun, Kim, Jin Kyung, Kim, Jin-Hoi, Kim, Joungmok, Kim, Ju Hwan, Kim, Keun Il, Kim, Peter, Kim, Seong-Jun, Kimball, Scot, Kimchi, Adi, Kimmelman, Alec, Kimura, Tomonori, King, Matthew, Kinghorn, Kerri, Kinsey, Conan, Kirkin, Vladimir, Kirshenbaum, Lorrie, Kiselev, Sergey, Kishi, Shuji, Kitamoto, Katsuhiko, Kitaoka, Yasushi, Kitazato, Kaio, Kitsis, Richard, Kittler, Josef, Kjaerulff, Ole, Klein, Peter, Klopstock, Thomas, Klucken, Jochen, Knævelsrud, Helene, Knorr, Roland, Ko, Ben, Ko, Fred, Ko, Jiunn-Liang, Kobayashi, Hotaka, Kobayashi, Satoru, Koch, Ina, Koch, Jan, Koenig, Ulrich, Kögel, Donat, Koh, Young Ho, Koike, Masato, Kohlwein, Sepp, Kocaturk, Nur, Komatsu, Masaaki, König, Jeannette, Kono, Toru, Kopp, Benjamin, Korcsmaros, Tamas, Korkmaz, Gözde, Korolchuk, Viktor, Korsnes, Mónica Suárez, Koskela, Ali, Kota, Janaiah, Kotake, Yaichiro, Kotler, Monica, Kou, Yanjun, Koukourakis, Michael, Koustas, Evangelos, Kovacs, Attila, Kovács, Tibor, Koya, Daisuke, Kozako, Tomohiro, Kraft, Claudine, Krainc, Dimitri, Krämer, Helmut, Krasnodembskaya, Anna, Kretz-Remy, Carole, Kroemer, Guido, Ktistakis, Nicholas, Kuchitsu, Kazuyuki, Kuenen, Sabine, Kuerschner, Lars, Kukar, Thomas, Kumar, Ajay, Kumar, Ashok, Kumar, Deepak, Kumar, Dhiraj, Kumar, Sharad, Kume, Shinji, Kumsta, Caroline, Kundu, Chanakya, Kundu, Mondira, Kunnumakkara, Ajaikumar, Kurgan, Lukasz, Kutateladze, Tatiana, Kutlu, Ozlem, Kwak, SeongAe, Kwon, Ho Jeong, Kwon, Taeg Kyu, Kwon, Yong Tae, Kyrmizi, Irene, La Spada, Albert, Labonté, Patrick, Ladoire, Sylvain, Laface, Ilaria, Lafont, Frank, Lagace, Diane, Lahiri, Vikramjit, Lai, Zhibing, Laird, Angela, Lakkaraju, Aparna, Lamark, Trond, Lan, Sheng-Hui, Landajuela, Ane, Lane, Darius, Lane, Jon, Lang, Charles, Lange, Carsten, Langel, Ülo, Langer, Rupert, Lapaquette, Pierre, Laporte, Jocelyn, LaRusso, Nicholas, Lastres-Becker, Isabel, Lau, Wilson Chun Yu, Laurie, Gordon, Lavandero, Sergio, Law, Betty Yuen Kwan, Law, Helen Ka-wai, Layfield, Rob, Le, Weidong, Le Stunff, Herve, Leary, Alexandre, Lebrun, Jean-Jacques, Leck, Lionel, Leduc-Gaudet, Jean-Philippe, Lee, Changwook, Lee, Chung-Pei, Lee, Da-Hye, Lee, Edward, Lee, Erinna, Lee, Gyun Min, Lee, He-Jin, Lee, Heung Kyu, Lee, Jae Man, Lee, Jason, Lee, Jin-A, Lee, Joo-Yong, Lee, Jun Hee, Lee, Michael, Lee, Min Goo, Lee, Min Jae, Lee, Myung-Shik, Lee, Sang Yoon, Lee, Seung-Jae, Lee, Stella, Lee, Sung Bae, Lee, Won Hee, Lee, Ying-Ray, Lee, Yong-ho, Lee, Youngil, Lefebvre, Christophe, Legouis, Renaud, Lei, Yu, Lei, Yuchen, Leikin, Sergey, Leitinger, Gerd, Lemus, Leticia, Leng, Shuilong, Lenoir, Olivia, Lenz, Guido, Lenz, Heinz Josef, Lenzi, Paola, León, Yolanda, Leopoldino, Andréia, Leschczyk, Christoph, Leskelä, Stina, Letellier, Elisabeth, Leung, Chi-Ting, Leung, Po Sing, Leventhal, Jeremy, Levine, Beth, Lewis, Patrick, Ley, Klaus, Li, Bin, Li, Da-Qiang, Li, Jianming, Li, Jing, Li, Jiong, Li, Ke, Li, Liwu, Li, Mei, Li, Min, Li, Ming, Li, Mingchuan, Li, Pin-Lan, Li, Ming-Qing, Li, Qing, Li, Sheng, Li, Tiangang, Li, Wei, Li, Wenming, Li, Xue, Li, Yi-Ping, Li, Yuan, Li, Zhiqiang, Li, Zhiyong, Li, Zhiyuan, Lian, Jiqin, Liang, Chengyu, Liang, Qiangrong, Liang, Weicheng, Liang, Yongheng, Liang, YongTian, Liao, Guanghong, Liao, Lujian, Liao, Mingzhi, Liao, Yung-Feng, Librizzi, Mariangela, Lie, Pearl, Lilly, Mary, Lim, Hyunjung, Lima, Thania, Limana, Federica, Lin, Chao, Lin, Chih-Wen, Lin, Dar-Shong, Lin, Fu-Cheng, Lin, Jiandie, Lin, Kurt, Lin, Kwang-Huei, Lin, Liang-Tzung, LIN, Pei-Hui, Lin, Qiong, Lin, Shaofeng, Lin, Su-Ju, Lin, Wenyu, Lin, Xueying, Lin, Yao-Xin, Lin, Yee-Shin, Linden, Rafael, Lindner, Paula, Ling, Shuo-Chien, Lingor, Paul, Linnemann, Amelia, Liou, Yih-Cherng, Lipinski, Marta, Lipovšek, Saška, Lira, Vitor, Lisiak, Natalia, Liton, Paloma, Liu, Chao, Liu, Ching-Hsuan, Liu, Chun-Feng, Liu, Cui Hua, Liu, Fang, Liu, Hao, Liu, Hsiao-Sheng, Liu, Hua-feng, Liu, Huifang, Liu, Jia, Liu, Jing, Liu, Julia, Liu, Leyuan, Liu, Longhua, Liu, Meilian, Liu, Qin, Liu, Wei, Liu, Wende, Liu, Xiao-Hong, Liu, Xiaodong, Liu, Xingguo, Liu, Xu, Liu, Xuedong, Liu, Yanfen, Liu, Yang, Liu, Yueyang, Liu, Yule, Livingston, J Andrew, Lizard, Gerard, Lizcano, Jose, Ljubojevic-Holzer, Senka, LLeonart, Matilde, Llobet-Navàs, David, Llorente, Alicia, Lo, Chih Hung, Lobato-Márquez, Damián, Long, Qi, Long, Yun Chau, Loos, Ben, Loos, Julia, López, Manuela, López-Doménech, Guillermo, López-Guerrero, José Antonio, López-Jiménez, Ana, López-Pérez, Óscar, López-Valero, Israel, Lorenowicz, Magdalena, Lorente, Mar, Lorincz, Peter, Lossi, Laura, Lotersztajn, Sophie, Lovat, Penny, Lovell, Jonathan, Lovy, Alenka, Lőw, Péter, Lu, Guang, Lu, Haocheng, Lu, Jia-Hong, Lu, Jin-Jian, Lu, Mengji, Lu, Shuyan, Luciani, Alessandro, Lucocq, John, Ludovico, Paula, Luftig, Micah, Luhr, Morten, Luis-Ravelo, Diego, Lum, Julian, Luna-Dulcey, Liany, Lund, Anders, Lund, Viktor, Lünemann, Jan, Lüningschrör, Patrick, Luo, Honglin, Luo, Rongcan, Luo, Shouqing, Luo, Zhi, Luparello, Claudio, Lüscher, Bernhard, Luu, Luan, Lyakhovich, Alex, Lyamzaev, Konstantin, Lystad, Alf Håkon, Lytvynchuk, Lyubomyr, Ma, Alvin, Ma, Changle, Ma, Mengxiao, Ma, Ning-Fang, Ma, Quan-Hong, Ma, Xinliang, Ma, Yueyun, Ma, Zhenyi, MacDougald, Ormond, Macian, Fernando, MacIntosh, Gustavo, MacKeigan, Jeffrey, Macleod, Kay, Maday, Sandra, Madeo, Frank, Madesh, Muniswamy, Madl, Tobias, Madrigal-Matute, Julio, Maeda, Akiko, Maejima, Yasuhiro, Magarinos, Marta, Mahavadi, Poornima, Maiani, Emiliano, Maiese, Kenneth, Maiti, Panchanan, Maiuri, Maria Chiara, Majello, Barbara, Major, Michael, Makareeva, Elena, Malik, Fayaz, Mallilankaraman, Karthik, Malorni, Walter, Maloyan, Alina, Mammadova, Najiba, Man, Gene Chi Wai, Manai, Federico, Mancias, Joseph, Mandelkow, Eva-Maria, Mandell, Michael, Manfredi, Angelo, Manjili, Masoud, Manjithaya, Ravi, Manque, Patricio, Manshian, Bella, Manzano, Raquel, Manzoni, Claudia, Mao, Kai, Marchese, Cinzia, Marchetti, Sandrine, Marconi, Anna Maria, Marcucci, Fabrizio, Mardente, Stefania, Mareninova, Olga, Margeta, Marta, Mari, Muriel, Marinelli, Sara, Marinelli, Oliviero, Mariño, Guillermo, Mariotto, Sofia, Marshall, Richard, Marten, Mark, Martens, Sascha, Martin, Alexandre, Martin, Katie, Martin, Sara, Martin, Shaun, Martín-Segura, Adrián, Martín-Acebes, Miguel, Martin-Burriel, Inmaculada, Martin-Rincon, Marcos, Martin-Sanz, Paloma, Martina, José, Martinet, Wim, Martinez, Aitor, Martinez, Ana, Martinez, Jennifer, Martinez Velazquez, Moises, Martinez-Lopez, Nuria, Martinez-Vicente, Marta, Martins, Daniel, Martins, Joilson, Martins, Waleska, Martins-Marques, Tania, Marzetti, Emanuele, Masaldan, Shashank, Masclaux-Daubresse, Celine, Mashek, Douglas, Massa, Valentina, Massieu, Lourdes, Masson, Glenn, Masuelli, Laura, Masyuk, Anatoliy, Masyuk, Tetyana, Matarrese, Paola, Matheu, Ander, Matoba, Satoaki, Matsuzaki, Sachiko, Mattar, Pamela, Matte, Alessandro, Mattoscio, Domenico, Mauriz, José, Mauthe, Mario, Mauvezin, Caroline, Maverakis, Emanual, Maycotte, Paola, Mayer, Johanna, Mazzoccoli, Gianluigi, Mazzoni, Cristina, Mazzulli, Joseph, McCarty, Nami, Mcdonald, Christine, McGill, Mitchell, McKenna, Sharon, Mclaughlin, Bethann, McLoughlin, Fionn, McNiven, Mark, McWilliams, Thomas, Mechta-Grigoriou, Fatima, Medeiros, Tania Catarina, Medina, Diego, Megeney, Lynn, Megyeri, Klara, Mehrpour, Maryam, Mehta, Jawahar, Meijer, Alfred, Meijer, Annemarie, Mejlvang, Jakob, Meléndez, Alicia, Melk, Annette, Memisoglu, Gonen, Mendes, Alexandrina, Meng, Delong, Meng, Fei, Meng, Tian, Menna-Barreto, Rubem, Menon, Manoj, Mercer, Carol, Mercier, Anne, MERGNY, Jean-Louis, Merighi, Adalberto, Merkley, Seth, Merla, Giuseppe, Meske, Volker, Mestre, Ana Cecilia, Metur, Shree Padma, Meyer, Christian, Meyer, Hemmo, Mi, Wenyi, Mialet-Perez, Jeanne, Miao, Junying, Micale, Lucia, Miki, Yasuo, Milan, Enrico, Milczarek, Małgorzata, Miller, Dana, Miller, Samuel, Miller, Silke, Millward, Steven, Milosevic, Ira, Minina, Elena, Mirzaei, Hamed, Mirzaei, Hamid Reza, Mirzaei, Mehdi, Mishra, Amit, Mishra, Nandita, Mishra, Paras Kumar, Misirkic Marjanovic, Maja, Misasi, Roberta, Misra, Amit, Misso, Gabriella, Mitchell, Claire, Mitou, Geraldine, Miura, Tetsuji, Miyamoto, Shigeki, MIYAZAKI, Makoto, Miyazaki, Mitsunori, Miyazaki, Taiga, Miyazawa, Keisuke, Mizushima, Noboru, Mogensen, Trine, Mograbi, Baharia, Mohammadinejad, Reza, Mohamud, Yasir, Mohanty, Abhishek, Mohapatra, Sipra, Möhlmann, Torsten, Mohmmed, Asif, Moles, Anna, Moley, Kelle, Molinari, Maurizio, Mollace, Vincenzo, Møller, Andreas Buch, Mollereau, Bertrand, Mollinedo, Faustino, Montagna, Costanza, Monteiro, Mervyn, Montella, Andrea, Montes, L Ruth, Montico, Barbara, Mony, Vinod, Monzio Compagnoni, Giacomo, Moore, Michael, Moosavi, Mohammad, Mora, Ana, Mora, Marina, Morales-Alamo, David, Moratalla, Rosario, Moreira, Paula, Morelli, Elena, Moreno, Sandra, Moreno-Blas, Daniel, Moresi, Viviana, Morga, Benjamin, Morgan, Alwena, Morin, Fabrice, Morishita, Hideaki, Moritz, Orson, Moriyama, Mariko, Moriyasu, Yuji, Morleo, Manuela, Morselli, Eugenia, Moruno-Manchon, Jose, Moscat, Jorge, Mostowy, Serge, Motori, Elisa, Moura, Andrea Felinto, Moustaid-Moussa, Naima, Mrakovcic, Maria, Muciño-Hernández, Gabriel, Mukherjee, Anupam, Mukhopadhyay, Subhadip, Mulcahy Levy, Jean, Mulero, Victoriano, Muller, Sylviane, Münch, Christian, Munjal, Ashok, Munoz-Canoves, Pura, Muñoz-Galdeano, Teresa, Münz, Christian, Murakawa, Tomokazu, Muratori, Claudia, Murphy, Brona, Murphy, J Patrick, Murthy, Aditya, Myöhänen, Timo, Mysorekar, Indira, Mytych, Jennifer, Nabavi, Seyed Mohammad, Nabissi, Massimo, Nagy, Péter, Nah, Jihoon, Nahimana, Aimable, Nakagawa, Ichiro, Nakamura, Ken, Nakatogawa, Hitoshi, Nandi, Shyam, Nanjundan, Meera, Nanni, Monica, Napolitano, Gennaro, Nardacci, Roberta, Narita, Masashi, Nassif, Melissa, Nathan, Ilana, Natsumeda, Manabu, Naude, Ryno, Naumann, Christin, Naveiras, Olaia, Navid, Fatemeh, Nawrocki, Steffan, Nazarko, Taras, Nazio, Francesca, Negoita, Florentina, Neill, Thomas, Neisch, Amanda, Neri, Luca, Netea, Mihai, Neubert, Patrick, Neufeld, Thomas, Neumann, Dietbert, Neutzner, Albert, Newton, Phillip, Ney, Paul, Nezis, Ioannis, Ng, Charlene, Ng, Tzi Bun, Nguyen, Hang, Nguyen, Long, Ni, Hong-Min, Ní Cheallaigh, Clíona, Ni, Zhenhong, Nicolao, M Celeste, Nicoli, Francesco, Nieto-Diaz, Manuel, Nilsson, Per, Ning, Shunbin, Niranjan, Rituraj, Nishimune, Hiroshi, Niso-Santano, Mireia, Nixon, Ralph, Nobili, Annalisa, Nobrega, Clevio, Noda, Takeshi, Nogueira-Recalde, Uxía, Nolan, Trevor, Nombela, Ivan, Novak, Ivana, Novoa, Beatriz, Nozawa, Takashi, Nukina, Nobuyuki, Nussbaum-Krammer, Carmen, Nylandsted, Jesper, O'Donovan, Tracey, O'Leary, Seónadh, O'Rourke, Eyleen, O'Sullivan, Mary, O'Sullivan, Timothy, Oddo, Salvatore, Oehme, Ina, Ogawa, Michinaga, Ogier-Denis, Eric, Ogmundsdottir, Margret, Ogretmen, Besim, Oh, Goo Taeg, Oh, Seon-Hee, Oh, Young, Ohama, Takashi, Ohashi, Yohei, Ohmuraya, Masaki, Oikonomou, Vasileios, Ojha, Rani, Okamoto, Koji, Okazawa, Hitoshi, Oku, Masahide, Oliván, Sara, Oliveira, Jorge, Ollmann, Michael, Olzmann, James, Omari, Shakib, Omary, M Bishr, Önal, Gizem, Ondrej, Martin, Ong, Sang-Bing, Ong, Sang-Ging, Onnis, Anna, Orellana, Juan, Orellana-Muñoz, Sara, Ortega-Villaizan, Maria Del Mar, Ortiz-Gonzalez, Xilma, Ortona, Elena, Osiewacz, Heinz, Osman, Abdel-Hamid, Osta, Rosario, Otegui, Marisa, Otsu, Kinya, Ott, Christiane, Ottobrini, Luisa, Ou, Jing-Hsiung James, Outeiro, Tiago, Oynebraten, Inger, Ozturk, Melek, Pagès, Gilles, Pahari, Susanta, Pajares, Marta, Pajvani, Utpal, Pal, Rituraj, Paladino, Simona, Pallet, Nicolas, Palmieri, Michela, Palmisano, Giuseppe, Palumbo, Camilla, Pampaloni, Francesco, Pan, Lifeng, Pan, Qingjun, Pan, Wenliang, Pan, Xin, Panasyuk, Ganna, Pandey, Rahul, Pandey, Udai, Pandya, Vrajesh, Paneni, Francesco, Pang, Shirley, Panzarini, Elisa, Papademetrio, Daniela, Papaleo, Elena, Papinski, Daniel, Papp, Diana, Park, Eun Chan, Park, Hwan Tae, Park, Ji-Man, Park, Jong-In, Park, Joon Tae, Park, Junsoo, Park, Sang Chul, Park, Sang-Youel, Parola, Abraham, Parys, Jan, Pasquier, Adrien, Pasquier, Benoit, Passos, João, Pastore, Nunzia, Patel, Hemal, Patschan, Daniel, Pattingre, Sophie, Pedraza-Alva, Gustavo, Pedraza-Chaverri, Jose, Pedrozo, Zully, Pei, Gang, Pei, Jianming, Peled-Zehavi, Hadas, Pellegrini, Joaquín, Pelletier, Joffrey, Peñalva, Miguel, Peng, Di, Peng, Ying, Penna, Fabio, Pennuto, Maria, Pentimalli, Francesca, Pereira, Cláudia MF, Pereira, Gustavo, Pereira, Lilian, Pereira de Almeida, Luis, Perera, Nirma, Pérez-Lara, Ángel, Perez-Oliva, Ana, Pérez-Pérez, María Esther, Periyasamy, Palsamy, Perl, Andras, Perrotta, Cristiana, Perrotta, Ida, Pestell, Richard, Petersen, Morten, Petrache, Irina, Petrovski, Goran, Pfirrmann, Thorsten, Pfister, Astrid, Philips, Jennifer, Pi, Huifeng, Picca, Anna, Pickrell, Alicia, Picot, Sandy, Pierantoni, Giovanna, Pierdominici, Marina, Pierre, Philippe, Pierrefite-Carle, Valérie, Pierzynowska, Karolina, Pietrocola, Federico, Pietruczuk, Miroslawa, Pignata, Claudio, Pimentel-Muiños, Felipe, Pinar, Mario, Pinheiro, Roberta, Pinkas-Kramarski, Ronit, Pinton, Paolo, Pircs, Karolina, Piya, Sujan, Pizzo, Paola, Plantinga, Theo, Platta, Harald, Plaza-Zabala, Ainhoa, Plomann, Markus, Plotnikov, Egor, Plun-Favreau, Helene, Pluta, Ryszard, Pocock, Roger, Pöggeler, Stefanie, Pohl, Christian, Poirot, Marc, Poletti, Angelo, Ponpuak, Marisa, Popelka, Hana, Popova, Blagovesta, Porta, Helena, Porte Alcon, Soledad, Portilla-Fernandez, Eliana, Post, Martin, Potts, Malia, Poulton, Joanna, Powers, Ted, Prahlad, Veena, Prajsnar, Tomasz, Praticò, Domenico, Prencipe, Rosaria, Priault, Muriel, Proikas-Cezanne, Tassula, Promponas, Vasilis, Proud, Christopher, Puertollano, Rosa, Puglielli, Luigi, Pulinilkunnil, Thomas, Puri, Deepika, Puri, Rajat, Puyal, Julien, Qi, Xiaopeng, Qi, Yongmei, Qian, Wenbin, Qiang, Lei, Qiu, Yu, Quadrilatero, Joe, Quarleri, Jorge, Raben, Nina, Rabinowich, Hannah, Ragona, Debora, Ragusa, Michael, Rahimi, Nader, Rahmati, Marveh, Raia, Valeria, Raimundo, Nuno, Rajasekaran, Namakkal-Soorappan, Ramachandra Rao, Sriganesh, Rami, Abdelhaq, Ramírez-Pardo, Ignacio, Ramsden, David, Randow, Felix, Rangarajan, Pundi, Ranieri, Danilo, Rao, Hai, Rao, Lang, Rao, Rekha, Rathore, Sumit, Ratnayaka, J Arjuna, Ratovitski, Edward, Ravanan, Palaniyandi, Ravegnini, Gloria, Ray, Swapan, Razani, Babak, Rebecca, Vito, Reggiori, Fulvio, Régnier-Vigouroux, Anne, Reichert, Andreas, Reigada, David, Reiling, Jan, Rein, Theo, Reipert, Siegfried, Rekha, Rokeya Sultana, Ren, Hongmei, Ren, Jun, Ren, Weichao, Renault, Tristan, Renga, Giorgia, Reue, Karen, Rewitz, Kim, Ribeiro de Andrade Ramos, Bruna, Riazuddin, S Amer, Ribeiro-Rodrigues, Teresa, Ricci, Jean-Ehrland, Ricci, Romeo, Riccio, Victoria, Richardson, Des, Rikihisa, Yasuko, Risbud, Makarand, Risueño, Ruth, Ritis, Konstantinos, Rizza, Salvatore, Rizzuto, Rosario, Roberts, Helen, Roberts, Luke, Robinson, Katherine, Roccheri, Maria Carmela, Rocchi, Stephane, Rodney, George, Rodrigues, Tiago, Rodrigues Silva, Vagner Ramon, Rodriguez, Amaia, Rodriguez-Barrueco, Ruth, Rodriguez-Henche, Nieves, Rodriguez-Rocha, Humberto, Roelofs, Jeroen, Rogers, Robert, Rogov, Vladimir, ROJO, Ana, Rolka, Krzysztof, Romanello, Vanina, Romani, Luigina, Romano, Alessandra, Romano, Patricia, Romeo-Guitart, David, Romero, Luis, Romero, Montserrat, Roney, Joseph, Rongo, Christopher, Roperto, Sante, Rosenfeldt, Mathias, Rosenstiel, Philip, Rosenwald, Anne, Roth, Kevin, Roth, Lynn, Roth, Steven, Rouschop, Kasper, Roussel, Benoit, Roux, Sophie, Rovere-Querini, Patrizia, Roy, Ajit, Rozieres, Aurore, Ruano, Diego, Rubinsztein, David, Rubtsova, Maria, Ruckdeschel, Klaus, Ruckenstuhl, Christoph, Rudolf, Emil, Rudolf, Rüdiger, Ruggieri, Alessandra, Ruparelia, Avnika Ashok, Rusmini, Paola, Russell, Ryan, Russo, Gian Luigi, Russo, Maria, Russo, Rossella, Ryabaya, Oxana, Ryan, Kevin, Ryu, Kwon-Yul, Sabater-Arcis, Maria, Sachdev, Ulka, Sacher, Michael, Sachse, Carsten, Sadhu, Abhishek, Sadoshima, Junichi, Safren, Nathaniel, Saftig, Paul, Sagona, Antonia, Sahay, Gaurav, Sahebkar, Amirhossein, Sahin, Mustafa, Sahin, Ozgur, Sahni, Sumit, Saito, Nayuta, Saito, Shigeru, Saito, Tsunenori, Sakai, Ryohei, Sakai, Yasuyoshi, Sakamaki, Jun-Ichi, Saksela, Kalle, Salazar, Gloria, Salazar-Degracia, Anna, Salekdeh, Ghasem, Saluja, Ashok, Sampaio-Marques, Belém, Sanchez, Maria Cecilia, Sanchez-Alcazar, Jose, Sanchez-Vera, Victoria, Sancho-Shimizu, Vanessa, Sanderson, J Thomas, Sandri, Marco, Santaguida, Stefano, Santambrogio, Laura, Santana, Magda, Santoni, Giorgio, Sanz, Alberto, Sanz, Pascual, Saran, Shweta, Sardiello, Marco, Sargeant, Timothy, Sarin, Apurva, Sarkar, Chinmoy, Sarkar, Sovan, Sarrias, Maria-Rosa, Sarkar, Surajit, Sarmah, Dipanka Tanu, Sarparanta, Jaakko, Sathyanarayan, Aishwarya, Sathyanarayanan, Ranganayaki, Scaglione, K Matthew, Scatozza, Francesca, Schaefer, Liliana, Schafer, Zachary, Schaible, Ulrich, Schapira, Anthony, Scharl, Michael, Schatzl, Hermann, Schein, Catherine, Scheper, Wiep, Scheuring, David, Schiaffino, Maria Vittoria, Schiappacassi, Monica, Schindl, Rainer, Schlattner, Uwe, Schmidt, Oliver, Schmitt, Roland, Schmidt, Stephen, Schmitz, Ingo, Schmukler, Eran, Schneider, Anja, Schneider, Bianca, Schober, Romana, Schoijet, Alejandra, Schott, Micah, Schramm, Michael, Schröder, Bernd, Schuh, Kai, Schüller, Christoph, Schulze, Ryan, Schürmanns, Lea, Schwamborn, Jens, Schwarten, Melanie, Scialo, Filippo, Sciarretta, Sebastiano, Scott, Melanie, Scotto, Kathleen, Scovassi, A Ivana, Scrima, Andrea, Scrivo, Aurora, Sebastian, David, Sebti, Salwa, Sedej, Simon, Segatori, Laura, Segev, Nava, Seglen, Per, Seiliez, Iban, Seki, Ekihiro, Selleck, Scott, Sellke, Frank, Selsby, Joshua, Sendtner, Michael, Senturk, Serif, Seranova, Elena, Sergi, Consolato, Serra-Moreno, Ruth, Sesaki, Hiromi, Settembre, Carmine, Setty, Subba Rao Gangi, Sgarbi, Gianluca, Sha, Ou, Shacka, John, Shah, Javeed, Shang, Dantong, Shao, Changshun, Shao, Feng, Sharbati, Soroush, Sharkey, Lisa, Sharma, Dipali, Sharma, Gaurav, Sharma, Kulbhushan, Sharma, Pawan, Sharma, Surendra, Shen, Han-Ming, Shen, Hongtao, Shen, Jiangang, Shen, Ming, Shen, Weili, Shen, Zheni, Sheng, Rui, Sheng, Zhi, Sheng, Zu-Hang, Shi, Jianjian, Shi, Xiaobing, Shi, Ying-Hong, Shiba-Fukushima, Kahori, Shieh, Jeng-Jer, Shimada, Yohta, Shimizu, Shigeomi, Shimozawa, Makoto, Shintani, Takahiro, Shoemaker, Christopher, Shojaei, Shahla, Shoji, Ikuo, Shravage, Bhupendra, Shridhar, Viji, Shu, Chih-Wen, Shu, Hong-Bing, Shui, Ke, Shukla, Arvind, Shutt, Timothy, Sica, Valentina, Siddiqui, Aleem, Sierra, Amanda, Sierra-Torre, Virginia, Signorelli, Santiago, Sil, Payel, Silva, Bruno, Silva, Johnatas, Silva-Pavez, Eduardo, Silvente-Poirot, Sandrine, Simmonds, Rachel, Simon, Anna Katharina, Simon, Hans-Uwe, Simons, Matias, Singh, Anurag, Singh, Lalit, Singh, Rajat, Singh, Shivendra, Singh, Shrawan, Singh, Sudha, Singh, Sunaina, Singh, Surinder Pal, Sinha, Debasish, Sinha, Rohit Anthony, Sinha, Sangita, Sirko, Agnieszka, Sirohi, Kapil, Sivridis, Efthimios, Skendros, Panagiotis, Skirycz, Aleksandra, Slaninová, Iva, Smaili, Soraya, Smertenko, Andrei, Smith, Matthew, Soenen, Stefaan, Sohn, Eun Jung, Sok, Sophia, Solaini, Giancarlo, Soldati, Thierry, Soleimanpour, Scott, Soler, Rosa, Solovchenko, Alexei, Somarelli, Jason, Sonawane, Avinash, Song, Fuyong, Song, Hyun Kyu, Song, Ju-Xian, Song, Kunhua, Song, Zhiyin, Soria, Leandro, Sorice, Maurizio, Soukas, Alexander, Soukup, Sandra-Fausia, Sousa, Diana, Sousa, Nadia, Spagnuolo, Paul, Spector, Stephen, Srinivas Bharath, M., St Clair, Daret, Stagni, Venturina, Staiano, Leopoldo, Stalnecker, Clint, Stankov, Metodi, Stathopulos, Peter, Stefan, Katja, Stefan, Sven Marcel, Stefanis, Leonidas, Steffan, Joan, Steinkasserer, Alexander, Stenmark, Harald, Sterneckert, Jared, Stevens, Craig, Stoka, Veronika, Storch, Stephan, Stork, Björn, Strappazzon, Flavie, Strohecker, Anne Marie, Stupack, Dwayne, Su, Huanxing, Su, Ling-Yan, Su, Longxiang, Suarez-Fontes, Ana, Subauste, Carlos, Subbian, Selvakumar, Subirada, Paula, Sudhandiran, Ganapasam, Sue, Carolyn, Sui, Xinbing, Summers, Corey, Sun, Guangchao, Sun, Jun, SUN, Kang, Sun, Meng-xiang, Sun, Qiming, Sun, Yi, Sun, Zhongjie, Sunahara, Karen, Sundberg, Eva, Susztak, Katalin, Sutovsky, Peter, Suzuki, Hidekazu, Sweeney, Gary, Symons, J David, Sze, Stephen Cho Wing, Szewczyk, Nathaniel, Tabęcka-Łonczynska, Anna, Tabolacci, Claudio, Tacke, Frank, Taegtmeyer, Heinrich, Tafani, Marco, Tagaya, Mitsuo, Tai, Haoran, Tait, Stephen, Takahashi, Yoshinori, Takats, Szabolcs, Talwar, Priti, Tam, Chit, Tam, Shing Yau, Tampellini, Davide, Tamura, Atsushi, Tan, Chong Teik, Tan, Eng-King, Tan, Ya-Qin, Tanaka, Masaki, Tanaka, Motomasa, Tang, Daolin, Tang, Jingfeng, Tang, Tie-Shan, Tanida, Isei, Tao, Zhipeng, Taouis, Mohammed, Tatenhorst, Lars, Tavernarakis, Nektarios, Taylor, Allen, Taylor, Gregory, Taylor, Joan, Tchetina, Elena, Tee, Andrew, Tegeder, Irmgard, Teis, David, Teixeira, Natercia, Teixeira-Clerc, Fatima, Tekirdag, Kumsal, Tencomnao, Tewin, Tenreiro, Sandra, Tepikin, Alexei, Testillano, Pilar, Tettamanti, Gianluca, Tharaux, Pierre-Louis, Thedieck, Kathrin, Thekkinghat, Arvind, Thellung, Stefano, Thinwa, Josephine, Thirumalaikumar, V.P., Thomas, Sufi Mary, Thomes, Paul, Thorburn, Andrew, Thukral, Lipi, Thum, Thomas, Thumm, Michael, Tian, Ling, Tichy, Ales, Till, Andreas, Timmerman, Vincent, Titorenko, Vladimir, Todi, Sokol, Todorova, Krassimira, Toivonen, Janne, Tomaipitinca, Luana, Tomar, Dhanendra, Tomas-Zapico, Cristina, Tomić, Sergej, Tong, Benjamin Chun-Kit, Tong, Chao, Tong, Xin, Tooze, Sharon, Torgersen, Maria, Torii, Satoru, Torres-López, Liliana, Torriglia, Alicia, Towers, Christina, Towns, Roberto, Toyokuni, Shinya, Trajkovic, Vladimir, Tramontano, Donatella, Tran, Quynh-Giao, Travassos, Leonardo, Trelford, Charles, Tremel, Shirley, Trougakos, Ioannis, Tsao, Betty, Tschan, Mario, Tse, Hung-Fat, Tse, Tak Fu, Tsugawa, Hitoshi, Tsvetkov, Andrey, Tumbarello, David, Tumtas, Yasin, Tuñón, María, Turcotte, Sandra, Turk, Boris, Turk, Vito, Turner, Bradley, Tuxworth, Richard, Tyler, Jessica, Tyutereva, Elena, Uchiyama, Yasuo, Ugun-Klusek, Aslihan, Uhlig, Holm, Ułamek-Kozioł, Marzena, Ulasov, Ilya, Umekawa, Midori, Ungermann, Christian, Unno, Rei, Urbe, Sylvie, Uribe-Carretero, Elisabet, Üstün, Suayib, Uversky, Vladimir, Vaccari, Thomas, Vaccaro, Maria, Vahsen, Björn, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Maria, Valko, Ayelén, Vallee, Richard, Valverde, Angela, Van Den Berghe, Greet, van der Veen, Stijn, Van Kaer, Luc, van Loosdregt, Jorg, van Wijk, Sjoerd, Vandenberghe, Wim, Vanhorebeek, Ilse, Vannier-Santos, Marcos, Vannini, Nicola, Vanrell, M Cristina, Vantaggiato, Chiara, Varano, Gabriele, Varela-Nieto, Isabel, Varga, Máté, Vasconcelos, M Helena, Vats, Somya, Vavvas, Demetrios, Vega-Naredo, Ignacio, Vega-Rubin-de-Celis, Silvia, Velasco, Guillermo, Velázquez, Ariadna, Vellai, Tibor, Vellenga, Edo, Velotti, Francesca, Verdier, Mireille, Verginis, Panayotis, Vergne, Isabelle, Verkade, Paul, Verma, Manish, Verstreken, Patrik, Vervliet, Tim, Vervoorts, Jörg, Vessoni, Alexandre, Victor, Victor, Vidal, Michel, Vidoni, Chiara, Vieira, Otilia, Vierstra, Richard, Viganó, Sonia, Vihinen, Helena, Vijayan, Vinoy, Vila, Miquel, Vilar, Marçal, Villalba, José, Villalobo, Antonio, Villarejo-Zori, Beatriz, Villarroya, Francesc, Villarroya, Joan, Vincent, Olivier, Vindis, Cecile, Viret, Christophe, Viscomi, Maria Teresa, Visnjic, Dora, Vitale, Ilio, Vocadlo, David, Voitsekhovskaja, Olga, Volonté, Cinzia, Volta, Mattia, Vomero, Marta, Von Haefen, Clarissa, Vooijs, Marc, Voos, Wolfgang, Vucicevic, Ljubica, Wade-Martins, Richard, Waguri, Satoshi, Waite, Kenrick, Wakatsuki, Shuji, Walker, David, Walker, Mark, Walker, Simon, Walter, Jochen, Wandosell, Francisco, Wang, Bo, Wang, Chao-Yung, Wang, Chen, Wang, Chenran, Wang, Chenwei, Wang, Cun-Yu, Wang, Dong, Wang, Fangyang, Wang, Feng, Wang, Fengming, Wang, Guansong, Wang, Han, Wang, Hao, Wang, Hexiang, Wang, Hong-Gang, Wang, Jianrong, Wang, Jigang, Wang, Jiou, Wang, Jundong, Wang, Kui, Wang, Lianrong, Wang, Liming, Wang, Maggie Haitian, Wang, Meiqing, Wang, Nanbu, Wang, PengWei, Wang, PeiPei, Wang, Ping, Wang, Qing Jun, Wang, Qing, Wang, Qing Kenneth, Wang, Qiong, Wang, Wen-Tao, Wang, Wuyang, Wang, Xinnan, Wang, Xuejun, Wang, Yan, Wang, Yanchang, Wang, Yanzhuang, Wang, Yen-Yun, Wang, Yihua, Wang, Yipeng, Wang, Yu, wang, yuqi, Wang, Zhe, Wang, Zhenyu, Wang, Zhouguang, Warnes, Gary, Warnsmann, Verena, Watada, Hirotaka, Watanabe, Eizo, Watchon, Maxinne, Wawrzyńska, Anna, Weaver, Timothy, Wegrzyn, Grzegorz, Wehman, Ann, Wei, Huafeng, Wei, Lei, Wei, Taotao, Wei, Yongjie, Weiergräber, Oliver, Weihl, Conrad, Weindl, Günther, Weiskirchen, Ralf, Wells, Alan, Wen, Runxia, Wen, Xin, Werner, Antonia, Weykopf, Beatrice, Wheatley, Sally, Whitton, J Lindsay, Whitworth, Alexander, Wiktorska, Katarzyna, Wildenberg, Manon, Wileman, Tom, Wilkinson, Simon, Willbold, Dieter, Williams, Brett, Williams, Robin, Williams, Roger, Williamson, Peter, Wilson, Richard, Winner, Beate, Winsor, Nathaniel, Witkin, Steven, Wodrich, Harald, Woehlbier, Ute, Wollert, Thomas, Wong, Esther, Wong, Jack Ho, Wong, Richard, Wong, Vincent Kam Wai, Wong, W Wei-Lynn, Wu, An-Guo, Wu, Chengbiao, Wu, Jian, Wu, Junfang, Wu, Kenneth, Wu, Min, Wu, Shan-Ying, Wu, Shengzhou, Wu, Shu-Yan, Wu, Shufang, Wu, William, Wu, Xiaohong, Wu, Xiaoqing, Wu, Yao-Wen, Wu, Yihua, Xavier, Ramnik, Xia, Hongguang, Xia, Lixin, Xia, Zhengyuan, Xiang, Ge, Xiang, Jin, Xiang, Mingliang, Xiang, Wei, Xiao, Bin, Xiao, Guozhi, Xiao, Hengyi, Xiao, Hong-tao, Xiao, Jian, Xiao, Lan, Xiao, Shi, Xiao, Yin, Xie, Baoming, Xie, Chuan-Ming, Xie, Min, Xie, Yuxiang, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, Jinrong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin, Yiu, Stephanie Pei Tung, Yoo, Young, Yoshida, Kiyotsugu, Yoshii, Saori, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond, Zacks, David, Zaffagnini, Gabriele, Zambelli, Vanessa, Zanella, Isabella, Zang, Qun, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos, Zarebkohan, Amir, Zarrouk, Amira, Zeitlin, Scott, Zeng, Jialiu, Zeng, Ju-deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin, Zhang, Leshuai, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, ZHOU, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith, Stallings, Christina, Tong, Chun-Kit, Ahmad, S. Tariq, Alim Al-Bari, M. Abdul, Bechara, Luiz R.G., Behrens, Georg M.N., Bhuiyan, Md. Shenuarin, Broaddus, V. Courtney, Buchan, J. Ross, Burón, M. Isabel, Carter, A. Brent, Chan, Matthew T.V., Choi, Augustine M.K., D’Adamo, Stefania, D’Amelio, Marcello, D’Arcangelo, Daniela, D’Lugos, Andrew, D’Orazi, Gabriella, De Meyer, Guido R.Y., Delpino, M. Victoria, Distler, Jörg H.W., Dixon, Ian M.C., Dobson, Renwick C.J., 2nd Dorn, Gerald, Eissa, N. Tony, Engelsen, Agnete S.T., Fairlie, W. Douglas, Ferreira, Julio C.B., H.B., Ranjitha, Hanson, Phyllis I., Hejtmancik, J. Fielding, Ho, Idy H.T., Hobbs, G. Aaron, Hoet, Peter H.M., Huang, Michael L.H., Iyer, Anand Krishnan V., Johnson, Gail V.W., Joosten, Leo A.B., Karim, Md. Razaul, Kaufmann, Stefan H.E., Ko, Ben C.B., Leck, Lionel Y.W., Lima, Thania R.R., Livingston, J. Andrew, Martin, Alexandre P.J., Montes, L. Ruth, Murphy, J. Patrick, Ng, Charlene C.W., Nicolao, M. Celeste, O’Donovan, Tracey, O’Leary, Seónadh, O’Rourke, Eyleen, O’Sullivan, Mary, O’Sullivan, Timothy, Omary, M. Bishr, Pereira, Gustavo J.S., Ratnayaka, J. Arjuna, Riazuddin, S. Amer, Rouschop, Kasper M.A., Sanderson, J. Thomas, Scaglione, K. Matthew, Schapira, Anthony H.V., Scovassi, A. Ivana, St. Clair, Daret, Sunahara, Karen K.S., Symons, J. David, Triola, Gemma, van Wijk, Sjoerd J.L., Vanrell, M. Cristina, Vasconcelos, M. Helena, Whitton, J. Lindsay, Williams, Robin S.B., Wong, W. Wei-Lynn, Wu, William K.K., Yakhine-Diop, Sokhna M.S., Yu, W. Haung, Zhang, Kalin Y.B., Dong, X. Charlie, Ain Shams University [ASU], Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University [JGU], Medical University Graz, Centre de Recherche des Cordeliers [CRC (UMR_S_1138 / U1138)], Institut Pasteur d'Iran, Leibniz Institute of Plant Biochemistry [IPB], The University of Texas M.D. Anderson Cancer Center [Houston], Institut de pharmacologie moléculaire et cellulaire [IPMC], Lipides - Nutrition - Cancer [Dijon - U1231] [LNC], Centre méditerranéen de médecine moléculaire [C3M], Institut de Biologie Valrose [IBV], Petites Molécules de neuroprotection, neurorégénération et remyélinisation, Signalisation Hormonale, Physiopathologie Endocrinienne et Métabolique, Institut Cochin [IC UM3 (UMR 8104 / U1016)], Institut NeuroMyoGène [INMG], Paris-Centre de Recherche Cardiovasculaire [PARCC (UMR_S 970/ U970)], Marqueurs cardiovasculaires en situation de stress [MASCOT (UMR_S_942 / U942)], Institut de Recherche sur le Cancer et le Vieillissement [IRCAN], Centre de Recherche en Cancérologie de Marseille [CRCM], Centre for Integrative Biology - CBI [Inserm U964 - CNRS UMR7104 - IGBMC], Oncogenesis, Stress, Signaling [OSS], Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)], Institut de Biologie Intégrative de la Cellule [I2BC], Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH], Centre de Recherches en Cancérologie de Toulouse [CRCT], Physiopathologie et traitement des maladies du foie, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL], Institut de Génétique et de Biologie Moléculaire et Cellulaire [IGBMC], Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] [BIO-PEROXIL], Centre de recherche sur l'Inflammation [CRI (UMR_S_1149 / ERL_8252 / U1149)], Unité de génétique et biologie des cancers [U830], Laboratoire d'Optique et Biosciences [LOB], Institut des Maladies Métaboliques et Casdiovasculaires [UPS/Inserm U1297 - I2MC], Différenciation et communication neuronale et neuroendocrine [DC2N], Institut de Recherche en Cancérologie de Montpellier [IRCM - U1194 Inserm - UM], Centre d'Immunologie de Marseille - Luminy [CIML], Physiopathologie et imagerie des troubles neurologiques [PhIND], Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée [LBFA], Imagine - Institut des maladies génétiques (IHU) [Imagine - U1163], Institut Mondor de Recherche Biomédicale [IMRB], Franco-czech Laboratory for clinical research on obesity, University of Michigan [Ann Arbor], University of Michigan System, Institut de pharmacologie moléculaire et cellulaire (IPMC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Université Côte d'Azur (UCA), Lipides - Nutrition - Cancer [Dijon - U1231] (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Institut de Biologie Valrose (IBV), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AP-HP Hôpital Bicêtre (Le Kremlin-Bicêtre), Nutrition, Métabolisme, Aquaculture (NuMéA), Université de Pau et des Pays de l'Adour (UPPA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut NeuroMyoGène (INMG), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Paris-Centre de Recherche Cardiovasculaire (PARCC - UMR-S U970), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de Recherche en Cancérologie de Marseille (CRCM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institute of genetics and molecular and cellular biology-Centre National de la Recherche Scientifique (CNRS), Chemistry, Oncogenesis, Stress and Signaling (COSS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut des Maladies Neurodégénératives [Bordeaux] (IMN), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches en Cancérologie de Toulouse (CRCT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physiologie et Génomique des Poissons (LPGP), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] (BIO-PEROXIL), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de génétique et biologie des cancers (U830), Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et imagerie des troubles neurologiques (PhIND), Université de Caen Normandie (UNICAEN), Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Grenoble Alpes (UGA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epithelial biology and disease - Liliane Bettencourt Chair of Developmental Biology (Equipe Inserm U1163), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Biomécanique cellulaire et respiratoire (BCR), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Charles University [Prague]-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by the National Institute of General Medical Sciences [GM131919]., Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Marqueurs cardiovasculaires en situation de stress (MASCOT (UMR_S_942 / U942)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Université Sorbonne Paris Nord, Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie des Adaptations Nutritionnelles (PhAN), Université de Nantes (UN)-Institut National de la Recherche Agronomique (INRA), Département Plateforme (PF I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut Gustave Roussy (IGR), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO), Chinese Academy of Medical Sciences [Suzhou, Chine] (CAMS), Karolinska Institutet [Stockholm], Karolinska University Hospital [Stockholm], Department of Women's and Children's Health [Stockholm, Sweden], Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École polytechnique (X), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, FHU OncoAge - Pathologies liées à l’âge [CHU Nice] (OncoAge), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA)-Institut de Pharmacologie Moléculaire et Cellulaire [UNIV Côte d'Azur] (UPMC), Institut Universitaire du Cancer de Toulouse - Oncopole (IUCT Oncopole - UMR 1037), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM), Life Sciences Institute [Ann Arbor, MI, USA], University of Michigan System-University of Michigan System, European Institute of Oncology IRCCS [Milan, Italy] (EIO), Ain Shams University (ASU), Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University (JGU), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), Réseau International des Instituts Pasteur (RIIP), Leibniz Institute of Plant Biochemistry (IPB), Hebrew University of Jerusalem, Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Paris-Centre de Recherche Cardiovasculaire (PARCC (UMR_S 970/ U970)), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Université Sorbonne Paris Nord, Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Oncogenesis, Stress, Signaling (OSS), Institut des Maladies Métaboliques et Casdiovasculaires (UPS/Inserm U1297 - I2MC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Charles University [Prague] (CU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., Adamopoulos, I. E., Adeli, K., Adolph, T. E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B. B., Agnello, M., Agostinis, P., Agrewala, J. N., Agrotis, A., Aguilar, P. V., Ahmad, S. T., Ahmed, Z. M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H. A., Al-Abd, A. M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M. A., Alberti, S., Alcocer-Gomez, E., Alessandri, C., Ali, M., Alim Al-Bari, M. A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G. D., Altan-Bonnet, N., Altieri, D. C., Alvarez, E. M. C., Alves, S., Alves da Costa, C., Alzaharna, M. M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A. O., Ammanathan, V., An, Z., Andersen, S. U., Andrabi, S. A., Andrade-Silva, M., Andres, A. M., Angelini, S., Ann, D., Anozie, U. C., Ansari, M. Y., Antas, P., Antebi, A., Anton, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araujo, W. L., Araya, J., Arden, C., Arevalo, M. -A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A. R., Armstrong-James, D., Arnaune-Pelloquin, L., Aroca, A., Arroyo, D. S., Arsov, I., Artero, R., Asaro, D. M. L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A. G., Au, A. K., Auberger, P., Auner, H. W., Aurelian, L., Autelli, R., Avagliano, L., Avalos, Y., Aveic, S., Aveleira, C. A., Avin-Wittenberg, T., Aydin, Y., Ayton, S., Ayyadevara, S., Azzopardi, M., Baba, M., Backer, J. M., Backues, S. K., Bae, D. -H., Bae, O. -N., Bae, S. H., Baehrecke, E. H., Baek, A., Baek, S. -H., Baek, S. H., Bagetta, G., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bai, Y., Bairagi, N., Baksi, S., Balbi, T., Baldari, C. T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banreti, A., Bao, Y., Baptista, M. S., Baracca, A., Barbati, C., Bargiela, A., Barila, D., Barlow, P. G., Barmada, S. J., Barreiro, E., Barreto, G. E., Bartek, J., Bartel, B., Bartolome, A., Barve, G. R., Basagoudanavar, S. H., Bassham, D. C., Bast, R. C., Basu, A., Batoko, H., Batten, I., Baulieu, E. E., Baumgarner, B. L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L. R. G., Beck, G. R., Beers, M. F., Begun, J., Behrends, C., Behrens, G. M. N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touze, N., Bellarosa, C., Belleudi, F., Bello Perez, M., Bello-Morales, R., Beltran, J. S. D. O., Beltran, S., Benbrook, D. M., Bendorius, M., Benitez, B. A., Benito-Cuesta, I., Bensalem, J., Berchtold, M. W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C. G., Besteiro, S., Betin, V. M., Beyaert, R., Bezbradica, J. S., Bhaskar, K., Bhatia-Kissova, I., Bhattacharya, R., Bhattacharya, S., Bhattacharyya, S., Bhuiyan, M. S., Bhutia, S. K., Bi, L., Bi, X., Biden, T. J., Bijian, K., Billes, V. A., Binart, N., Bincoletto, C., Birgisdottir, A. B., Bjorkoy, G., Blanco, G., Blas-Garcia, A., Blasiak, J., Blomgran, R., Blomgren, K., Blum, J. S., Boada-Romero, E., Boban, M., Boesze-Battaglia, K., Boeuf, P., Boland, B., Bomont, P., Bonaldo, P., Bonam, S. R., Bonfili, L., Bonifacino, J. S., Boone, B. A., Bootman, M. D., Bordi, M., Borner, C., Bornhauser, B. C., Borthakur, G., Bosch, J., Bose, S., Botana, L. M., Botas, J., Boulanger, C. M., Boulton, M. E., Bourdenx, M., Bourgeois, B., Bourke, N. M., Bousquet, G., Boya, P., Bozhkov, P. V., Bozi, L. H. M., Bozkurt, T. O., Brackney, D. E., Brandts, C. H., Braun, R. J., Braus, G. H., Bravo-Sagua, R., Bravo-San Pedro, J. M., Brest, P., Bringer, M. -A., Briones-Herrera, A., Broaddus, V. C., Brodersen, P., Brodsky, J. L., Brody, S. L., Bronson, P. G., Bronstein, J. M., Brown, C. N., Brown, R. E., Brum, P. C., Brumell, J. H., Brunetti-Pierri, N., Bruno, D., Bryson-Richardson, R. J., Bucci, C., Buchrieser, C., Bueno, M., Buitrago-Molina, L. E., Buraschi, S., Buch, S., Buchan, J. R., Buckingham, E. M., Budak, H., Budini, M., Bultynck, G., Burada, F., Burgoyne, J. R., Buron, M. I., Bustos, V., Buttner, S., Butturini, E., Byrd, A., Cabas, I., Cabrera-Benitez, S., Cadwell, K., Cai, J., Cai, L., Cai, Q., Cairo, M., Calbet, J. A., Caldwell, G. A., Caldwell, K. A., Call, J. A., Calvani, R., Calvo, A. C., Calvo-Rubio Barrera, M., Camara, N. O. S., Camonis, J. H., Camougrand, N., Campanella, M., Campbell, E. M., Campbell-Valois, F. -X., Campello, S., Campesi, I., Campos, J. C., Camuzard, O., Cancino, J., Candido de Almeida, D., Canesi, L., Caniggia, I., Canonico, B., Canti, C., Cao, B., Caraglia, M., Carames, B., Carchman, E. H., Cardenal-Munoz, E., Cardenas, C., Cardenas, L., Cardoso, S. M., Carew, J. S., Carle, G. F., Carleton, G., Carloni, S., Carmona-Gutierrez, D., Carneiro, L. A., Carnevali, O., Carosi, J. M., Carra, S., Carrier, A., Carrier, L., Carroll, B., Carter, A. B., Carvalho, A. N., Casanova, M., Casas, C., Casas, J., Cassioli, C., Castillo, E. F., Castillo, K., Castillo-Lluva, S., Castoldi, F., Castori, M., Castro, A. F., Castro-Caldas, M., Castro-Hernandez, J., Castro-Obregon, S., Catz, S. D., Cavadas, C., Cavaliere, F., Cavallini, G., Cavinato, M., Cayuela, M. L., Cebollada Rica, P., Cecarini, V., Cecconi, F., Cechowska-Pasko, M., Cenci, S., Ceperuelo-Mallafre, V., Cerqueira, J. J., Cerutti, J. M., Cervia, D., Cetintas, V. B., Cetrullo, S., Chae, H. -J., Chagin, A. S., Chai, C. -Y., Chakrabarti, G., Chakrabarti, O., Chakraborty, T., Chami, M., Chamilos, G., Chan, D. W., Chan, E. Y. W., Chan, E. D., Chan, H. Y. E., Chan, H. H., Chan, H., Chan, M. T. V., Chan, Y. S., Chandra, P. K., Chang, C. -P., Chang, C., Chang, H. -C., Chang, K., Chao, J., Chapman, T., Charlet-Berguerand, N., Chatterjee, S., Chaube, S. K., Chaudhary, A., Chauhan, S., Chaum, E., Checler, F., Cheetham, M. E., Chen, C. -S., Chen, G. -C., Chen, J. -F., Chen, L. L., Chen, L., Chen, M., Chen, M. -K., Chen, N., Chen, Q., Chen, R. -H., Chen, S., Chen, W., Chen, X. -M., Chen, X. -W., Chen, X., Chen, Y., Chen, Y. -G., Chen, Y. -J., Chen, Y. -Q., Chen, Z. S., Chen, Z., Chen, Z. -H., Chen, Z. J., Cheng, H., Cheng, J., Cheng, S. -Y., Cheng, W., Cheng, X., Cheng, X. -T., Cheng, Y., Cheng, Z., Cheong, H., Cheong, J. K., Chernyak, B. V., Cherry, S., Cheung, C. F. R., Cheung, C. H. A., Cheung, K. -H., Chevet, E., Chi, R. J., Chiang, A. K. S., Chiaradonna, F., Chiarelli, R., Chiariello, M., Chica, N., Chiocca, S., Chiong, M., Chiou, S. -H., Chiramel, A. I., Chiurchiu, V., Cho, D. -H., Choe, S. -K., Choi, A. M. K., Choi, M. E., Choudhury, K. R., Chow, N. S., Chu, C. T., Chua, J. P., Chua, J. J. E., Chung, H., Chung, K. P., Chung, S., Chung, S. -H., Chung, Y. -L., Cianfanelli, V., Ciechomska, I. A., Cifuentes, M., Cinque, L., Cirak, S., Cirone, M., Clague, M. J., Clarke, R., Clementi, E., Coccia, E. M., Codogno, P., Cohen, E., Cohen, M. M., Colasanti, T., Colasuonno, F., Colbert, R. A., Colell, A., Colic, M., Coll, N. S., Collins, M. O., Colombo, M. I., Colon-Ramos, D. A., Combaret, L., Comincini, S., Cominetti, M. R., Consiglio, A., Conte, A., Conti, F., Contu, V. R., Cookson, M. R., Coombs, K. M., Coppens, I., Corasaniti, M. T., Corkery, D. P., Cordes, N., Cortese, K., Costa, M. D. C., Costantino, S., Costelli, P., Coto-Montes, A., Crack, P. J., Crespo, J. L., Criollo, A., Crippa, V., Cristofani, R., Csizmadia, T., Cuadrado, A., Cui, B., Cui, J., Cui, Y., Culetto, E., Cumino, A. C., Cybulsky, A. V., Czaja, M. J., Czuczwar, S. J., D'Adamo, S., D'Amelio, M., D'Arcangelo, D., D'Lugos, A. C., D'Orazi, G., da Silva, J. A., Dafsari, H. S., Dagda, R. K., Dagdas, Y., Daglia, M., Dai, X., Dai, Y., Dal Col, J., Dalhaimer, P., Dalla Valle, L., Dallenga, T., Dalmasso, G., Damme, M., Dando, I., Dantuma, N. P., Darling, A. L., Das, H., Dasarathy, S., Dasari, S. K., Dash, S., Daumke, O., Dauphinee, A. N., Davies, J. S., Davila, V. A., Davis, R. J., Davis, T., Dayalan Naidu, S., De Amicis, F., De Bosscher, K., De Felice, F., De Franceschi, L., De Leonibus, C., de Mattos Barbosa, M. G., De Meyer, G. R. Y., De Milito, A., De Nunzio, C., De Palma, C., De Santi, M., De Virgilio, C., De Zio, D., Debnath, J., Debosch, B. J., Decuypere, J. -P., Deehan, M. A., Deflorian, G., Degregori, J., Dehay, B., Del Rio, G., Delaney, J. R., Delbridge, L. M. D., Delorme-Axford, E., Delpino, M. V., Demarchi, F., Dembitz, V., Demers, N. D., Deng, H., Deng, Z., Dengjel, J., Dent, P., Denton, D., Depamphilis, M. L., Der, C. J., Deretic, V., Descoteaux, A., Devis, L., Devkota, S., Devuyst, O., Dewson, G., Dharmasivam, M., Dhiman, R., di Bernardo, D., Di Cristina, M., Di Domenico, F., Di Fazio, P., Di Fonzo, A., Di Guardo, G., Di Guglielmo, G. M., Di Leo, L., Di Malta, C., Di Nardo, A., Di Rienzo, M., Di Sano, F., Diallinas, G., Diao, J., Diaz-Araya, G., Diaz-Laviada, I., Dickinson, J. M., Diederich, M., Dieude, M., Dikic, I., Ding, S., Ding, W. -X., Dini, L., Dinic, J., Dinic, M., Dinkova-Kostova, A. T., Dionne, M. S., Distler, J. H. W., Diwan, A., Dixon, I. M. C., Djavaheri-Mergny, M., Dobrinski, I., Dobrovinskaya, O., Dobrowolski, R., Dobson, R. C. J., Dokic, J., Dokmeci Emre, S., Donadelli, M., Dong, B., Dong, X., Dong, Z., Dorn II, G. W., Dotsch, V., Dou, H., Dou, J., Dowaidar, M., Dridi, S., Drucker, L., Du, A., Du, C., Du, G., Du, H. -N., Du, L. -L., du Toit, A., Duan, S. -B., Duan, X., Duarte, S. P., Dubrovska, A., Dunlop, E. A., Dupont, N., Duran, R. V., Dwarakanath, B. S., Dyshlovoy, S. A., Ebrahimi-Fakhari, D., Eckhart, L., Edelstein, C. L., Efferth, T., Eftekharpour, E., Eichinger, L., Eid, N., Eisenberg, T., Eissa, N. T., Eissa, S., Ejarque, M., El Andaloussi, A., El-Hage, N., El-Naggar, S., Eleuteri, A. M., El-Shafey, E. S., Elgendy, M., Eliopoulos, A. G., Elizalde, M. M., Elks, P. M., Elsasser, H. -P., Elsherbiny, E. S., Emerling, B. M., Emre, N. C. T., Eng, C. H., Engedal, N., Engelbrecht, A. -M., Engelsen, A. S. T., Enserink, J. M., Escalante, R., Esclatine, A., Escobar-Henriques, M., Eskelinen, E. -L., Espert, L., Eusebio, M. -O., Fabrias, G., Fabrizi, C., Facchiano, A., Facchiano, F., Fadeel, B., Fader, C., Faesen, A. C., Fairlie, W. D., Falco, A., Falkenburger, B. H., Fan, D., Fan, J., Fan, Y., Fang, E. F., Fang, Y., Fanto, M., Farfel-Becker, T., Faure, M., Fazeli, G., Fedele, A. O., Feldman, A. M., Feng, D., Feng, J., Feng, L., Feng, Y., Feng, W., Fenz Araujo, T., Ferguson, T. A., Fernandez, A. F., Fernandez-Checa, J. C., Fernandez-Veledo, S., Fernie, A. R., Ferrante, A. W., Ferraresi, A., Ferrari, M. F., Ferreira, J. C. B., Ferro-Novick, S., Figueras, A., Filadi, R., Filigheddu, N., Filippi-Chiela, E., Filomeni, G., Fimia, G. M., Fineschi, V., Finetti, F., Finkbeiner, S., Fisher, E. A., Fisher, P. B., Flamigni, F., Fliesler, S. J., Flo, T. H., Florance, I., Florey, O., Florio, T., Fodor, E., Follo, C., Fon, E. A., Forlino, A., Fornai, F., Fortini, P., Fracassi, A., Fraldi, A., Franco, B., Franco, R., Franconi, F., Frankel, L. B., Friedman, S. L., Frohlich, L. F., Fruhbeck, G., Fuentes, J. M., Fujiki, Y., Fujita, N., Fujiwara, Y., Fukuda, M., Fulda, S., Furic, L., Furuya, N., Fusco, C., Gack, M. U., Gaffke, L., Galadari, S., Galasso, A., Galindo, M. F., Gallolu Kankanamalage, S., Galluzzi, L., Galy, V., Gammoh, N., Gan, B., Ganley, I. G., Gao, F., Gao, H., Gao, M., Gao, P., Gao, S. -J., Gao, W., Gao, X., Garcera, A., Garcia, M. N., Garcia, V. E., Garcia-Del Portillo, F., Garcia-Escudero, V., Garcia-Garcia, A., Garcia-Macia, M., Garcia-Moreno, D., Garcia-Ruiz, C., Garcia-Sanz, P., Garg, A. D., Gargini, R., Garofalo, T., Garry, R. F., Gassen, N. C., Gatica, D., Ge, L., Ge, W., Geiss-Friedlander, R., Gelfi, C., Genschik, P., Gentle, I. E., Gerbino, V., Gerhardt, C., Germain, K., Germain, M., Gewirtz, D. A., Ghasemipour Afshar, E., Ghavami, S., Ghigo, A., Ghosh, M., Giamas, G., Giampietri, C., Giatromanolaki, A., Gibson, G. E., Gibson, S. B., Ginet, V., Giniger, E., Giorgi, C., Girao, H., Girardin, S. E., Giridharan, M., Giuliano, S., Giulivi, C., Giuriato, S., Giustiniani, J., Gluschko, A., Goder, V., Goginashvili, A., Golab, J., Goldstone, D. C., Golebiewska, A., Gomes, L. R., Gomez, R., Gomez-Sanchez, R., Gomez-Puerto, M. C., Gomez-Sintes, R., Gong, Q., Goni, F. M., Gonzalez-Gallego, J., Gonzalez-Hernandez, T., Gonzalez-Polo, R. A., Gonzalez-Reyes, J. A., Gonzalez-Rodriguez, P., Goping, I. S., Gorbatyuk, M. S., Gorbunov, N. V., Gorgulu, K., Gorojod, R. M., Gorski, S. M., Goruppi, S., Gotor, C., Gottlieb, R. A., Gozes, I., Gozuacik, D., Graef, M., Graler, M. H., Granatiero, V., Grasso, D., Gray, J. P., Green, D. R., Greenhough, A., Gregory, S. L., Griffin, E. F., Grinstaff, M. W., Gros, F., Grose, C., Gross, A. S., Gruber, F., Grumati, P., Grune, T., Gu, X., Guan, J. -L., Guardia, C. M., Guda, K., Guerra, F., Guerri, C., Guha, P., Guillen, C., Gujar, S., Gukovskaya, A., Gukovsky, I., Gunst, J., Gunther, A., Guntur, A. R., Guo, C., Guo, H., Guo, L. -W., Guo, M., Gupta, P., Gupta, S. K., Gupta, S., Gupta, V. B., Gupta, V., Gustafsson, A. B., Gutterman, D. D., H. B, R., Haapasalo, A., Haber, J. E., Hac, A., Hadano, S., Hafren, A. J., Haidar, M., Hall, B. S., Hallden, G., Hamacher-Brady, A., Hamann, A., Hamasaki, M., Han, W., Hansen, M., Hanson, P. I., Hao, Z., Harada, M., Harhaji-Trajkovic, L., Hariharan, N., Haroon, N., Harris, J., Hasegawa, T., Hasima Nagoor, N., Haspel, J. A., Haucke, V., Hawkins, W. D., Hay, B. A., Haynes, C. M., Hayrabedyan, S. B., Hays, T. S., He, C., He, Q., He, R. -R., He, Y. -W., He, Y. -Y., Heakal, Y., Heberle, A. M., Hejtmancik, J. F., Helgason, G. V., Henkel, V., Herb, M., Hergovich, A., Herman-Antosiewicz, A., Hernandez, A., Hernandez, C., Hernandez-Diaz, S., Hernandez-Gea, V., Herpin, A., Herreros, J., Hervas, J. H., Hesselson, D., Hetz, C., Heussler, V. T., Higuchi, Y., Hilfiker, S., Hill, J. A., Hlavacek, W. S., Ho, E. A., Ho, I. H. T., Ho, P. W. -L., Ho, S. -L., Ho, W. Y., Hobbs, G. A., Hochstrasser, M., Hoet, P. H. M., Hofius, D., Hofman, P., Hohn, A., Holmberg, C. I., Hombrebueno, J. R., Yi-Ren Hong, C. -W. H., Hooper, L. V., Hoppe, T., Horos, R., Hoshida, Y., Hsin, I. -L., Hsu, H. -Y., Hu, B., Hu, D., Hu, L. -F., Hu, M. C., Hu, R., Hu, W., Hu, Y. -C., Hu, Z. -W., Hua, F., Hua, J., Hua, Y., Huan, C., Huang, C., Huang, H., Huang, K., Huang, M. L. H., Huang, R., Huang, S., Huang, T., Huang, X., Huang, Y. J., Huber, T. B., Hubert, V., Hubner, C. A., Hughes, S. M., Hughes, W. E., Humbert, M., Hummer, G., Hurley, J. H., Hussain, S., Hussey, P. J., Hutabarat, M., Hwang, H. -Y., Hwang, S., Ieni, A., Ikeda, F., Imagawa, Y., Imai, Y., Imbriano, C., Imoto, M., Inman, D. M., Inoki, K., Iovanna, J., Iozzo, R. V., Ippolito, G., Irazoqui, J. E., Iribarren, P., Ishaq, M., Ishikawa, M., Ishimwe, N., Isidoro, C., Ismail, N., Issazadeh-Navikas, S., Itakura, E., Ito, D., Ivankovic, D., Ivanova, S., Iyer, A. K. V., Izquierdo, J. M., Izumi, M., Jaattela, M., Jabir, M. S., Jackson, W. T., Jacobo-Herrera, N., Jacomin, A. -C., Jacquin, E., Jadiya, P., Jaeschke, H., Jagannath, C., Jakobi, A. J., Jakobsson, J., Janji, B., Jansen-Durr, P., Jansson, P. J., Jantsch, J., Januszewski, S., Jassey, A., Jean, S., Jeltsch-David, H., Jendelova, P., Jenny, A., Jensen, T. E., Jessen, N., Jewell, J. L., Ji, J., Jia, L., Jia, R., Jiang, L., Jiang, Q., Jiang, R., Jiang, T., Jiang, X., Jiang, Y., Jimenez-Sanchez, M., Jin, E. -J., Jin, F., Jin, H., Jin, L., Jin, M., Jin, S., Jo, E. -K., Joffre, C., Johansen, T., Johnson, G. V. W., Johnston, S. A., Jokitalo, E., Jolly, M. K., Joosten, L. A. B., Jordan, J., Joseph, B., Ju, D., Ju, J. -S., Ju, J., Juarez, E., Judith, D., Juhasz, G., Jun, Y., Jung, C. H., Jung, S. -C., Jung, Y. K., Jungbluth, H., Jungverdorben, J., Just, S., Kaarniranta, K., Kaasik, A., Kabuta, T., Kaganovich, D., Kahana, A., Kain, R., Kajimura, S., Kalamvoki, M., Kalia, M., Kalinowski, D. S., Kaludercic, N., Kalvari, I., Kaminska, J., Kaminskyy, V. O., Kanamori, H., Kanasaki, K., Kang, C., Kang, R., Kang, S. S., Kaniyappan, S., Kanki, T., Kanneganti, T. -D., Kanthasamy, A. G., Kanthasamy, A., Kantorow, M., Kapuy, O., Karamouzis, M. V., Karim, M. R., Karmakar, P., Katare, R. G., Kato, M., Kaufmann, S. H. E., Kauppinen, A., Kaushal, G. P., Kaushik, S., Kawasaki, K., Kazan, K., Ke, P. -Y., Keating, D. J., Keber, U., Kehrl, J. H., Keller, K. E., Keller, C. W., Kemper, J. K., Kenific, C. M., Kepp, O., Kermorgant, S., Kern, A., Ketteler, R., Keulers, T. G., Khalfin, B., Khalil, H., Khambu, B., Khan, S. Y., Khandelwal, V. K. M., Khandia, R., Kho, W., Khobrekar, N. V., Khuansuwan, S., Khundadze, M., Killackey, S. A., Kim, D., Kim, D. R., Kim, D. -H., Kim, D. -E., Kim, E. Y., Kim, E. -K., Kim, H. -R., Kim, H. -S., Hyung-Ryong, Kim, Kim, J. H., Kim, J. K., Kim, J. -H., Kim, J., Kim, K. I., Kim, P. K., Kim, S. -J., Kimball, S. R., Kimchi, A., Kimmelman, A. C., Kimura, T., King, M. A., Kinghorn, K. J., Kinsey, C. G., Kirkin, V., Kirshenbaum, L. A., Kiselev, S. L., Kishi, S., Kitamoto, K., Kitaoka, Y., Kitazato, K., Kitsis, R. N., Kittler, J. T., Kjaerulff, O., Klein, P. S., Klopstock, T., Klucken, J., Knaevelsrud, H., Knorr, R. L., Ko, B. C. B., Ko, F., Ko, J. -L., Kobayashi, H., Kobayashi, S., Koch, I., Koch, J. C., Koenig, U., Kogel, D., Koh, Y. H., Koike, M., Kohlwein, S. D., Kocaturk, N. M., Komatsu, M., Konig, J., Kono, T., Kopp, B. T., Korcsmaros, T., Korkmaz, G., Korolchuk, V. I., Korsnes, M. S., Koskela, A., Kota, J., Kotake, Y., Kotler, M. L., Kou, Y., Koukourakis, M. I., Koustas, E., Kovacs, A. L., Kovacs, T., Koya, D., Kozako, T., Kraft, C., Krainc, D., Kramer, H., Krasnodembskaya, A. D., Kretz-Remy, C., Kroemer, G., Ktistakis, N. T., Kuchitsu, K., Kuenen, S., Kuerschner, L., Kukar, T., Kumar, A., Kumar, D., Kumar, S., Kume, S., Kumsta, C., Kundu, C. N., Kundu, M., Kunnumakkara, A. B., Kurgan, L., Kutateladze, T. G., Kutlu, O., Kwak, S., Kwon, H. J., Kwon, T. K., Kwon, Y. T., Kyrmizi, I., La Spada, A., Labonte, P., Ladoire, S., Laface, I., Lafont, F., Lagace, D. C., Lahiri, V., Lai, Z., Laird, A. S., Lakkaraju, A., Lamark, T., Lan, S. -H., Landajuela, A., Lane, D. J. R., Lane, J. D., Lang, C. H., Lange, C., Langel, U., Langer, R., Lapaquette, P., Laporte, J., Larusso, N. F., Lastres-Becker, I., Lau, W. C. Y., Laurie, G. W., Lavandero, S., Law, B. Y. K., Law, H. K. -W., Layfield, R., Le, W., Le Stunff, H., Leary, A. Y., Lebrun, J. -J., Leck, L. Y. W., Leduc-Gaudet, J. -P., Lee, C., Lee, C. -P., Lee, D. -H., Lee, E. B., Lee, E. F., Lee, G. M., Lee, H. -J., Lee, H. K., Lee, J. M., Lee, J. S., Lee, J. -A., Lee, J. -Y., Lee, J. H., Lee, M., Lee, M. G., Lee, M. J., Lee, M. -S., Lee, S. Y., Lee, S. -J., Lee, S. B., Lee, W. H., Lee, Y. -R., Lee, Y. -H., Lee, Y., Lefebvre, C., Legouis, R., Lei, Y. L., Lei, Y., Leikin, S., Leitinger, G., Lemus, L., Leng, S., Lenoir, O., Lenz, G., Lenz, H. J., Lenzi, P., Leon, Y., Leopoldino, A. M., Leschczyk, C., Leskela, S., Letellier, E., Leung, C. -T., Leung, P. S., Leventhal, J. S., Levine, B., Lewis, P. A., Ley, K., Li, B., Li, D. -Q., Li, J., Li, K., Li, L., Li, M., Li, P. -L., Li, M. -Q., Li, Q., Li, S., Li, T., Li, W., Li, X., Li, Y. -P., Li, Y., Li, Z., Lian, J., Liang, C., Liang, Q., Liang, W., Liang, Y., Liao, G., Liao, L., Liao, M., Liao, Y. -F., Librizzi, M., Lie, P. P. Y., Lilly, M. A., Lim, H. J., Lima, T. R. R., Limana, F., Lin, C., Lin, C. -W., Lin, D. -S., Lin, F. -C., Lin, J. D., Lin, K. M., Lin, K. -H., Lin, L. -T., Lin, P. -H., Lin, Q., Lin, S., Lin, S. -J., Lin, W., Lin, X., Lin, Y. -X., Lin, Y. -S., Linden, R., Lindner, P., Ling, S. -C., Lingor, P., Linnemann, A. K., Liou, Y. -C., Lipinski, M. M., Lipovsek, S., Lira, V. A., Lisiak, N., Liton, P. B., Liu, C., Liu, C. -H., Liu, C. -F., Liu, C. H., Liu, F., Liu, H., Liu, H. -S., Liu, H. -F., Liu, J., Liu, L., Liu, M., Liu, Q., Liu, W., Liu, X. -H., Liu, X., Liu, Y., Livingston, J. A., Lizard, G., Lizcano, J. M., Ljubojevic-Holzer, S., Lleonart, M. E., Llobet-Navas, D., Llorente, A., Lo, C. H., Lobato-Marquez, D., Long, Q., Long, Y. C., Loos, B., Loos, J. A., Lopez, M. G., Lopez-Domenech, G., Lopez-Guerrero, J. A., Lopez-Jimenez, A. T., Lopez-Perez, O., Lopez-Valero, I., Lorenowicz, M. J., Lorente, M., Lorincz, P., Lossi, L., Lotersztajn, S., Lovat, P. E., Lovell, J. F., Lovy, A., Low, P., Lu, G., Lu, H., Lu, J. -H., Lu, J. -J., Lu, M., Lu, S., Luciani, A., Lucocq, J. M., Ludovico, P., Luftig, M. A., Luhr, M., Luis-Ravelo, D., Lum, J. J., Luna-Dulcey, L., Lund, A. H., Lund, V. K., Lunemann, J. D., Luningschror, P., Luo, H., Luo, R., Luo, S., Luo, Z., Luparello, C., Luscher, B., Luu, L., Lyakhovich, A., Lyamzaev, K. G., Lystad, A. H., Lytvynchuk, L., Ma, A. C., Ma, C., Ma, M., Ma, N. -F., Ma, Q. -H., Ma, X., Ma, Y., Ma, Z., Macdougald, O. A., Macian, F., Macintosh, G. C., Mackeigan, J. P., Macleod, K. F., Maday, S., Madeo, F., Madesh, M., Madl, T., Madrigal-Matute, J., Maeda, A., Maejima, Y., Magarinos, M., Mahavadi, P., Maiani, E., Maiese, K., Maiti, P., Maiuri, M. C., Majello, B., Major, M. B., Makareeva, E., Malik, F., Mallilankaraman, K., Malorni, W., Maloyan, A., Mammadova, N., Man, G. C. W., Manai, F., Mancias, J. D., Mandelkow, E. -M., Mandell, M. A., Manfredi, A. A., Manjili, M. H., Manjithaya, R., Manque, P., Manshian, B. B., Manzano, R., Manzoni, C., Mao, K., Marchese, C., Marchetti, S., Marconi, A. M., Marcucci, F., Mardente, S., Mareninova, O. A., Margeta, M., Mari, M., Marinelli, S., Marinelli, O., Marino, G., Mariotto, S., Marshall, R. S., Marten, M. R., Martens, S., Martin, A. P. J., Martin, K. R., Martin, S., Martin-Segura, A., Martin-Acebes, M. A., Martin-Burriel, I., Martin-Rincon, M., Martin-Sanz, P., Martina, J. A., Martinet, W., Martinez, A., Martinez, J., Martinez Velazquez, M., Martinez-Lopez, N., Martinez-Vicente, M., Martins, D. O., Martins, J. O., Martins, W. K., Martins-Marques, T., Marzetti, E., Masaldan, S., Masclaux-Daubresse, C., Mashek, D. G., Massa, V., Massieu, L., Masson, G. R., Masuelli, L., Masyuk, A. I., Masyuk, T. V., Matarrese, P., Matheu, A., Matoba, S., Matsuzaki, S., Mattar, P., Matte, A., Mattoscio, D., Mauriz, J. L., Mauthe, M., Mauvezin, C., Maverakis, E., Maycotte, P., Mayer, J., Mazzoccoli, G., Mazzoni, C., Mazzulli, J. R., Mccarty, N., Mcdonald, C., Mcgill, M. R., Mckenna, S. L., Mclaughlin, B., Mcloughlin, F., Mcniven, M. A., Mcwilliams, T. G., Mechta-Grigoriou, F., Medeiros, T. C., Medina, D. L., Megeney, L. A., Megyeri, K., Mehrpour, M., Mehta, J. L., Meijer, A. J., Meijer, A. H., Mejlvang, J., Melendez, A., Melk, A., Memisoglu, G., Mendes, A. F., Meng, D., Meng, F., Meng, T., Menna-Barreto, R., Menon, M. B., Mercer, C., Mercier, A. E., Mergny, J. -L., Merighi, A., Merkley, S. D., Merla, G., Meske, V., Mestre, A. C., Metur, S. P., Meyer, C., Meyer, H., Mi, W., Mialet-Perez, J., Miao, J., Micale, L., Miki, Y., Milan, E., Milczarek, M., Miller, D. L., Miller, S. I., Miller, S., Millward, S. W., Milosevic, I., Minina, E. A., Mirzaei, H., Mirzaei, H. R., Mirzaei, M., Mishra, A., Mishra, N., Mishra, P. K., Misirkic Marjanovic, M., Misasi, R., Misra, A., Misso, G., Mitchell, C., Mitou, G., Miura, T., Miyamoto, S., Miyazaki, M., Miyazaki, T., Miyazawa, K., Mizushima, N., Mogensen, T. H., Mograbi, B., Mohammadinejad, R., Mohamud, Y., Mohanty, A., Mohapatra, S., Mohlmann, T., Mohmmed, A., Moles, A., Moley, K. H., Molinari, M., Mollace, V., Moller, A. B., Mollereau, B., Mollinedo, F., Montagna, C., Monteiro, M. J., Montella, A., Montes, L. R., Montico, B., Mony, V. K., Monzio Compagnoni, G., Moore, M. N., Moosavi, M. A., Mora, A. L., Mora, M., Morales-Alamo, D., Moratalla, R., Moreira, P. I., Morelli, E., Moreno, S., Moreno-Blas, D., Moresi, V., Morga, B., Morgan, A. H., Morin, F., Morishita, H., Moritz, O. L., Moriyama, M., Moriyasu, Y., Morleo, M., Morselli, E., Moruno-Manchon, J. F., Moscat, J., Mostowy, S., Motori, E., Moura, A. F., Moustaid-Moussa, N., Mrakovcic, M., Mucino-Hernandez, G., Mukherjee, A., Mukhopadhyay, S., Mulcahy Levy, J. M., Mulero, V., Muller, S., Munch, C., Munjal, A., Munoz-Canoves, P., Munoz-Galdeano, T., Munz, C., Murakawa, T., Muratori, C., Murphy, B. M., Murphy, J. P., Murthy, A., Myohanen, T. T., Mysorekar, I. U., Mytych, J., Nabavi, S. M., Nabissi, M., Nagy, P., Nah, J., Nahimana, A., Nakagawa, I., Nakamura, K., Nakatogawa, H., Nandi, S. S., Nanjundan, M., Nanni, M., Napolitano, G., Nardacci, R., Narita, M., Nassif, M., Nathan, I., Natsumeda, M., Naude, R. J., Naumann, C., Naveiras, O., Navid, F., Nawrocki, S. T., Nazarko, T. Y., Nazio, F., Negoita, F., Neill, T., Neisch, A. L., Neri, L. M., Netea, M. G., Neubert, P., Neufeld, T. P., Neumann, D., Neutzner, A., Newton, P. T., Ney, P. A., Nezis, I. P., Ng, C. C. W., Ng, T. B., Nguyen, H. T. T., Nguyen, L. T., Ni, H. -M., Ni Cheallaigh, C., Ni, Z., Nicolao, M. C., Nicoli, F., Nieto-Diaz, M., Nilsson, P., Ning, S., Niranjan, R., Nishimune, H., Niso-Santano, M., Nixon, R. A., Nobili, A., Nobrega, C., Noda, T., Nogueira-Recalde, U., Nolan, T. M., Nombela, I., Novak, I., Novoa, B., Nozawa, T., Nukina, N., Nussbaum-Krammer, C., Nylandsted, J., O'Donovan, T. R., O'Leary, S. M., O'Rourke, E. J., O'Sullivan, M. P., O'Sullivan, T. E., Oddo, S., Oehme, I., Ogawa, M., Ogier-Denis, E., Ogmundsdottir, M. H., Ogretmen, B., Oh, G. T., Oh, S. -H., Oh, Y. J., Ohama, T., Ohashi, Y., Ohmuraya, M., Oikonomou, V., Ojha, R., Okamoto, K., Okazawa, H., Oku, M., Olivan, S., Oliveira, J. M. A., Ollmann, M., Olzmann, J. A., Omari, S., Omary, M. B., Onal, G., Ondrej, M., Ong, S. -B., Ong, S. -G., Onnis, A., Orellana, J. A., Orellana-Munoz, S., Ortega-Villaizan, M. D. M., Ortiz-Gonzalez, X. R., Ortona, E., Osiewacz, H. D., Osman, A. -H. K., Osta, R., Otegui, M. S., Otsu, K., Ott, C., Ottobrini, L., Ou, J. -H. J., Outeiro, T. F., Oynebraten, I., Ozturk, M., Pages, G., Pahari, S., Pajares, M., Pajvani, U. B., Pal, R., Paladino, S., Pallet, N., Palmieri, M., Palmisano, G., Palumbo, C., Pampaloni, F., Pan, L., Pan, Q., Pan, W., Pan, X., Panasyuk, G., Pandey, R., Pandey, U. B., Pandya, V., Paneni, F., Pang, S. Y., Panzarini, E., Papademetrio, D. L., Papaleo, E., Papinski, D., Papp, D., Park, E. C., Park, H. T., Park, J. -M., Park, J. -I., Park, J. T., Park, J., Park, S. C., Park, S. -Y., Parola, A. H., Parys, J. B., Pasquier, A., Pasquier, B., Passos, J. F., Pastore, N., Patel, H. H., Patschan, D., Pattingre, S., Pedraza-Alva, G., Pedraza-Chaverri, J., Pedrozo, Z., Pei, G., Pei, J., Peled-Zehavi, H., Pellegrini, J. M., Pelletier, J., Penalva, M. A., Peng, D., Peng, Y., Penna, F., Pennuto, M., Pentimalli, F., Pereira, C. M. F., Pereira, G. J. S., Pereira, L. C., Pereira de Almeida, L., Perera, N. D., Perez-Lara, A., Perez-Oliva, A. B., Perez-Perez, M. E., Periyasamy, P., Perl, A., Perrotta, C., Perrotta, I., Pestell, R. G., Petersen, M., Petrache, I., Petrovski, G., Pfirrmann, T., Pfister, A. S., Philips, J. A., Pi, H., Picca, A., Pickrell, A. M., Picot, S., Pierantoni, G. M., Pierdominici, M., Pierre, P., Pierrefite-Carle, V., Pierzynowska, K., Pietrocola, F., Pietruczuk, M., Pignata, C., Pimentel-Muinos, F. X., Pinar, M., Pinheiro, R. O., Pinkas-Kramarski, R., Pinton, P., Pircs, K., Piya, S., Pizzo, P., Plantinga, T. S., Platta, H. W., Plaza-Zabala, A., Plomann, M., Plotnikov, E. Y., Plun-Favreau, H., Pluta, R., Pocock, R., Poggeler, S., Pohl, C., Poirot, M., Poletti, A., Ponpuak, M., Popelka, H., Popova, B., Porta, H., Porte Alcon, S., Portilla-Fernandez, E., Post, M., Potts, M. B., Poulton, J., Powers, T., Prahlad, V., Prajsnar, T. K., Pratico, D., Prencipe, R., Priault, M., Proikas-Cezanne, T., Promponas, V. J., Proud, C. G., Puertollano, R., Puglielli, L., Pulinilkunnil, T., Puri, D., Puri, R., Puyal, J., Qi, X., Qi, Y., Qian, W., Qiang, L., Qiu, Y., Quadrilatero, J., Quarleri, J., Raben, N., Rabinowich, H., Ragona, D., Ragusa, M. J., Rahimi, N., Rahmati, M., Raia, V., Raimundo, N., Rajasekaran, N. -S., Ramachandra Rao, S., Rami, A., Ramirez-Pardo, I., Ramsden, D. B., Randow, F., Rangarajan, P. N., Ranieri, D., Rao, H., Rao, L., Rao, R., Rathore, S., Ratnayaka, J. A., Ratovitski, E. A., Ravanan, P., Ravegnini, G., Ray, S. K., Razani, B., Rebecca, V., Reggiori, F., Regnier-Vigouroux, A., Reichert, A. S., Reigada, D., Reiling, J. H., Rein, T., Reipert, S., Rekha, R. S., Ren, H., Ren, J., Ren, W., Renault, T., Renga, G., Reue, K., Rewitz, K., Ribeiro de Andrade Ramos, B., Riazuddin, S. A., Ribeiro-Rodrigues, T. M., Ricci, J. -E., Ricci, R., Riccio, V., Richardson, D. R., Rikihisa, Y., Risbud, M. V., Risueno, R. M., Ritis, K., Rizza, S., Rizzuto, R., Roberts, H. C., Roberts, L. D., Robinson, K. J., Roccheri, M. C., Rocchi, S., Rodney, G. G., Rodrigues, T., Rodrigues Silva, V. R., Rodriguez, A., Rodriguez-Barrueco, R., Rodriguez-Henche, N., Rodriguez-Rocha, H., Roelofs, J., Rogers, R. S., Rogov, V. V., Rojo, A. I., Rolka, K., Romanello, V., Romani, L., Romano, A., Romano, P. S., Romeo-Guitart, D., Romero, L. C., Romero, M., Roney, J. C., Rongo, C., Roperto, S., Rosenfeldt, M. T., Rosenstiel, P., Rosenwald, A. G., Roth, K. A., Roth, L., Roth, S., Rouschop, K. M. A., Roussel, B. D., Roux, S., Rovere-Querini, P., Roy, A., Rozieres, A., Ruano, D., Rubinsztein, D. C., Rubtsova, M. P., Ruckdeschel, K., Ruckenstuhl, C., Rudolf, E., Rudolf, R., Ruggieri, A., Ruparelia, A. A., Rusmini, P., Russell, R. R., Russo, G. L., Russo, M., Russo, R., Ryabaya, O. O., Ryan, K. M., Ryu, K. -Y., Sabater-Arcis, M., Sachdev, U., Sacher, M., Sachse, C., Sadhu, A., Sadoshima, J., Safren, N., Saftig, P., Sagona, A. P., Sahay, G., Sahebkar, A., Sahin, M., Sahin, O., Sahni, S., Saito, N., Saito, S., Saito, T., Sakai, R., Sakai, Y., Sakamaki, J. -I., Saksela, K., Salazar, G., Salazar-Degracia, A., Salekdeh, G. H., Saluja, A. K., Sampaio-Marques, B., Sanchez, M. C., Sanchez-Alcazar, J. A., Sanchez-Vera, V., Sancho-Shimizu, V., Sanderson, J. T., Sandri, M., Santaguida, S., Santambrogio, L., Santana, M. M., Santoni, G., Sanz, A., Sanz, P., Saran, S., Sardiello, M., Sargeant, T. J., Sarin, A., Sarkar, C., Sarkar, S., Sarrias, M. -R., Sarmah, D. T., Sarparanta, J., Sathyanarayan, A., Sathyanarayanan, R., Scaglione, K. M., Scatozza, F., Schaefer, L., Schafer, Z. T., Schaible, U. E., Schapira, A. H. V., Scharl, M., Schatzl, H. M., Schein, C. H., Scheper, W., Scheuring, D., Schiaffino, M. V., Schiappacassi, M., Schindl, R., Schlattner, U., Schmidt, O., Schmitt, R., Schmidt, S. D., Schmitz, I., Schmukler, E., Schneider, A., Schneider, B. E., Schober, R., Schoijet, A. C., Schott, M. B., Schramm, M., Schroder, B., Schuh, K., Schuller, C., Schulze, R. J., Schurmanns, L., Schwamborn, J. C., Schwarten, M., Scialo, F., Sciarretta, S., Scott, M. J., Scotto, K. W., Scovassi, A. I., Scrima, A., Scrivo, A., Sebastian, D., Sebti, S., Sedej, S., Segatori, L., Segev, N., Seglen, P. O., Seiliez, I., Seki, E., Selleck, S. B., Sellke, F. W., Selsby, J. T., Sendtner, M., Senturk, S., Seranova, E., Sergi, C., Serra-Moreno, R., Sesaki, H., Settembre, C., Setty, S. R. G., Sgarbi, G., Sha, O., Shacka, J. J., Shah, J. A., Shang, D., Shao, C., Shao, F., Sharbati, S., Sharkey, L. M., Sharma, D., Sharma, G., Sharma, K., Sharma, P., Sharma, S., Shen, H. -M., Shen, H., Shen, J., Shen, M., Shen, W., Shen, Z., Sheng, R., Sheng, Z., Sheng, Z. -H., Shi, J., Shi, X., Shi, Y. -H., Shiba-Fukushima, K., Shieh, J. -J., Shimada, Y., Shimizu, S., Shimozawa, M., Shintani, T., Shoemaker, C. J., Shojaei, S., Shoji, I., Shravage, B. V., Shridhar, V., Shu, C. -W., Shu, H. -B., Shui, K., Shukla, A. K., Shutt, T. E., Sica, V., Siddiqui, A., Sierra, A., Sierra-Torre, V., Signorelli, S., Sil, P., Silva, B. J. D. A., Silva, J. D., Silva-Pavez, E., Silvente-Poirot, S., Simmonds, R. E., Simon, A. K., Simon, H. -U., Simons, M., Singh, A., Singh, L. P., Singh, R., Singh, S. V., Singh, S. K., Singh, S. B., Singh, S., Singh, S. P., Sinha, D., Sinha, R. A., Sinha, S., Sirko, A., Sirohi, K., Sivridis, E. L., Skendros, P., Skirycz, A., Slaninova, I., Smaili, S. S., Smertenko, A., Smith, M. D., Soenen, S. J., Sohn, E. J., Sok, S. P. M., Solaini, G., Soldati, T., Soleimanpour, S. A., Soler, R. M., Solovchenko, A., Somarelli, J. A., Sonawane, A., Song, F., Song, H. K., Song, J. -X., Song, K., Song, Z., Soria, L. R., Sorice, M., Soukas, A. A., Soukup, S. -F., Sousa, D., Sousa, N., Spagnuolo, P. A., Spector, S. A., Srinivas Bharath, M. M., S, t. Clair D., Stagni, V., Staiano, L., Stalnecker, C. A., Stankov, M. V., Stathopulos, P. B., Stefan, K., Stefan, S. M., Stefanis, L., Steffan, J. S., Steinkasserer, A., Stenmark, H., Sterneckert, J., Stevens, C., Stoka, V., Storch, S., Stork, B., Strappazzon, F., Strohecker, A. M., Stupack, D. G., Su, H., Su, L. -Y., Su, L., Suarez-Fontes, A. M., Subauste, C. S., Subbian, S., Subirada, P. V., Sudhandiran, G., Sue, C. M., Sui, X., Summers, C., Sun, G., Sun, J., Sun, K., Sun, M. -X., Sun, Q., Sun, Y., Sun, Z., Sunahara, K. K. S., Sundberg, E., Susztak, K., Sutovsky, P., Suzuki, H., Sweeney, G., Symons, J. D., Sze, S. C. W., Szewczyk, N. J., Tabecka-Lonczynska, A., Tabolacci, C., Tacke, F., Taegtmeyer, H., Tafani, M., Tagaya, M., Tai, H., Tait, S. W. G., Takahashi, Y., Takats, S., Talwar, P., Tam, C., Tam, S. Y., Tampellini, D., Tamura, A., Tan, C. T., Tan, E. -K., Tan, Y. -Q., Tanaka, M., Tang, D., Tang, J., Tang, T. -S., Tanida, I., Tao, Z., Taouis, M., Tatenhorst, L., Tavernarakis, N., Taylor, A., Taylor, G. A., Taylor, J. M., Tchetina, E., Tee, A. R., Tegeder, I., Teis, D., Teixeira, N., Teixeira-Clerc, F., Tekirdag, K. A., Tencomnao, T., Tenreiro, S., Tepikin, A. V., Testillano, P. S., Tettamanti, G., Tharaux, P. -L., Thedieck, K., Thekkinghat, A. A., Thellung, S., Thinwa, J. W., Thirumalaikumar, V. P., Thomas, S. M., Thomes, P. G., Thorburn, A., Thukral, L., Thum, T., Thumm, M., Tian, L., Tichy, A., Till, A., Timmerman, V., Titorenko, V. I., Todi, S. V., Todorova, K., Toivonen, J. M., Tomaipitinca, L., Tomar, D., Tomas-Zapico, C., Tomic, S., Tong, B. C. -K., Tong, C., Tong, X., Tooze, S. A., Torgersen, M. L., Torii, S., Torres-Lopez, L., Torriglia, A., Towers, C. G., Towns, R., Toyokuni, S., Trajkovic, V., Tramontano, D., Tran, Q. -G., Travassos, L. H., Trelford, C. B., Tremel, S., Trougakos, I. P., Tsao, B. P., Tschan, M. P., Tse, H. -F., Tse, T. F., Tsugawa, H., Tsvetkov, A. S., Tumbarello, D. A., Tumtas, Y., Tunon, M. J., Turcotte, S., Turk, B., Turk, V., Turner, B. J., Tuxworth, R. I., Tyler, J. K., Tyutereva, E. V., Uchiyama, Y., Ugun-Klusek, A., Uhlig, H. H., Ulamek-Koziol, M., Ulasov, I. V., Umekawa, M., Ungermann, C., Unno, R., Urbe, S., Uribe-Carretero, E., Ustun, S., Uversky, V. N., Vaccari, T., Vaccaro, M. I., Vahsen, B. F., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, M. J., Valko, A., Vallee, R. B., Valverde, A. M., Van den Berghe, G., van der Veen, S., Van Kaer, L., van Loosdregt, J., van Wijk, S. J. L., Vandenberghe, W., Vanhorebeek, I., Vannier-Santos, M. A., Vannini, N., Vanrell, M. C., Vantaggiato, C., Varano, G., Varela-Nieto, I., Varga, M., Vasconcelos, M. H., Vats, S., Vavvas, D. G., Vega-Naredo, I., Vega-Rubin-de-Celis, S., Velasco, G., Velazquez, A. P., Vellai, T., Vellenga, E., Velotti, F., Verdier, M., Verginis, P., Vergne, I., Verkade, P., Verma, M., Verstreken, P., Vervliet, T., Vervoorts, J., Vessoni, A. T., Victor, V. M., Vidal, M., Vidoni, C., Vieira, O. V., Vierstra, R. D., Vigano, S., Vihinen, H., Vijayan, V., Vila, M., Vilar, M., Villalba, J. M., Villalobo, A., Villarejo-Zori, B., Villarroya, F., Villarroya, J., Vincent, O., Vindis, C., Viret, C., Viscomi, M. T., Visnjic, D., Vitale, I., Vocadlo, D. J., Voitsekhovskaja, O. V., Volonte, C., Volta, M., Vomero, M., Von Haefen, C., Vooijs, M. A., Voos, W., Vucicevic, L., Wade-Martins, R., Waguri, S., Waite, K. A., Wakatsuki, S., Walker, D. W., Walker, M. J., Walker, S. A., Walter, J., Wandosell, F. G., Wang, B., Wang, C. -Y., Wang, C., Wang, D., Wang, F., Wang, G., Wang, H., Wang, H. -G., Wang, J., Wang, K., Wang, L., Wang, M. H., Wang, M., Wang, N., Wang, P., Wang, Q. J., Wang, Q., Wang, Q. K., Wang, Q. A., Wang, W. -T., Wang, W., Wang, X., Wang, Y., Wang, Y. -Y., Wang, Z., Warnes, G., Warnsmann, V., Watada, H., Watanabe, E., Watchon, M., Wawrzynska, A., Weaver, T. E., Wegrzyn, G., Wehman, A. M., Wei, H., Wei, L., Wei, T., Wei, Y., Weiergraber, O. H., Weihl, C. C., Weindl, G., Weiskirchen, R., Wells, A., Wen, R. H., Wen, X., Werner, A., Weykopf, B., Wheatley, S. P., Whitton, J. L., Whitworth, A. J., Wiktorska, K., Wildenberg, M. E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R. S. B., Williams, R. L., Williamson, P. R., Wilson, R. A., Winner, B., Winsor, N. J., Witkin, S. S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J. H., Wong, R. W., Wong, V. K. W., Wong, W. W. -L., Wu, A. -G., Wu, C., Wu, J., Wu, K. K., Wu, M., Wu, S. -Y., Wu, S., Wu, W. K. K., Wu, X., Wu, Y. -W., Wu, Y., Xavier, R. J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H. -T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C. -M., Xie, M., Xie, Y., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, L., Xu, W. W., Xu, X., Xue, Y., Yakhine-Diop, S. M. S., Yamaguchi, M., Yamaguchi, O., Yamamoto, A., Yamashina, S., Yan, S., Yan, S. -J., Yan, Z., Yanagi, Y., Yang, C., Yang, D. -S., Yang, H., Yang, H. -T., Yang, J. -M., Yang, J., Yang, L., Yang, M., Yang, P. -M., Yang, Q., Yang, S., Yang, S. -F., Yang, W., Yang, W. Y., Yang, X., Yang, Y., Yao, H., Yao, S., Yao, X., Yao, Y. -G., Yao, Y. -M., Yasui, T., Yazdankhah, M., Yen, P. M., Yi, C., Yin, X. -M., Yin, Y., Yin, Z., Ying, M., Ying, Z., Yip, C. K., Yiu, S. P. T., Yoo, Y. H., Yoshida, K., Yoshii, S. R., Yoshimori, T., Yousefi, B., Yu, B., Yu, H., Yu, J., Yu, L., Yu, M. -L., Yu, S. -W., Yu, V. C., Yu, W. H., Yu, Z., Yuan, J., Yuan, L. -Q., Yuan, S., Yuan, S. -S. F., Yuan, Y., Yuan, Z., Yue, J., Yue, Z., Yun, J., Yung, R. L., Zacks, D. N., Zaffagnini, G., Zambelli, V. O., Zanella, I., Zang, Q. S., Zanivan, S., Zappavigna, S., Zaragoza, P., Zarbalis, K. S., Zarebkohan, A., Zarrouk, A., Zeitlin, S. O., Zeng, J., Zeng, J. -D., Zerovnik, E., Zhan, L., Zhang, B., Zhang, D. D., Zhang, H., Zhang, H. -L., Zhang, J., Zhang, J. -P., Zhang, K. Y. B., Zhang, L. W., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X. -W., Zhang, X. D., Zhang, Y., Zhang, Y. -D., Zhang, Y. -Y., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X. -F., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X. -L., Zheng, Y., Zheng, Z. -G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, J., Zhou, K., Zhou, R., Zhou, X. -J., Zhou, Y., Zhou, Z. -Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G. -Q., Zhu, H., Zhu, W. -G., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C. M., Ziviani, E., Zoladek, T., Zong, W. -X., Zorov, D. B., Zorzano, A., Zou, W., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X. C., Kenchappa, C. S., Lin, Y., Oshima, S., Rong, Y., Sluimer, J. C., Stallings, C. L., Tong, C. -K., and Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Programmed cell death, Settore BIO/06, Autophagosome, Autolysosome, [SDV]Life Sciences [q-bio], lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Autophagy-Related Proteins, Review, Computational biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Settore MED/04, 03 medical and health sciences, stress, Chaperone-mediated autophagy, ddc:570, Autophagy, LC3, Animals, Humans, cancer, Settore BIO/10, flux, lysosome, macroautophagy, neurodegeneration, phagophore, vacuole, Set (psychology), Molecular Biology, 030102 biochemistry & molecular biology, business.industry, Interpretation (philosophy), Autophagosomes, Cell Biology, Multicellular organism, 030104 developmental biology, Knowledge base, Biological Assay, Lysosomes, business, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract: Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access) In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021
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13. LifeTime and improving European healthcare through cell-based interceptive medicine

Author: Rajewsky, Nikolaus, Almouzni, Geneviève, Gorski, Stanislaw A, et al, Becher, Burkhard, University of Zurich, Rajewsky, Nikolaus, Almouzni, Geneviève, and Gorski, Stanislaw A
Subjects: 1000 Multidisciplinary, 570 Life sciences, biology, 610 Medicine & health, 10263 Institute of Experimental Immunology
Published: 2020
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14. Electroanalysis of Enzyme Activity in Small Biological Samples: Alkaline Phosphatase

Author: Michael Bekhit, Waldemar Gorski, and Teresa Blazek
Subjects: musculoskeletal diseases, Chromatography, biology, medicine.diagnostic_test, Hydroquinone, Chemistry, Substrate (chemistry), Glassy carbon, Alkaline Phosphatase, Enzyme assay, Carbon, Analytical Chemistry, chemistry.chemical_compound, Linear range, biology.protein, medicine, Glucose test, Alkaline phosphatase, Humans, Biological Assay, Incubation, Electrodes, Enzyme Assays
Abstract: The discovery of sulfite-stabilized anodic current of hydroquinone (HQ) at high pH was used to develop two new methods for measuring the activity of the key biomarker alkaline phosphatase (ALP). Both approaches relied on the monitoring of ALP-triggered release of HQ from a substrate hydroquinone diphosphate (HQDP) into a pH 10.00 solution. One detected the released HQ via the internally calibrated electrochemical continuous enzyme assay (ICECEA) at a glassy carbon (GC) electrode with no sample incubation. The other used sample incubation with HQDP and quantified the released HQ via a coulometric assay at a commercial glucose test strip (GTS). The assay solution was optimized by investigating the ALP/HQDP/HQ system at a GC electrode. The ICECEA revealed high affinity of ALP for HQDP (Kmapp, 87 μM; Vmax, 0.36 μM min-1) and detected ALP down to 0.022 U L-1. At GTS, ALP was detected down to 0.064 U L-1 in a 1 μL sample of human serum after a 20 min incubation at room temperature. The linear range (R2, 0.994) extended at least up to 1.7 U L-1 ALP, which covered more than the clinical range for ALP in serum. The interferences from the sample matrix including those from indigenous glucose were eliminated using a charge difference ΔQ (=Qtotal - Qsample matrix) as a signal for ALP. Both advances proposed here are direct (no auxiliary enzymes or labels required), accurate (98 ± 3% ALP signal recovery), and precise (relative standard deviation (RSD)
Published: 2021

15. Exercise-induced angiogenesis is dependent on metabolically primed ATF3/4(+) endothelial cells

Author: Gillian Fitzgerald, Bart Ghesquière, Evi Masschelein, Christopher M. Adams, Abdiel Alvarado-Diaz, Tatiane Gorski, Paola Gilardoni, Tea Kocijan, Ge Tan, Raphaela Ardicoglu, Moheb Ghobrial, Katrien De Bock, Zheng Fan, Guillermo Turiel, Jing Zhang, University of Zurich, and De Bock, Katrien
Subjects: Adult, muscle angiogenesis, Physiology, Angiogenesis, Muscle Fibers, Skeletal, Neovascularization, Physiologic, 610 Medicine & health, 10071 Functional Genomics Center Zurich, Oxidative phosphorylation, amino acid metabolism, Article, 1307 Cell Biology, 03 medical and health sciences, endothelial metabolism, 0302 clinical medicine, 1312 Molecular Biology, medicine, Humans, 10239 Institute of Laboratory Animal Science, Glycolysis, single-cell RNA-Seq, exercise, endothelial heterogeneity, Muscle, Skeletal, Molecular Biology, 030304 developmental biology, 0303 health sciences, ATF3, Activating Transcription Factor 3, single-cell RNA-seq, Neovascularization, Pathologic, Chemistry, ATF4, Skeletal muscle, Endothelial Cells, 1314 Physiology, Cell Biology, Metabolism, Cell biology, Endothelial stem cell, medicine.anatomical_structure, 10036 Medical Clinic, 570 Life sciences, biology, 590 Animals (Zoology), 030217 neurology & neurosurgery
Abstract: Summary Exercise is a powerful driver of physiological angiogenesis during adulthood, but the mechanisms of exercise-induced vascular expansion are poorly understood. We explored endothelial heterogeneity in skeletal muscle and identified two capillary muscle endothelial cell (mEC) populations that are characterized by differential expression of ATF3/4. Spatial mapping showed that ATF3/4+ mECs are enriched in red oxidative muscle areas while ATF3/4low ECs lie adjacent to white glycolytic fibers. In vitro and in vivo experiments revealed that red ATF3/4+ mECs are more angiogenic when compared with white ATF3/4low mECs. Mechanistically, ATF3/4 in mECs control genes involved in amino acid uptake and metabolism and metabolically prime red (ATF3/4+) mECs for angiogenesis. As a consequence, supplementation of non-essential amino acids and overexpression of ATF4 increased proliferation of white mECs. Finally, deleting Atf4 in ECs impaired exercise-induced angiogenesis. Our findings illustrate that spatial metabolic angiodiversity determines the angiogenic potential of muscle ECs., Graphical abstract, Highlights • Capillary mEC populations have differential ATF3/4 and anabolic gene expression • ATF3/4+ ECs in oxidative muscle areas are metabolically primed for angiogenesis • Non-essential amino acids and ATF4 activation promote ATF3/4low WmEC proliferation • EC-specific loss of Atf4 impairs exercise-induced angiogenesis, Fan et al. discover two populations of muscle endothelial cells (mECs) that have differential ATF3/4 expression. Notably, ATF3/4+ mECs lie next to oxidative myofibers and have higher expression of amino acid metabolic genes, which metabolically prepare mECs for exercise-induced vascular expansion. Consequently, EC-specific loss of Atf4 impairs exercise-induced angiogenesis.
Published: 2021

16. Complete Genome Sequence of Enterobacter asburiae Strain AEB30, Determined Using Illumina and PacBio Sequencing

Author: Thao Dang-Hien Tran, Jeffery A. McGarvey, Steven Huynh, Craig T. Parker, Lisa Gorski, and Robert Hnasko
Subjects: Whole genome sequencing, Genetics, Immunology and Microbiology (miscellaneous), Strain (chemistry), Genome Sequences, Enterobacter asburiae, Biology, Molecular Biology
Abstract: The complete genome sequence of Enterobacter asburiae strain AEB30 is presented. The strain was isolated from store-bought ginger in Albany, CA, in 2016.
Published: 2021
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17. Histone deacetylase 9 promotes endothelial-mesenchymal transition and an unfavorable atherosclerotic plaque phenotype

Author: Przemek A. Gorski, Axelle Caudrillier, Valentin Fuster, Ha Won Kim, Laura Lecce, Maria Paola Santini, Emily Bernstein, Lijiang Ma, Simon Koplev, Jacob F. Bentzon, Yang Xu, Martin M. Bjørklund, Jason C. Kovacic, Bhargavi V’Gangula, Venu Pothula, Nirupama Chandel, Neal L. Weintraub, Johan L.M. Björkegren, Manfred Boehm, Valentina d'Escamard, Delaine K. Ceholski, and Andy Baker
Subjects: Mice, Knockout, ApoE, Endothelial cells, Cardiology, Histone Deacetylases, Mice, In vivo, Vascular Biology, medicine, Human Umbilical Vein Endothelial Cells, Animals, Humans, Epigenetics, Endothelium, biology, Mesenchymal stem cell, HDAC9, Fibrous cap, General Medicine, Atherosclerosis, Phenotype, Plaque, Atherosclerotic, Repressor Proteins, medicine.anatomical_structure, Histone, Cancer research, biology.protein, Ex vivo, Research Article
Abstract: Endothelial-mesenchymal transition (EndMT) is associated with various cardiovascular diseases and in particular with atherosclerosis and plaque instability. However, the molecular pathways that govern EndMT are poorly defined. Specifically, the role of epigenetic factors and histone deacetylases (HDACs) in controlling EndMT and the atherosclerotic plaque phenotype remains unclear. Here, we identified histone deacetylation, specifically that mediated by HDAC9 (a class IIa HDAC), as playing an important role in both EndMT and atherosclerosis. Using in vitro models, we found class IIa HDAC inhibition sustained the expression of endothelial proteins and mitigated the increase in mesenchymal proteins, effectively blocking EndMT. Similarly, ex vivo genetic knockout of Hdac9 in endothelial cells prevented EndMT and preserved a more endothelial-like phenotype. In vivo, atherosclerosis-prone mice with endothelial-specific Hdac9 knockout showed reduced EndMT and significantly reduced plaque area. Furthermore, these mice displayed a more favorable plaque phenotype, with reduced plaque lipid content and increased fibrous cap thickness. Together, these findings indicate that HDAC9 contributes to vascular pathology by promoting EndMT. Our study provides evidence for a pathological link among EndMT, HDAC9, and atherosclerosis and suggests that targeting of HDAC9 may be beneficial for plaque stabilization or slowing the progression of atherosclerotic disease.
Published: 2021
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18. A transcriptome-wide association study based on 27 tissues identifies 106 genes potentially relevant for disease pathology in age-related macular degeneration

Author: Strunz, Tobias, Lauwen, Susette, Kiel, Christina, Fritsche, Lars G., Igl, Wilmar, Bailey, Jessica N.Cooke, Grassmann, Felix, Sengupta, Sebanti, Bragg-Gresham, Jennifer L., Burdon, Kathryn P., Hebbring, Scott J., Wen, Cindy, Gorski, Mathias, Kim, Ivana K., Cho, David, Zack, Donald, Souied, Eric, Scholl, Hendrik P.N., Bala, Elisa, Lee, Kristine E., Hunter, David J., Sardell, Rebecca J., Mitchell, Paul, Merriam, Joanna E., Cipriani, Valentina, Hoffman, Joshua D., Schick, Tina, Lechanteur, Yara T.E., Guymer, Robyn H., Johnson, Matthew P., Jiang, Yingda, Stanton, Chloe M., Buitendijk, Gabriëlle H.S., Zhan, Xiaowei, Kwong, Alan M., Boleda, Alexis, Brooks, Matthew, Gieser, Linn, Ratnapriya, Rinki, Branham, Kari E., Foerster, Johanna R., Heckenlively, John R., Othman, Mohammad I., Vote, Brendan J., Liang, Helena Hai, Souzeau, Emmanuelle, Cree, Angela J., Goverdhan, Srinivas V., Moore, Emily L., Lotery, Andrew J., Epidemiology, Ophthalmology, Public Health, and Apollo - University of Cambridge Repository
Subjects: 0301 basic medicine, Pathology, medicine.medical_specialty, genetic structures, Gene regulatory network, lcsh:Medicine, Genome-wide association study, Pathogenesis, Disease, Biology, Quantitative trait, Sensory disorders Donders Center for Medical Neuroscience [Radboudumc 12], Article, Transcriptome, Macular Degeneration, 03 medical and health sciences, 0302 clinical medicine, SDG 3 - Good Health and Well-being, medicine, Humans, Gene Regulatory Networks, Genetic Predisposition to Disease, lcsh:Science, Gene, Genetic association study, Genetic association, Multidisciplinary, Molecular medicine, Gene Expression Profiling, lcsh:R, eye diseases, Computational biology and bioinformatics, Gene regulation, Gene expression profiling, 030104 developmental biology, Genes, Human genome, lcsh:Q, Gene expression, 030217 neurology & neurosurgery, Genome-Wide Association Study
Abstract: Contains fulltext : 218949.pdf (Publisher’s version ) (Open Access) Genome-wide association studies (GWAS) for late stage age-related macular degeneration (AMD) have identified 52 independent genetic variants with genome-wide significance at 34 genomic loci. Typically, such an approach rarely results in the identification of functional variants implicating a defined gene in the disease process. We now performed a transcriptome-wide association study (TWAS) allowing the prediction of effects of AMD-associated genetic variants on gene expression. The TWAS was based on the genotypes of 16,144 late-stage AMD cases and 17,832 healthy controls, and gene expression was imputed for 27 different human tissues which were obtained from 134 to 421 individuals. A linear regression model including each individuals imputed gene expression data and the respective AMD status identified 106 genes significantly associated to AMD variants in at least one tissue (Q-value < 0.001). Gene enrichment analysis highlighted rather systemic than tissue- or cell-specific processes. Remarkably, 31 of the 106 genes overlapped with significant GWAS signals of other complex traits and diseases, such as neurological or autoimmune conditions. Taken together, our study highlights the fact that expression of genes associated with AMD is not restricted to retinal tissue as could be expected for an eye disease of the posterior pole, but instead is rather ubiquitous suggesting processes underlying AMD pathology to be of systemic nature.
Published: 2020
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19. Identification of circulating microRNA signatures as potential biomarkers in the serum of elk infected with chronic wasting disease

Author: Damian Gorski, Megan Klassen, Claudio Soto, Michael B. Coulthart, Jessy A Slota, Sandra Pritzkow, Gordon Mitchell, Stephanie A. Booth, Catherine Robertson, Sarah J. Medina, and Christine Mesa
Subjects: Prions, animal diseases, Science, Scrapie, Disease, Biology, Article, 03 medical and health sciences, 0302 clinical medicine, Gene expression analysis, Cricetinae, microRNA, medicine, Animals, Gene Regulatory Networks, Circulating MicroRNA, KEGG, 030304 developmental biology, 0303 health sciences, Multidisciplinary, Transmission (medicine), Deer, Gene Expression Profiling, Molecular Sequence Annotation, Chronic wasting disease, medicine.disease, 3. Good health, Gene expression profiling, Immunology, Wasting Disease, Chronic, Medicine, Pathogens, 030217 neurology & neurosurgery, Biomarkers
Abstract: Chronic wasting disease (CWD) is an emerging infectious prion disorder that is spreading rapidly in wild populations of cervids in North America. The risk of zoonotic transmission of CWD is as yet unclear but a high priority must be to minimize further spread of the disease. No simple diagnostic tests are available to detect CWD quickly or in live animals; therefore, easily accessible biomarkers may be useful in identifying infected animals. MicroRNAs (miRNAs) are a class of small, non-coding RNA molecules that circulate in blood and are promising biomarkers for several infectious diseases. In this study we used next-generation sequencing to characterize the serum miRNA profiles of 35 naturally infected elk that tested positive for CWD in addition to 35 elk that tested negative for CWD. A total of 21 miRNAs that are highly conserved amongst mammals were altered in abundance in sera, irrespective of hemolysis in the samples. A number of these miRNAs have previously been associated with prion diseases. Receiver operating characteristic (ROC) curve analysis was performed to evaluate the discriminative potential of these miRNAs as biomarkers for the diagnosis of CWD. We also determined that a subgroup of 6 of these miRNAs were consistently altered in abundance in serum from hamsters experimentally infected with scrapie. This suggests that common miRNA candidate biomarkers could be selected for prion diseases in multiple species. Furthermore, Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analyses pointed to a strong correlation for 3 of these miRNAs, miR-148a-3p, miR-186-5p, miR-30e-3p, with prion disease.
Published: 2019

20. Use of Phyllosphere-associated Lactic Acid Bacteria as Biocontrol Agents to Reduce Salmonella enterica Serovar Poona Growth on Cantaloupe Melons

Author: Thao Dang-Hien Tran, Robert M. Hnasko, Lisa Gorski, and Jeffery A. McGarvey
Subjects: Serotype, 0303 health sciences, Salmonella, biology, 030306 microbiology, Lactococcus lactis, Virulence, biology.organism_classification, medicine.disease_cause, Microbiology, Lactic acid, 03 medical and health sciences, chemistry.chemical_compound, chemistry, Salmonella enterica, medicine, Phyllosphere, Bacteria, 030304 developmental biology, Food Science
Abstract: Foodborne illness associated with fresh, ready-to-eat produce continues to be a significant challenge to public health. In this study, we created a phyllosphere-associated lactic acid bacteria (PLAB) library and screened it via a high-throughput in vitro fluorescent assay to identify bacteria capable of inhibiting the growth of the pathogenic bacterium Salmonella enterica. One isolate, 14B4, inhibited the growth of S. enterica by >45-fold in vitro; it was able to grow and persist on the surfaces of cantaloupe melons at both ambient (25°C) and refrigerator (5°C) temperatures. Isolate 14B4 inhibited the growth of S. enterica on the surfaces of cantaloupes by >3 log when incubated at 25°C for 24 h and by >4 log when the cantaloupes were stored at 5°C for 3 days and the temperature was shifted to 25°C for 2 days. Genomic DNA sequence analysis of isolate 14B4 revealed that it was Lactococcus lactis and that it did not contain any known antibiotic biosynthesis gene clusters, antibiotic resistance genes, or genes encoding any known virulence factors. Organic acid analysis revealed that L. lactis produces substantial amounts of lactic acid, which is likely the inhibitory substance that reduced the growth of Salmonella on the cantaloupes.
Published: 2019
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21. Inhibition of the hyaluronan matrix enhances metabolic anticancer therapy by dichloroacetate in vitro and in vivo

Author: Inga Kretschmer, Daniel J. Gorski, Christina Reichert, Oliver Reiners, Sören Twarock, Katharina Bach, Maria Grandoch, Jens W. Fischer, and Katharina Gorges
Subjects: Male, 0301 basic medicine, Pyruvate dehydrogenase kinase, Esophageal Neoplasms, Mice, Nude, Antineoplastic Agents, Apoptosis, Mice, Structure-Activity Relationship, 03 medical and health sciences, 0302 clinical medicine, Nude mouse, In vivo, Immunochemistry, Tumor Cells, Cultured, Animals, Humans, Hyaluronic Acid, Cell Proliferation, Pharmacology, Dichloroacetic Acid, Dose-Response Relationship, Drug, Molecular Structure, biology, Chemistry, Cell growth, Neoplasms, Experimental, biology.organism_classification, Research Papers, Extracellular Matrix, Mitochondria, Disease Models, Animal, 030104 developmental biology, Anaerobic glycolysis, Cell culture, Cancer research, Regression Analysis, Esophageal Squamous Cell Carcinoma, Drug Screening Assays, Antitumor, Hymecromone, 030217 neurology & neurosurgery, Research Paper
Abstract: Background and purpose Aerobic glycolysis is a unique feature of tumour cells that entails several advantages for cancer progression such as resistance to apoptosis. The low MW compound, dichloroacetate, is a pyruvate dehydrogenase kinase inhibitor, which restores oxidative phosphorylation and induces apoptosis in a variety of cancer entities. However, its therapeutic effectiveness is limited by resistance mechanisms. This study aimed to examine the role of the anti-apoptotic hyaluronan (HA) matrix in this context and to identify a potential add-on treatment option to overcome this limitation. Experimental approach The metabolic connection between dichloroacetate treatment and HA matrix augmentation was analysed in vitro by quantitative PCR and affinity cytochemistry. Metabolic pathways were analysed using Seahorse, HPLC, fluorophore-assisted carbohydrate electrophoresis, colourimetry, immunoblots, and immunochemistry. The effects of combining dichloroacetate with the HA synthesis inhibitor 4-methylumbelliferone was evaluated in 2D and 3D cell cultures and in a nude mouse tumour xenograft regression model by immunoblot, immunochemistry, and FACS analysis. Key results Mitochondrial reactivation induced by dichloroacetate metabolically activated HA synthesis by augmenting precursors as well as O-GlcNAcylation. This process was blocked by 4-methylumbelliferone, resulting in enhanced anti-tumour efficacy in 2D and 3D cell culture and in a nude mouse tumour xenograft regression model. Conclusions and implications The HA rich tumour micro-environment represents a metabolic factor contributing to chemotherapy resistance. HA synthesis inhibition exhibited pronounced synergistic actions with dichloroacetate treatment on oesophageal tumour cell proliferation and survival in vitro and in vivo suggesting the combination of these two strategies is an effective anticancer therapy.
Published: 2019
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22. Impact of the Radiation Factor on Mean Survival Time for Chernobyl Clean-up Workers with Solid Cancer

Author: M. A. Maksioutov, E.V. Kochergina, K. A. Tumanov, V.K. Ivanov, and A.I. Gorski
Subjects: Pediatrics, medicine.medical_specialty, Solid cancer, Cancer, Biology, medicine.disease, General Biochemistry, Genetics and Molecular Biology, Mean Survival Time, Tumor stage, Cohort, medicine, Dosimetry, Exclusion zone, Stage (cooking), General Agricultural and Biological Sciences
Abstract: The aim of this study was to investigate the mean survival time for Chernobyl clean-up workers (liquidators) with diagnosed solid cancer. The cohort of liquidators contained 142 871 males who worked in the Chernobyl exclusion zone from 1986–1987. Individual medical and dosimetry information collected during the follow-up period from 1991 up to 2015 was used in the study. The number of liquidators cases with documented stages of the disease was 7652, the number of overall death cases among those liquidators was 5085 (4351 deaths were due to cancer). Mean survival time for liquidators after the diagnosis of solid cancer (ICD-10: C00-C80.9) and documented tumor stages between 2000 over 2015 was 4.73 years. For tumors of respiratory organs (ICD-10: C30-C39.9), the mean survival time was 2.57 years; for tumors of digestive organs (ICD-10: C15-C26.9), 3.55 years. The mean survival time for liquidators with a documented diagnosis of cancer was continuously increasing despite the cohort aging and the increase of total mortality. The relationship between the mean survival time and tumor stage was studied. The dependence of the mean survival time on the stage of the tumor was investigated. The survival time, when changing from the 1st stage to the 4th stage, decreased seven times (from 8.62 to 1.22 years). The relationship between the mean survival time and radiation dose received by a liquidator was studied. Two dose groups were identified: group 0–100 mGy (average dose: 56.6 mGy) and group 100+ mGy (average dose: 187.9 mGy). Mean survival time was 4.66 and 4.72 years and the difference between the values was insignificant. Studies carried out in the cohort with varying size and age provided actual estimates of the effects of technological factors on health of certain human populations and groups.
Published: 2019
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23. On the differences between mega‐ and meta‐imputation and analysis exemplified on the genetics of age‐related macular degeneration

Author: Bernhard H. F. Weber, Iris M. Heid, Mathias Gorski, Thomas W. Winkler, and Felix Günther
Subjects: Epidemiology, Genome-wide association study, Genomics, Computational biology, Biology, Mega, Polymorphism, Single Nucleotide, genome‐wide association studies, Genotype‐imputation, 03 medical and health sciences, Macular Degeneration, Age related, medicine, Humans, Genetic Predisposition to Disease, mega‐analysis, Genetics (clinical), Research Articles, 030304 developmental biology, Genetic association, 0303 health sciences, Models, Genetic, 030305 genetics & heredity, age‐related macular degeneration, Macular degeneration, medicine.disease, meta‐analysis, Genetic Loci, Meta-analysis, Chromosomes, Human, Pair 5, Imputation (genetics), Research Article, Genome-Wide Association Study
Abstract: While current genome‐wide association analyses often rely on meta‐analysis of study‐specific summary statistics, individual participant data (IPD) from multiple studies increase options for modeling. When multistudy IPD is available, however, it is unclear whether this data is to be imputed and modeled across all participants (mega‐imputation and mega‐analysis) or study‐specifically (meta‐imputation and meta‐analysis). Here, we investigated different approaches toward imputation and analysis using 52,189 subjects from 25 studies of the International Age‐related Macular Degeneration (AMD) Genomics Consortium including, 16,144 AMD cases and 17,832 controls for association analysis. From 27,448,454 genetic variants after 1,000‐Genomes‐based imputation, mega‐imputation yielded ~400,000 more variants with high imputation quality (mostly rare variants) compared to meta‐imputation. For AMD signal detection (P
Published: 2019

24. Perinatal phthalate and high-fat diet exposure induce sex-specific changes in adipocyte size and DNA methylation

Author: Hong Chen, Aleksandra Gorski, Laura Moody, Isabel Digan, Yuan Xiang Pan, Daniel G. Kougias, Janice M. Juraska, Aaron Hong, and Paul M. Jung
Subjects: Male, 0301 basic medicine, medicine.medical_specialty, Offspring, Endocrinology, Diabetes and Metabolism, Clinical Biochemistry, Phthalic Acids, Adipose tissue, 010501 environmental sciences, Biology, Diet, High-Fat, 01 natural sciences, Biochemistry, Article, 03 medical and health sciences, chemistry.chemical_compound, Sex Factors, Pregnancy, Internal medicine, Lactation, Adipocyte, Adipocytes, medicine, Animals, Rats, Long-Evans, Molecular Biology, Cell Size, 0105 earth and related environmental sciences, Lipoprotein lipase, Adipogenesis, Nutrition and Dietetics, Triglyceride, Body Weight, Phthalate, DNA Methylation, Frizzled Receptors, Receptors, Neurotransmitter, Lipoprotein Lipase, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, Animals, Newborn, Gene Expression Regulation, chemistry, Prenatal Exposure Delayed Effects, DNA methylation, Body Composition, Female
Abstract: Environmental factors such as diet and endocrine-disrupting chemicals have individually been shown to mediate metabolic function. However, the underlying mechanism by which the combination disrupts adipocyte morphology and fat storage remains unknown. The current study evaluated early-life programming by diet and phthalate exposure. During gestation and lactation, pregnant Long-Evans hooded rat dams were fed either a control (C) or high-fat (HF) diet and were orally administered one of three phthalate dosages (0, 200 or 1000 μg/kg/day), yielding six groups of offspring: C-0, C-200, C-1000, HF-0, HF-200 and HF-1000. On postnatal day (PND) 90, gonadal fat pads were collected and analyzed for histology, gene expression and DNA methylation. Differences in body weight were observed only in males. Hematoxylin and eosin staining revealed larger adipocyte size in HF-0 vs. C-0 females. Exposure to 200 or 1000 μg/kg/day phthalates modulated diet-induced changes in adipose morphology. Compared to C-0 females, HF-0 females also had higher expression of the adipogenesis gene Wnt receptor, frizzled 1 (Fzd1) and the triglyceride cleaving enzyme lipoprotein lipase (Lpl). These increases in gene expression were accompanied by lower DNA methylation surrounding the transcription start sites of the two genes. Diet-driven effects were observed in unexposed females but not in phthalate-treated rats. Results suggest a sex-specific association between perinatal HF diet and body weight, adipocyte size and DNA methylation. Perinatal phthalate exposure appears to produce a phenotype that more closely resembles HF-fed animals.
Published: 2019
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25. Complications of whole-exome sequencing for causal gene discovery in primary platelet secretion defects

Author: Anna Lecchi, Flora Peyvandi, Silvia La Marca, Andrea Cairo, Andrea Artoni, Marcin M. Gorski, Luca A. Lotta, Emanuela Pappalardo, and Eti A. Femia
Subjects: Adult, Male, Candidate gene, Pilot Projects, Hematology, Computational biology, Middle Aged, FCGR2A, Biology, Phenotype, Article, Platelet Biology & its Disorders, 03 medical and health sciences, 0302 clinical medicine, PRKCD, Child, Preschool, Exome Sequencing, Humans, Missense mutation, Female, Blood Platelet Disorders, Candidate Gene Analysis, Gene, Exome sequencing, 030215 immunology
Abstract: Primary platelet secretion defects constitute a heterogeneous group of functional defects characterized by reduced platelet granule secretion upon stimulation by different agonists. The clinical and laboratory heterogeneity of primary platelet secretion defects warrants a tailored approach. We performed a pilot study in order to develop DNA sequence analysis pipelines for gene discovery and to create a list of candidate causal genes for platelet secretion defects. Whole-exome sequencing analysis of 14 unrelated Italian patients with primary secretion defects and 16 controls was performed on Illumina HiSeq. Variant prioritization was carried out using two filtering approaches: identification of rare, potentially damaging variants in platelet candidate genes or by selecting singletons. To corroborate the results, exome sequencing was applied in a family in which platelet secretion defects and a bleeding diathesis were present. Platelet candidate gene analysis revealed gene defects in 10/14 patients, which included ADRA2A, ARHGAP1, DIAPH1, EXOC1, FCGR2A, ITPR1, LTBP1, PTPN7, PTPN12, PRKACG, PRKCD, RAP1GAP, STXBP5L, and VWF. The analysis of singletons identified additional gene defects in PLG and PHACTR2 in two other patients. The family analysis confirmed a missense variant p.D1144N in the STXBP5L gene and p.P83H in the KCNMB3 gene as potentially causal. In summary, exome sequencing revealed potential causal variants in 12 of 14 patients with primary platelet secretion defects, highlighting the limitations of the genomic approaches for causal gene identification in this heterogeneous clinical and laboratory phenotype.
Published: 2019
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26. Prion Dissemination through the Environment and Medical Practices: Facts and Risks for Human Health

Author: Sandra Pritzkow, Frank Ramirez, Claudio Soto, and Damian Gorski
Subjects: 0301 basic medicine, Microbiology (medical), General Immunology and Microbiology, Epidemiology, Transmission (medicine), Prions, animal diseases, Public Health, Environmental and Occupational Health, Computational biology, Review, Biology, nervous system diseases, Genetic Materials, Prion Diseases, 03 medical and health sciences, Human health, 030104 developmental biology, 0302 clinical medicine, Infectious Diseases, Animals, Humans, 030217 neurology & neurosurgery, Infectious agent
Abstract: Prion diseases are a group of fatal, infectious neurodegenerative disorders affecting various species of mammals, including humans. The infectious agent in these diseases, termed prion, is composed exclusively of a misfolded protein that can spread and multiply in the absence of genetic materials. In this article, we provide an overview of the mechanisms of prion replication, interindividual transmission, and dissemination in communities. In particular, we review the potential role of the natural environment in prion transmission, including the mechanisms and pathways for prion entry and accumulation in the environment as well as its roles in prion mutation, adaptation, evolution, and transmission. We also discuss the transmission of prion diseases through medical practices, scientific research, and use of biological products. Detailed knowledge of these aspects is crucial to limit the spreading of existing prion diseases as well as to prevent the emergence of new diseases with possible catastrophic consequences for public health.
Published: 2021

27. North American and Norwegian Chronic Wasting Disease Prions Exhibit Different Potential for Interspecies Transmission and Zoonotic Risk

Author: Frank Ramirez, Glenn C. Telling, Claudio Soto, Damian Gorski, Sandra Pritzkow, and Sylvie L. Benestad
Subjects: Norway, Prions, animal diseases, Deer, Chronic wasting disease, Biology, medicine.disease, Virology, Interspecies transmission, Major Articles and Brief Reports, Infectious Diseases, North America, medicine, Immunology and Allergy, Animals, Humans, Wasting Disease, Chronic, Prion Proteins
Abstract: Background Chronic wasting disease (CWD) is a rapidly spreading prion disorder affecting various species of wild and captive cervids. The risk that CWD poses to cohabiting animals or more importantly to humans is largely unknown. Methods In this study, we investigated differences in the capacity of CWD isolates obtained from 6 different cervid species to induce prion conversion in vitro by protein misfolding cyclic amplification. We define and quantify spillover and zoonotic potential indices as the efficiency by which CWD prions sustain prion generation in vitro at expenses of normal prion proteins from various mammals and human, respectively. Results Our data suggest that reindeer and red deer from Norway could be the most transmissible CWD prions to other mammals, whereas North American CWD prions were more prone to generate human prions in vitro. Conclusions Our results suggest that Norway and North American CWD prions correspond to different strains with distinct spillover and zoonotic potentials.
Published: 2021

28. Functionally Selective Signaling and Broad Metabolic Benefits by Novel Insulin Receptor Partial Agonists

Author: Geoffrey Walford, Julie Lao, Terri M. Kelly, Haihong Zhou, Danqing Feng, Stephen F. Previs, Songnian Lin, Ahmet Kekec, Ying Chen, Mark D. Erion, Margaret Wu, Ester Carballo-Jane, Peter Zafian, Dmitri A. Pissarnitski, Pei Huo, James Mu, Scott A. Hollingsworth, Lin Yan, David E. Kelley, Mindy Liu, Ge Dai, Yacob Gomez-Llorente, Judith N. Gorski, and Giovanna Scapin
Subjects: Insulin receptor, biology, Chemistry, biology.protein, Pharmacology, Partial agonist
Abstract: Since its debut a century ago, insulin therapies have saved many lives and are now routinely used by patients with diabetes to manage hyperglycemia. Exemplary early studies of insulin molecular pathways led to the realization of the critical roles of signaling transduction in mediating its pleiotropic actions. Multiple insulin analogs have been developed in the last few decades primarily focused on improving the time action profile without affecting ligand-receptor interaction or functional selectivity in downstream signaling. As a result, inherent liabilities of injectable insulins continue to limit insulin’s true therapeutic potential. For example, fear of hypoglycemia often leads to underdosing and inadequate glycemic control and, as a consequence, continued risk of diabetic complications. Efforts to develop hepatic targeted basal insulin analogs lead to reduced effect on skeletal muscle and lower hypoglycemic risk but failed to adequately suppress lipolysis. To achieve both functional selectivity and a more desirable pharmacological profile, we evaluated a series of covalent insulin dimers that act in cellular assays as insulin receptor partial agonists (IRPA). Structural studies revealed distinct insulin receptor interactions compared to insulin analogs. Furthermore, IRPAs were shown to induce biased signaling in cellular assays that supports the potential for reduced mitogenic and atherosclerotic activities compared to regular insulin. In vivo, IRPAs exhibit tissue preferential action that attenuates stimulation of skeletal muscle glucose uptake while retaining hepatic and adipose actions to regulate glucose production and lipolysis, respectively. These attributes are expected to significantly reduce the hypoglycemic risk while achieving similar glycemic control and less body weight gain relative to comparator insulin analogs in animal models. Furthermore, IRPA lessens receptor internalization resulting in a slower clearance and long duration of action across species, an optimal feature for a basal insulin. In summary, IRPA possesses the desired molecular features that are required to reduce the hypoglycemic risk while maintaining the broad metabolic benefits of insulin therapy and as such represents a potential transformative therapy for patients with diabetes.
Published: 2021
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29. A repeated triple lysine motif anchors complexes containing bone sialoprotein and the type XI collagen A1 chain involved in bone mineralization

Author: Jeffrey P. Gorski, Daniel Pernoud, Julia Thom Oxford, David R. Eyre, Andrew Keightley, and Nichole T. Franz
Subjects: 0301 basic medicine, Bone sialoprotein, collagen, Male, Nucleolus, Lysine, Peptide, confocal microscopy, Collagen Type XI, Biochemistry, bone, VR, variable region, Extracellular matrix, Column Buffer, 0.05 M sodium acetate buffer (pH 5.2) containing 8 M urea and 0.02% sodium azide, BSP, bone sialoprotein, CHAPS, (3-((3-cholamidopropyl) dimethylammonio)-1-propanesulfonate), chemistry.chemical_classification, biology, Chemistry, RNA-Binding Proteins, Fluoresceins, BGP, β-glycerolphosphate, Research Article, N-terminal domain, Immunoprecipitation, extracellular matrix, Sialoglycoproteins, bone sialoprotein, PVDF, polyvinylfluoride, Bone and Bones, BMF, biomineralization foci, 03 medical and health sciences, alternative splicing, Calcification, Physiologic, stomatognathic system, Extracellular, Animals, Integrin-Binding Sialoprotein, NTD, N-terminal domain, TBST, Tris-buffered saline containing Tween-20, Molecular Biology, cell culture, Osteoblasts, 030102 biochemistry & molecular biology, Cell Biology, type XI collagen, Phosphoproteins, Molecular biology, Rats, 030104 developmental biology, biology.protein, peptides, AEBSF, 4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride, Npp, N-propeptide, Osteopontin, Nucleolin, FAM, 6-carboxyfluorescein
Abstract: While details remain unclear, initiation of woven bone mineralization is believed to be mediated by collagen and potentially nucleated by bone sialoprotein (BSP). Interestingly, our recent publication showed that BSP and type XI collagen form complexes in mineralizing osteoblastic cultures. To learn more, we examined the protein composition of extracellular sites of de novo hydroxyapatite deposition which were enriched in BSP and Col11a1 containing an alternatively spliced "6b" exonal sequence. An alternate splice variant "6a" sequence was not similarly co-localized. BSP and Col11a1 co-purify upon ion-exchange chromatography or immunoprecipitation. Binding of the Col11a1 "6b" exonal sequence to bone sialoprotein was demonstrated with overlapping peptides. Peptide 3, containing three unique lysine-triplet sequences, displayed the greatest binding to osteoblastic cultures; peptides containing fewer lysine triplet motifs or derived from the "6a" exon yielded dramatically lower binding. Similar results were obtained with 6-carboxyfluorescein (FAM)-conjugated peptides and western blots containing extracts from osteoblastic cultures. Mass spectroscopic mapping demonstrated that FAM-peptide 3 bound to 90 kDa BSP and its 18 to 60 kDa fragments, as well as to 110 kDa nucleolin. In osteoblastic cultures, FAM-peptide 3 localized to biomineralization foci (site of BSP) and to nucleoli (site of nucleolin). In bone sections, biotin-labeled peptide 3 bound to sites of new bone formation which were co-labeled with anti-BSP antibodies. These results establish the fluorescent peptide 3 conjugate as the first nonantibody-based method to identify BSP on western blots and in/on cells. Further examination of the "6b" splice variant interactions will likely reveal new insights into bone mineralization during development.
Published: 2021

30. A catalog of genetic loci associated with kidney function from analyses of a million individuals

Author: Wuttke, Matthias, Li, Yong, Li, Man, Sieber, Karsten B., Feitosa, Mary F., Gorski, Mathias, Tin, Adrienne, Wang, Lihua, Chu, Audrey Y., Hoppmann, Anselm, Kirsten, Holger, Giri, Ayush, Chai, Jin-Fang, Sveinbjornsson, Gardar, Tayo, Bamidele O., Nutile, Teresa, Fuchsberger, Christian, Marten, Jonathan, Cocca, Massimiliano, Ghasemi, Sahar, Xu, Yizhe, Horn, Katrin, Noce, Damia, van der Most, Peter J., Sedaghat, Sanaz, Yu, Zhi, Akiyama, Masato, Afaq, Saima, Ahluwalia, Tarunveer S., Almgren, Peter, Amin, Najaf, Ärnlöv, Johan, Bakker, Stephan J. L., Bansal, Nisha, Baptista, Daniela, Bergmann, Sven, Biggs, Mary L., Biino, Ginevra, Boehnke, Michael, Boerwinkle, Eric, Boissel, Mathilde, Bottinger, Erwin P., Boutin, Thibaud S., Brenner, Hermann, Brumat, Marco, Burkhardt, Ralph, Butterworth, Adam S., Campana, Eric, Campbell, Archie, Campbell, Harry, Canouil, Mickaël, Carroll, Robert J., Catamo, Eulalia, Chambers, John C., Chee, Miao-Ling, Chee, Miao-Li, Chen, Xu, Cheng, Ching-Yu, Cheng, Yurong, Christensen, Kaare, Cifkova, Renata, Ciullo, Marina, Pina Concas, Maria, Cook, James P., Coresh, Josef, Corre, Tanguy, Sala, Cinzia Felicita, Cusi, Daniele, Danesh, John, Daw, E. Warwick, de Borst, Martin H., De Grandi, Alessandro, de Mutsert, Renée, de Vries, Aiko P. J., Degenhardt, Frauke, Delgado, Graciela, Demirkan, Ayse, Di Angelantonio, Emanuele, Dittrich, Katalin, Divers, Jasmin, Dorajoo, Rajkumar, Eckardt, Kai-Uwe, Ehret, Georg, Elliott, Paul, Endlich, Karlhans, Evans, Michele K., Felix, Janine F., Foo, Valencia Hui Xian, Franco, Oscar H., Franke, Andre, Freedman, Barry I., Freitag-Wolf, Sandra, Friedlander, Yechiel, Froguel, Philippe, Gansevoort, Ron T., Gao, He, Gasparini, Paolo, Gaziano, J. Michael, Giedraitis, Vilmantas, Gieger, Christian, Girotto, Giorgia, Giulianini, Franco, Gögele, Martin, Gordon, Scott D., Gudbjartsson, Daniel F., Gudnason, Vilmundur, Haller, Toomas, Hamet, Pavel, Harris, Tamara B., Hartman, Catharina A., Hayward, Caroline, Hellwege, Jacklyn N., Heng, Chew-Kiat, Hickst, Andrew A., Hofer, Edith, Huang, Wei, Hutri-Kähönen, Nina, Hwang, Shih-Jen, ikram, M. Arfan, indridason, Olafur S., Ingelsson, Erik, ising, Marcus, Jaddoe, Vincent W. V., Jakobsdottir, Johanna, Jonas, Jost B, Joshi, Peter K., Shilpa Josyula, Navya, Jung, Bettina, Kähönen, Mika, Kamatani, Yoichiro, Kammerer, Candace M., Kanai, Masahiro, Kastarinen, Mika, Kerr, Shona M., Khor, Chiea-Chuen, Kiess, Wieland, Kleber, Marcus E., Koenig, Wolfgang, Kooner, Jaspal S., Körner, Antje, Kovacs, Peter, Kraja, Aldi T., Krajcoviechova, Alena, Kramer, Holly, Krämer, Bernhard K., Kronenberg, Florian, Kubo, Michiaki, Kühnel, Brigitte, Kuokkanen, Mikko, Kuusisto, Johanna, La Bianca, Martina, Laakso, Markku, Lange, Leslie A., Langefeld, Carl D., Jen-Mai Lee, Jeannette, Lehne, Benjamin, Lehtimäki, Terho, Lieb, Wolfgang, Cohort Study, Lifelines, Lim, Su-Chi, Lind, Lars, Lindgren, Cecilia M., Liu, Jun, Liu, Jianjun, Loeffler, Markus, Loos, Ruth J. F., Lucae, Susanne, Ann Lukas, Mary, Lyytikäinen, Leo-Pekka, Mägi, Reedik, Magnusson, Patrik K. E., Mahajan, Anubha, Martin, Nicholas G., Martins, Jade, März, Winfried, Mascalzoni, Deborah, Matsuda, Koichi, Christa Meisinger, Meitinger, Thomas, Melander, Olle, Metspalu, Andres, Mikaelsdottir, Evgenia K., Milaneschi, Yuri, Miliku, Kozeta, Mishra, Pashupati P., Veteran Program, V. A. Million, Mohlke, Karen L., Mononen, Nina, Montgomery, Grant W., Mook-Kanamori, Dennis O., Mychaleckyj, Josyf C., Nadkarni, Girish N, Nalls, Mike A., Nauck, Matthias, Nikus, Kjell, Ning, Boting, Nolte, ilja M., Noordam, Raymond, O’Connell, Jeffrey, O’Donoghue, Michelle L., Olafsson, Isleifur, Oldehinkel, Albertine J., Orho-Melander, Marju, Ouwehand, Willem H., Padmanabhan, Sandosh, Palmer, Nicholette D., Palsson, Runolfur, Penninx, Brenda W. J. H., Perls, Thomas, Perola, Markus, Pirastu, Mario, Pirastu, Nicola, Pistis, Giorgio, Podgornaia, Anna I., Polasek, Ozren, Ponte, Belen, Porteous, David J., Poulain, Tanja, Pramstaller, Peter P., Preuss, Michael H., Prins, Bram P., Province, Michael A., Rabelink, Ton J., Raffield, Laura M., Raitakari, Olli T., Reilly, Dermot F., Rettig, Rainer, Rheinberger, Myriam, Rice, Kenneth M., Ridker, Paul M., Rivadeneira, Fernando, Rizzi, Federica, Roberts, David J., Robino, Antonietta, Rossing, Peter, Rudan, Igor, Rueedi, Rico, Ruggiero, Daniela, Ryan, Kathleen A., Saba, Yasaman, Sabanayagam, Charumathi, Salomaa, Veikko, Salvi, Erika, Saum, Kai-Uwe, Schmidt, Helena, Schmidt, Reinhold, Schöttker, Ben, Schulz, Christina-Alexandra, Schupf, Nicole, Shaffer, Christian M., Shi, Yuan, Smith, Albert V., Smith, Blair H., Soranzo, Nicole, Spracklen, Cassandra N., Strauch, Konstantin, Stringham, Heather M., Stumvoll, Michael, Svensson, Per O., Szymczak, Silke, Tai, E-Shyong, Tajuddin, Salman M., Tan, Nicholas Y. Q., Taylor, Kent D., Teren, Andrej, Tham, Yih-Chung, Thiery, Joachim, Thio, Chris H. L., Thomsen, Hauke, Thorleifsson, Gudmar, Toniolo, Daniela, Tönjes, Anke, Tremblay, Johanne, Tzoulaki, Ioanna, Uitterlinden, André G., Vaccargiu, Simona, van Dam, Rob M., van der Harst, Pim, van Duijn, Cornelia M., Velez Edward, Digna R., Verweij, Niek, Vogelezang, suzanne, Völker, üwe, Vollenweider, Peter, Waeber, Gerard, Waldenberger, Melanie, Wallentin, Lars, Wang, Ya Xing, Wang, Chaolong, Waterworth, Dawn M., Bin Wei, Wen, White, Harvey, Whitfield, John B., Wild, Sarah H., Wilson, James F., Wojczynski, Mary K., Wong, Charlene, Wong, Tien-Yin, Xu, Liang, Yang, Qiong, Yasuda, Masayuki, Yerges-Armstrong, Laura M., Zhang, Weihua, Zonderman, Alan B., Rotter, Jerome I., Bochud, Murielle, Psaty, Bruce M., Vitart, Veronique, Wilson, James G., Dehghan, Abbas, Parsa, Afshin, Chasman, Daniel I., Ho, Kevin, Morris, Andrew P., Devuyst, Olivier, Akilesh, Shreeram, Pendergrass, Sarah A., Sim, Xueling, Böger, Carsten A., Okada, Yukinori, Edwards, Todd L., Snieder, Harold, Stefansson, Kari, Hung, Adriana M., Heid, Iris M., Markus Scholz, Teumer, Alexander, Köttgen, Anna, Pattaro, Cristian, Groningen Institute for Organ Transplantation (GIOT), Lifestyle Medicine (LM), Groningen Kidney Center (GKC), Cardiovascular Centre (CVC), Interdisciplinary Centre Psychopathology and Emotion regulation (ICPE), Life Course Epidemiology (LCE), Internal Medicine, Epidemiology, Erasmus MC other, Pediatrics, Psychiatry, APH - Mental Health, APH - Digital Health, Wuttke, M, Li, Y, Li, M, Sieber, Kb, Feitosa, Mf, Gorski, M, Tin, A, Wang, L, Chu, Ay, Hoppmann, A, Kirsten, H, Giri, A, Chai, Jf, Sveinbjornsson, G, Tayo, Bo, Nutile, T, Fuchsberger, C, Marten, J, Cocca, M, Ghasemi, S, Xu, Y, Horn, K, Noce, D, van der Most, Pj, Sedaghat, S, Yu, Z, Akiyama, M, Afaq, S, Ahluwalia, T, Almgren, P, Amin, N, Ärnlöv, J, Bakker, Sjl, Bansal, N, Baptista, D, Bergmann, S, Biggs, Ml, Biino, G, Boehnke, M, Boerwinkle, E, Boissel, M, Bottinger, Ep, Boutin, T, Brenner, H, Brumat, M, Burkhardt, R, Butterworth, A, Campana, Eric, Campbell, A, Campbell, H, Canouil, M, Carroll, Rj, Catamo, E, Chambers, Jc, Chee, Ml, Chen, X, Cheng, Cy, Cheng, Y, Christensen, K, Cifkova, R, Ciullo, M, Concas, Mp, Cook, Jp, Coresh, J, Corre, T, Sala, Cf, Cusi, D, Danesh, J, Daw, Ew, de Borst, Mh, De Grandi, A, de Mutsert, R, de Vries, Apj, Degenhardt, F, Delgado, G, Demirkan, A, Di Angelantonio, E, Dittrich, K, Divers, J, Dorajoo, R, Eckardt, Ku, Ehret, G, Elliott, P, Endlich, K, Evans, Mk, Felix, Jf, Foo, Vhx, Franco, Oh, Franke, A, Freedman, Bi, Freitag-Wolf, S, Friedlander, Y, Froguel, P, Gansevoort, Rt, Gao, H, Gasparini, P, Gaziano, Jm, Giedraitis, V, Gieger, C, Girotto, G, Giulianini, F, Gögele, M, Gordon, Sd, Gudbjartsson, Df, Gudnason, V, Haller, T, Hamet, P, Harris, Tb, Hartman, Ca, Hayward, C, Hellwege, Jn, Heng, Ck, Hicks, Aa, Hofer, E, Huang, W, Hutri-Kähönen, N, Hwang, Sj, Ikram, Ma, Indridason, O, Ingelsson, E, Ising, M, Jaddoe, Vwv, Jakobsdottir, J, Jonas, Jb, Joshi, Pk, Josyula, N, Jung, B, Kähönen, M, Kamatani, Y, Kammerer, Cm, Kanai, M, Kastarinen, M, Kerr, Sm, Khor, Cc, Kiess, W, Kleber, Me, Koenig, W, Kooner, J, Körner, A, Kovacs, P, Kraja, At, Krajcoviechova, A, Kramer, H, Krämer, Bk, Kronenberg, F, Kubo, M, Kühnel, B, Kuokkanen, M, Kuusisto, J, La Bianca, M, Laakso, M, Lange, La, Langefeld, Cd, Lee, Jj, Lehne, B, Lehtimäki, T, Lieb, W, Lifelines Cohort, Study, Lim, Sc, Lind, L, Lindgren, Cm, Liu, J, Loeffler, M, Loos, Rjf, Lucae, S, Lukas, Ma, Lyytikäinen, Lp, Mägi, R, Magnusson, Pke, Mahajan, A, Martin, Ng, Martins, J, März, W, Mascalzoni, D, Matsuda, K, Meisinger, C, Meitinger, T, Melander, O, Metspalu, A, Mikaelsdottir, Ek, Milaneschi, Y, Miliku, K, Mishra, Pp, V. A., Million Veteran Program, Mohlke, Kl, Mononen, N, Montgomery, Gw, Mook-Kanamori, Do, Mychaleckyj, Jc, Nadkarni, Gn, Nalls, Ma, Nauck, M, Nikus, K, Ning, B, Nolte, Im, Noordam, R, O'Connell, J, O'Donoghue, Ml, Olafsson, I, Oldehinkel, Aj, Orho-Melander, M, Ouwehand, Wh, Padmanabhan, S, Palmer, Nd, Palsson, R, Penninx, Bwjh, Perls, T, Perola, M, Pirastu, M, Pirastu, N, Pistis, G, Podgornaia, Ai, Polasek, O, Ponte, B, Porteous, Dj, Poulain, T, Pramstaller, Pp, Preuss, Mh, Prins, Bp, Province, Ma, Rabelink, Tj, Raffield, Lm, Raitakari, Ot, Reilly, Df, Rettig, R, Rheinberger, M, Rice, Km, Ridker, Pm, Rivadeneira, F, Rizzi, F, Roberts, Dj, Robino, A, Rossing, P, Rudan, I, Rueedi, R, Ruggiero, D, Ryan, Ka, Saba, Y, Sabanayagam, C, Salomaa, V, Salvi, E, Saum, Ku, Schmidt, H, Schmidt, R, Schöttker, B, Schulz, Ca, Schupf, N, Shaffer, Cm, Shi, Y, Smith, Av, Smith, Bh, Soranzo, N, Spracklen, Cn, Strauch, K, Stringham, Hm, Stumvoll, M, Svensson, Po, Szymczak, S, Tai, E, Tajuddin, Sm, Tan, Nyq, Taylor, Kd, Teren, A, Tham, Yc, Thiery, J, Thio, Chl, Thomsen, H, Thorleifsson, G, Toniolo, D, Tönjes, A, Tremblay, J, Tzoulaki, I, Uitterlinden, Ag, Vaccargiu, S, van Dam, Rm, van der Harst, P, van Duijn, Cm, Velez Edward, Dr, Verweij, N, Vogelezang, S, Völker, U, Vollenweider, P, Waeber, G, Waldenberger, M, Wallentin, L, Wang, Yx, Wang, C, Waterworth, Dm, Bin Wei, W, White, H, Whitfield, Jb, Wild, Sh, Wilson, Jf, Wojczynski, Mk, Wong, C, Wong, Ty, Xu, L, Yang, Q, Yasuda, M, Yerges-Armstrong, Lm, Zhang, W, Zonderman, Ab, Rotter, Ji, Bochud, M, Psaty, Bm, Vitart, V, Wilson, Jg, Dehghan, A, Parsa, A, Chasman, Di, Ho, K, Morris, Ap, Devuyst, O, Akilesh, S, Pendergrass, Sa, Sim, X, Böger, Ca, Okada, Y, Edwards, Tl, Snieder, H, Stefansson, K, Hung, Am, Heid, Im, Scholz, M, Teumer, A, Köttgen, A, and Pattaro, C.
Subjects: catalog, Inheritance Patterns, Hasso-Plattner-Institut für Digital Engineering GmbH, Genome-wide association study, Disease, Kidney Function Tests, Bioinformatics, DISEASE, 0302 clinical medicine, Uromodulin/urine, kidney function, 11 Medical and Health Sciences, Genetics & Heredity, ddc:616, 0303 health sciences, Kidney, Genome-wide association, HERITABILITY, GENOME-WIDE ASSOCIATION, COMMON VARIANTS, RENAL-FUNCTION, TRANS-EQTLS, METAANALYSIS, TRANSPORTER, CLASSIFICATION, INTEGRATION, Chromosome Mapping, 3. Good health, Phenotype, medicine.anatomical_structure, Medical genetics, Common variants, Renal function, Trans-EQTLS, Metaanalysis, Heritability, Transporter, Life Sciences & Biomedicine, Glomerular Filtration Rate, Metaanalysi, medicine.medical_specialty, Genotype, European Continental Ancestry Group, Quantitative Trait Loci, Common variant, Quantitative trait locus, Biology, Polymorphism, Single Nucleotide, Article, White People, V. A. Million Veteran Program, 03 medical and health sciences, Quantitative Trait, Heritable, Lifelines Cohort Study, Uromodulin, Genetics, medicine, Humans, Genetic Predisposition to Disease, Renal Insufficiency, Chronic, Genetic Association Studies, 030304 developmental biology, Genetic association, Science & Technology, urogenital system, association, genetic loci, 06 Biological Sciences, medicine.disease, Renal Insufficiency, Chronic/genetics/physiopathology/urine, Genetic Association Studies/methods, ddc:000, 030217 neurology & neurosurgery, Developmental Biology, Genome-Wide Association Study, Kidney disease
Abstract: Chronic kidney disease (CKD) is responsible for a public health burden with multi-systemic complications. Through trans-ancestry meta-analysis of genome-wide association studies of estimated glomerular filtration rate (eGFR) and independent replication (n = 1,046,070), we identified 264 associated loci (166 new). Of these, 147 were likely to be relevant for kidney function on the basis of associations with the alternative kidney function marker blood urea nitrogen (n = 416,178). Pathway and enrichment analyses, including mouse models with renal phenotypes, support the kidney as the main target organ. A genetic risk score for lower eGFR was associated with clinically diagnosed CKD in 452,264 independent individuals. Colocalization analyses of associations with eGFR among 783,978 European-ancestry individuals and gene expression across 46 human tissues, including tubulo-interstitial and glomerular kidney compartments, identified 17 genes differentially expressed in kidney. Fine-mapping highlighted missense driver variants in 11 genes and kidney-specific regulatory variants. These results provide a comprehensive priority list of molecular targets for translational research.
Published: 2019
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31. The Comparative Methylome and Transcriptome After Change of Direction Compared to Straight Line Running Exercise in Human Skeletal Muscle

Author: Mohd-Firdaus Maasar, Daniel C. Turner, Piotr P. Gorski, Robert A. Seaborne, Juliette A. Strauss, Sam O. Shepherd, Matt Cocks, Nicolas J. Pillon, Juleen R. Zierath, Andrew T. Hulton, Barry Drust, and Adam P. Sharples
Subjects: 0301 basic medicine, AMPK, medicine.medical_specialty, PGC1 alpha, Physiology, NR4A3, Biology, lcsh:Physiology, Transcriptome, RC1200, 03 medical and health sciences, 0302 clinical medicine, change of direction, Physiology (medical), Internal medicine, medicine, Aerobic exercise, Exertion, Original Research, DNA methylation, lcsh:QP1-981, Skeletal muscle, MAPK, VEGF, 030104 developmental biology, Endocrinology, medicine.anatomical_structure, Sprint, Exercise intensity, PPARGC1A, High-intensity interval training, 030217 neurology & neurosurgery, NR4A1 (Nur77)
Abstract: The methylome and transcriptome signatures following exercise that are physiologically and metabolically relevant to sporting contexts such as team sports or health prescription scenarios (e.g., high intensity interval training/HIIT) has not been investigated. To explore this, we performed two different sport/exercise relevant high-intensity running protocols in five male sport team members using a repeated measures design of: (1) change of direction (COD) versus; (2) straight line (ST) running exercise with a wash-out period of at least 2 weeks between trials. Skeletal muscle biopsies collected from the vastus lateralis 30 min and 24 h post exercise, were assayed using 850K methylation arrays and a comparative analysis with recent (subject-unmatched) sprint and acute aerobic exercise meta-analysis transcriptomes was performed. Despite COD and ST exercise being matched for classically defined intensity measures (speed × distance and number of accelerations/decelerations), COD exercise elicited greater movement (GPS-Playerload), physiological (HR), metabolic (lactate) as well as central and peripheral (differential RPE) exertion measures compared with ST exercise, suggesting COD exercise evoked a higher exercise intensity. The exercise response alone across both conditions evoked extensive alterations in the methylome 30 min and 24 h post exercise, particularly in MAPK, AMPK and axon guidance pathways. COD evoked a considerably greater hypomethylated signature across the genome compared with ST exercise, particularly at 30 min post exercise, enriched in: Protein binding, MAPK, AMPK, insulin, and axon guidance pathways. Comparative methylome analysis with sprint running transcriptomes identified considerable overlap, with 49% of genes that were altered at the expression level also differentially methylated after COD exercise. After differential methylated region analysis, we observed that VEGFA and its downstream nuclear transcription factor, NR4A1 had enriched hypomethylation within their promoter regions. VEGFA and NR4A1 were also significantly upregulated in the sprint transcriptome and meta-analysis of exercise transcriptomes. We also confirmed increased gene expression of VEGFA, and considerably larger increases in the expression of canonical metabolic genes PPARGC1A (that encodes PGC1-α) and NR4A3 in COD vs. ST exercise. Overall, we demonstrate that increased physiological/metabolic load via COD exercise in human skeletal muscle evokes considerable epigenetic modifications that are associated with changes in expression of genes responsible for adaptation to exercise.
Published: 2021
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32. Meta-analysis uncovers genome-wide significant variants for rapid kidney function decline

Author: Lukas Habegger, Charumathi Sabanayagam, Michael Preuss, Laura M. Raffield, Mary F. Feitosa, Bamidele O. Tayo, Kevin Ho, Leo-Pekka Lyytikäinen, Florian Kronenberg, Valencia Hui Xian Foo, Adrienne Tin, Michael Cantor, Nisha Bansal, Tarunveer S. Ahluwalia, Melanie Waldenberger, Sarah A. Pendergrass, Behrooz Z. Alizadeh, Wolfgang Koenig, Qiong Yang, Xiaodong Bai, Christoph Wanner, Ben Schöttker, Giovanni Coppola, A. R. Shuldiner, Leslie A. Lange, Piyush Gampawar, Markus Scholz, Tien Yin Wong, Mary L. Biggs, Morris Swertz, Alicia Hawes, Girish N. Nadkarni, Christina-Alexandra Schulz, Chiea Chuen Khor, Ricardo H. Ulloa, Jeffrey C. Staples, Miao-Li Chee, Laura M. Yerges-Armstrong, Andrew Blumenfeld, Karlhans Endlich, Bernhard Banas, Bruce H.R. Wolffenbuttel, Kai-Uwe Eckardt, Pavel Hamet, Carsten A. Böger, Harold Snieder, Marcus B. Jones, Judy Wang, Shih-Jen Hwang, Mathias Gorski, Anselm Hoppmann, Josyf C. Mychaleckyj, Bernd Holleczek, Pamela R. Matias-Garcia, Rainer Rettig, Karsten B. Sieber, Manasi Pradhan, Pashupati P. Mishra, Peter Rossing, Matthias Wuttke, Miao-Ling Chee, H. Marike Boezen, Yong Li, M. Arfan Ikram, Jeffrey G. Reid, Teresa Nutile, Maria Sotiropoulos Padilla, Lude Franke, Robert J. Carroll, Luca A. Lotta, Bernhard K. Krämer, Kjell Nikus, Jerome I. Rotter, Thomas Meitinger, Lars Wallentin, Cisca Wijmenga, Kent D. Taylor, Holly Kramer, Louis Widom, Olli T. Raitakari, Marcus E. Kleber, Man Li, Nina Hutri-Kähönen, Massimiliano Cocca, Reinhold Schmidt, John D. Overton, Cristian Pattaro, Michael Lattari, Sarah E. Wolf, Jin-Fang Chai, Karina Toledo, Brigitte Kühnel, Zhenhua Gu, Peter Almgren, Caitlin Forsythe, Yuri Milaneschi, Stephan J. L. Bakker, Layal Chaker, Dawn M. Waterworth, Silke Szymczak, James G. Wilson, Peter J. van der Most, Michelle L. O'Donoghue, William Salerno, Masayuki Yasuda, Sahar Ghasemi, Eric Boerwinkle, Josef Coresh, Ilja M. Nolte, Kia Manoochehri, Konstantin Strauch, Thomas D. Schleicher, Myriam Rheinberger, Audrey Y. Chu, Sanaz Sedaghat, Sandra Freitag-Wolf, Boting Ning, Matthias Nauck, Christina Beechert, Helena Schmidt, Harvey D. White, Nina Mononen, Johanne Tremblay, Navya Shilpa Josyula, Mika Kähönen, Katrin Horn, Andre Franke, Marianne Rots, Bettina Jung, Alexander R. Rosenkranz, Christian M. Shaffer, Mary Ann Lukas, Gerjan Navis, Christian Gieger, John Chalmers, Shareef Khalid, Uwe Völker, Marju Orho-Melander, Iris M. Heid, Brenda W.J.H. Penninx, A. Baras, Alexander Lopez, Evan Maxwell, Ruth J. F. Loos, Erin D. Fuller, Christa Meisinger, Gonçalo R. Abecasis, Suganthi Balasubramanian, Chris H. L. Thio, Martin H. de Borst, Stefan Coassin, Ching-Yu Cheng, Wolfgang Lieb, Kenneth Rice, Alexander Teumer, Mark Woodward, Gisu Eom, Hermann Brenner, Thomas W. Winkler, Anna Köttgen, Edith Hofer, Aris Economides, Ron T. Gansevoort, Pim van der Harst, Lyndon J. Mitnaul, Bruce M. Psaty, Erwin P. Bottinger, Olle Melander, Niek Verweij, Frauke Degenhardt, Yan Zhang, Mohsen Ghanbari, Veronika Wanner, Terho Lehtimäki, Leland Barnard, Tampere University, Primary Health Care, Department of Paediatrics, Clinical Medicine, Department of Clinical Physiology and Nuclear Medicine, Department of Clinical Chemistry, TAYS Heart Centre, Groningen Institute for Organ Transplantation (GIOT), Groningen Kidney Center (GKC), Cardiovascular Centre (CVC), Life Course Epidemiology (LCE), Department of Marketing Management, Epidemiology, Internal Medicine, Psychiatry, Amsterdam Neuroscience - Complex Trait Genetics, Amsterdam Neuroscience - Mood, Anxiety, Psychosis, Stress & Sleep, APH - Mental Health, and APH - Digital Health
Subjects: 0301 basic medicine, medicine.medical_specialty, Genome-wide association study, 030232 urology & nephrology, Protein Disulfide-Isomerases, Hasso-Plattner-Institut für Digital Engineering GmbH, Renal function, Locus (genetics), Biology, AMP-Activated Protein Kinases, Kidney, 3121 Internal medicine, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, end-stage kidney disease, rapid eGFRcrea decline, Urologi och njurmedicin, medicine, Humans, Urology and Nephrology, ddc:610, Allele, Genetic association, Genetics, Creatinine, genome-wide association study, Acute kidney injury, acute kidney injury, medicine.disease, United Kingdom, ddc, 030104 developmental biology, chemistry, Nephrology, Medical genetics, 3111 Biomedicine, 610 Medizin und Gesundheit, Glomerular Filtration Rate
Abstract: Rapid decline of glomerular filtration rate estimated from creatinine (eGFRcrea) is associated with severe clinical endpoints. In contrast to cross-sectionally assessed eGFRcrea, the genetic basis for rapid eGFRcrea decline is largely unknown. To help define this, we meta-analyzed 42 genome-wide association studies from the Chronic Kidney Diseases Genetics Consortium and United Kingdom Biobank to identify genetic loci for rapid eGFRcrea decline. Two definitions of eGFRcrea decline were used: 3 mL/min/1.73m(2)/year or more ("Rapid3"; encompassing 34,874 cases, 107,090 controls) and eGFRcrea decline 25% or more and eGFRcrea under 60 mL/min/1.73m(2) at follow-up among those with eGFRcrea 60 mL/min/1.73m(2) or more at baseline ("CKDi25"; encompassing 19,901 cases, 175,244 controls). Seven independent variants were identified across six loci for Rapid3 and/or CKDi25: consisting of five variants at four loci with genome-wide significance (near UMOD-PDILT (2), PRKAG2, WDR72, OR2S2) and two variants among 265 known eGFRcrea variants (near GATM, LARP4B). All these loci were novel for Rapid3 and/or CKDi25 and our bioinformatic follow-up prioritized variants and genes underneath these loci. The OR2S2 locus is novel for any eGFRcrea trait including interesting candidates. For the five genome-wide significant lead variants, we found supporting effects for annual change in blood urea nitrogen or cystatin-based eGFR, but not for GATM or (LARP4B). Individuals at high compared to those at low genetic risk (8-14 vs. 0-5 adverse alleles) had a 1.20-fold increased risk of acute kidney injury (95% confidence interval 1.08-1.33). Thus, our identified loci for rapid kidney function decline may help prioritize therapeutic targets and identify mechanisms and individuals at risk for sustained deterioration of kidney function., Zweitveröffentlichungen der Universität Potsdam : Reihe der Digital Engineering Fakultät; 19
Published: 2021
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33. Growth and Survival of Attached Listeria on Lettuce and Stainless Steel Varies by Strain and Surface Type

Author: Kelly F. Romanolo, Sophia Kathariou, Samarpita Walker, and Lisa Gorski
Subjects: Serotype, Listeria, Colony Count, Microbial, Surface type, medicine.disease_cause, Microbiology, Bacterial Adhesion, 03 medical and health sciences, Listeria monocytogenes, medicine, Food science, Pathogen, 030304 developmental biology, 0303 health sciences, Strain (chemistry), biology, Foodborne pathogen, 030306 microbiology, Chemistry, fungi, Lettuce, biology.organism_classification, Stainless Steel, Biofilms, Food Microbiology, Food Science
Abstract: The foodborne pathogen Listeria monocytogenes lives as a saprophyte in nature and can adhere to and grow on surfaces as diverse as leaves, sediment, and stainless steel. To discern the mechanisms used by L. monocytogenes for attachment and growth on various surfaces, we studied interactions between the pathogen on lettuce and stainless steel. A panel of 24 strains (23 L. monocytogenes and 1 Listeria innocua) were screened for attachment and growth on lettuce at 4 and 25°C and on stainless steel at 10 and 37°C. Overnight growth of attached cells resulted in a 0- to 3-log increase on lettuce, depending on the strain and the temperature. Among the worst-performing strains on lettuce were two from a large cantaloupe outbreak, indicating that factors important for interactions with cantaloupe may be different from those required on lettuce tissue. Strains that grew the best on lettuce belonged to serotypes 1/2a, 1/2b, and 4b and were from cheese, potatoes, and water-sediment near produce fields. Confocal microscopy of L. monocytogenes tagged with constitutively expressed green fluorescent protein indicated associations with the cut edges and veins of lettuce leaves. On stainless steel coupons, there was a 5- to 7-log increase at 10°C after 7 days and a 4- to 7-log increase at 37°C after 40 h. Statistically, surface growth on stainless steel was better for serotype 1/2a than for serotype 4b strains, even though certain serotype 4b strains grew well on the coupons. The latter included strains that originated from produce and water-sediment. Some strains were fit in both environments, whereas others showed variability between the two different surfaces. Further analysis of these strains should reveal molecular factors needed for adherence and surface growth of L. monocytogenes on different biotic and abiotic surfaces. HIGHLIGHTS
Published: 2020

34. Serotype Assignment by Sero-agglutination, ELISA, and PCR

Author: Lisa Gorski
Subjects: Serotype, Antiserum, Whole genome sequencing, Biology, medicine.disease_cause, biology.organism_classification, Virology, Subtyping, law.invention, Agglutination (biology), Listeria monocytogenes, law, medicine, Listeria, Polymerase chain reaction
Abstract: For assessing isolates of Listeria monocytogenes, serotype designation is the first subtyping method used. Methodologies used to assign serotype are currently evolving and will eventually be replaced with whole genome sequencing. Traditionally, serotyping has been done with agglutination reactions; however, alternative methods utilizing enzyme linked immunosorbent assay (ELISA) and polymerase chain reaction (PCR) are common. Described here are the three non-genomic methods and the advantages and disadvantages of each.
Published: 2020
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35. DNA methylation across the genome in aged human skeletal muscle tissue and muscle-derived cells: the role of HOX genes and physical activity

Author: Nir Eynon, Sarah Voisin, Claire E. Stewart, Daniil V. Popov, Piotr P. Gorski, R. Sultanov, I. Dos-Remedios, Philipp Baumert, Daniel J. Owens, Ildus I. Ahmetov, Adam P. Sharples, Ekaterina Semenova, Andrey K. Larin, Edward V. Generozov, Robert A. Seaborne, Robert M. Erskine, Oleg V. Borisov, Alexander D. Brown, Mark O. Kitchen, Mohd Firdaus Maasar, Daniel C. Turner, Barry Drust, and Sportbiologie
Subjects: Epigenomics, Male, Physiology, Cellular differentiation, lcsh:Medicine, Gene Expression, Naturwissenschaften, Stem cells, MyoD, Epigenesis, Genetic, RC1200, ddc:790, lcsh:Science, Hox gene, Adult stem cells, Aged, 80 and over, Multidisciplinary, Genes, Homeobox, R735, Methylation, Cell biology, medicine.anatomical_structure, DNA methylation, Epigenetics, Female, ddc:500, Signal Transduction, Adult, Epigenetic memory, Stem-cell differentiation, Biology, Article, QH301, ddc:570, medicine, Humans, ddc:610, Muscle, Skeletal, QH426, Exercise, QM, Muscle Cells, Medizin und Gesundheit, Genome, Human, lcsh:R, Skeletal muscle, DNA Methylation, R1, Ageing, Biowissenschaften, Biologie, lcsh:Q, CpG Islands
Abstract: Skeletal muscle tissue demonstrates global hypermethylation with age. However, methylome changes across the time-course of differentiation in aged human muscle derived cells, and larger coverage arrays in aged muscle tissue have not been undertaken. Using 850K DNA methylation arrays we compared the methylomes of young (27 ± 4.4 years) and aged (83 ± 4 years) human skeletal muscle and that of young/aged heterogenous muscle-derived human primary cells (HDMCs) over several time points of differentiation (0, 72 h, 7, 10 days). Aged muscle tissue was hypermethylated compared with young tissue, enriched for; pathways-in-cancer (including; focal adhesion, MAPK signaling, PI3K-Akt-mTOR signaling, p53 signaling, Jak-STAT signaling, TGF-beta and notch signaling), rap1-signaling, axon-guidance and hippo-signalling. Aged cells also demonstrated a hypermethylated profile in pathways; axon-guidance, adherens-junction and calcium-signaling, particularly at later timepoints of myotube formation, corresponding with reduced morphological differentiation and reductions in MyoD/Myogenin gene expression compared with young cells. While young cells showed little alterations in DNA methylation during differentiation, aged cells demonstrated extensive and significantly altered DNA methylation, particularly at 7 days of differentiation and most notably in focal adhesion and PI3K-AKT signalling pathways. While the methylomes were vastly different between muscle tissue and HDMCs, we identified a small number of CpG sites showing a hypermethylated state with age, in both muscle tissue and cells on genes KIF15, DYRK2, FHL2, MRPS33, ABCA17P. Most notably, differential methylation analysis of chromosomal regions identified three locations containing enrichment of 6–8 CpGs in the HOX family of genes altered with age. With HOXD10, HOXD9, HOXD8, HOXA3, HOXC9, HOXB1, HOXB3, HOXC-AS2 and HOXC10 all hypermethylated in aged tissue. In aged cells the same HOX genes (and additionally HOXC-AS3) displayed the most variable methylation at 7 days of differentiation versus young cells, with HOXD8, HOXC9, HOXB1 and HOXC-AS3 hypermethylated and HOXC10 and HOXC-AS2 hypomethylated. We also determined that there was an inverse relationship between DNA methylation and gene expression for HOXB1, HOXA3 and HOXC-AS3. Finally, increased physical activity in young adults was associated with oppositely regulating HOXB1 and HOXA3 methylation compared with age. Overall, we demonstrate that a considerable number of HOX genes are differentially epigenetically regulated in aged human skeletal muscle and HDMCs and increased physical activity may help prevent age-related epigenetic changes in these HOX genes.
Published: 2020
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36. The methylome and comparative transcriptome after high intensity sprint exercise in human skeletal muscle

Author: Matthew Cocks, Sam O. Shepherd, Piotr P. Gorski, Nicolas J. Pillon, Juleen R. Zierath, Juliette A. Strauss, Mohd Firdaus Maasar, Andrew T. Hulton, Adam P. Sharples, Barry Drust, Daniel C. Turner, and Robert A. Seaborne
Subjects: medicine.medical_specialty, Insulin, medicine.medical_treatment, AMPK, Skeletal muscle, Biology, Transcriptome, Endocrinology, medicine.anatomical_structure, Sprint, Internal medicine, DNA methylation, medicine, Aerobic exercise, High-intensity interval training
Abstract: The methylome and transcriptome signature following exercise that is physiologically and metabolic relevant to sporting contexts such as team sports or health prescription scenarios (e.g. high intensity interval training/HIIT) has not been investigated. To explore this, we undertook two different sport/exercise relevant high-intensity sprint running protocols in humans using a repeated measures design of: 1) Change of direction (COD) versus; 2) straight line (ST) sprint exercise. We took skeletal muscle biopsies from the vastus lateralis 30 minutes and 24 hours post exercise followed by 850K methylation arrays and comparative analysis with recent sprint and acute aerobic exercise meta-analysis transcriptomes. Despite matched intensity (speed x distance and number of accelerations/decelerations) between COD and ST exercise, COD exercise elicited greater movement (GPS Playerload™), physiological (HR), metabolic (lactate) as well as central and peripheral (differential RPE) loading compared with ST exercise. The exercise response alone across both conditions evoked extensive alterations in the methylome immediately post and 24 hrs after exercise, particularly in MAPK, AMPK and axon guidance pathways. COD evoked a considerably greater hypomethylated signature across the genome compared with ST sprint exercise, particularly enriched in: Protein binding, MAPK, AMPK, insulin, and axon guidance pathways. A finding that was more prominent immediately post exercise. Comparative methylome analysis with sprint running transcriptomes identified considerable overlap, with 49% of the genes altered at the expression level also differentially methylated after COD exercise. After differential methylated region analysis, we discovered that VEGFA and its downstream nuclear transcription factor, NR4A1 had enriched hypomethylation within their promoter regions. VEGFA and NR4A1 were also significantly upregulated in the sprint transcriptome and meta-analysis of exercise transcriptomes. We confirmed increased mRNA expression of VEGFA, and considerably larger increases in the expression of canonical metabolic genes, PGC1-α and NR4A3, 3 hrs post COD vs. ST exercise. Overall, we demonstrate that increased physiological load via change of direction sprint exercise in human skeletal muscle evokes considerable epigenetic modifications that are associated with changes in expression of genes responsible for adaptation to exercise. These data imply that introducing changes in direction into high intensity running protocols could serve as an important modulator of a favourable epigenomic and transcriptomic landscape in response to exercise in athletes and trigger greater skeletal muscle remodelling through enhanced gene expression.
Published: 2020
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37. Discovery and prioritization of variants and genes for kidney function in >1.2 million individuals

Author: Iris M. Heid, Anna Köttgen, Thomas W. Winkler, Matthias Wuttke, Mathias Gorski, Klaus Stark, Kira-Julia Stanzick, Cristian Pattaro, and Yong Li
Subjects: In silico, medicine, Renal function, Genome-wide association study, Computational biology, Biology, medicine.disease, Explained variation, Gene, Biobank, Kidney disease, Genetic association
Abstract: Chronic kidney disease (CKD) has a complex genetic underpinning. Genome-wide association studies (GWAS) of CKD-defining glomerular filtration rate (GFR) have identified hundreds of loci, but prioritization of variants and genes is challenging. To expand and refine GWAS discovery, we meta-analyzed GWAS data for creatinine-based estimated GFR (eGFRcrea) from the Chronic Kidney Disease Genetics Consortium (CKDGen, n=765,348, trans-ethnic) and UK Biobank (UKB, n=436,581, Europeans). The results (i) extend the number of eGFRcrea loci (424 loci; 201 novel; 8.9% eGFRcrea variance explained by 634 independent signals); (ii) improve fine-mapping resolution (138 99% credible sets with ≤5 variants, 44 single-variant sets); (iii) ascertain likely kidney function relevance for 343 loci (consistent association with alternative biomarkers); and (iv) highlight 34 genes with strong evidence by a systematic Gene PrioritiSation (GPS). We provide a sortable, searchable and customizable GPS tool to navigate through the in silico functional evidence and select relevant targets for functional investigations.
Published: 2020
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38. Knockdown of the E3 Ubiquitin ligase UBR5 and its role in skeletal muscle anabolism

Author: David C. Hughes, Daniel C. Turner, Jonathan C. Jarvis, Robert A. Seaborne, Mark Viggars, Leslie M. Baehr, Piotr P. Gorski, Daniel J. Owens, Claire E. Stewart, Adam P. Sharples, and Sue C. Bodine
Subjects: Male, MAPK/ERK pathway, RM, medicine.medical_specialty, Time Factors, Anabolism, Physiology, Ubiquitin-Protein Ligases, Down-Regulation, Biology, Ribosomal Protein S6 Kinases, 90-kDa, Muscle hypertrophy, RC1200, Atrophy, Tibialis anterior muscle, Internal medicine, medicine, Animals, Phosphorylation, Extracellular Signal-Regulated MAP Kinases, Muscle, Skeletal, Protein kinase B, QM, Gene knockdown, Glycogen Synthase Kinase 3 beta, Chemistry, Myogenesis, Skeletal muscle, Cell Biology, medicine.disease, QP, Cell biology, Ubiquitin ligase, Mice, Inbred C57BL, Muscular Atrophy, Endocrinology, medicine.anatomical_structure, Gene Knockdown Techniques, biology.protein, RNA Interference, Energy Metabolism, Proto-Oncogene Proteins c-akt, Signal Transduction
Abstract: UBR5 is an E3-ubiquitin-ligase positively associated with anabolism, hypertrophy and recovery from atrophy in skeletal muscle. The precise mechanisms underpinning UBR5’s role in the regulation of skeletal muscle mass remain unknown. The present study aimed to elucidate these mechanisms by silencing the UBR5 gene in-vitro and in-vivo. The siRNA-induced reduction (−77%) in UBR5 gene expression in human myotubes was prevented by mechanical loading, suggesting that UBR5 gene expression may be regulated via mechano-transduction signalling. Therefore, we electroporated a UBR5-RNAi plasmid into mouse tibialis anterior muscle in-vivo to investigate the impact of reduced UBR5 on mechano-transduction signalling MEK/ERK/p90RSK and Akt/p70S6K/4E-BP1/rpS6 pathways. Seven days post UBR5 RNAi electroporation, while reductions in overall muscle mass were not detected, mean CSA of GFP-positive fibers was reduced (−9.5%) and the number of large fibers was lower versus the control. Importantly, UBR5-RNAi significantly reduced total RNA, muscle protein synthesis, ERK1/2 and Akt phosphorylation. Whilst p90RSK phosphorylation significantly increased, total p90RSK protein levels demonstrated a 45% reduction with UBR5-RNAi. Finally, these early signalling events after 7 days of UBR5 knockdown culminated in significant reductions in muscle mass (−4.6%) and larger reductions in fiber CSA (−18.5%) after 30 days. This was associated with increased levels of the phosphatase, PP2Ac, and inappropriate chronic elevation of p70S6K and rpS6 between 7 and 30 days, and corresponding reductions in eIF4e. This study demonstrates UBR5 plays an important role in anabolism/hypertrophy, whereby knockdown of UBR5 culminates in skeletal muscle atrophy.
Published: 2020
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39. Exercise promotes satellite cell contribution to myofibers in a load-dependent manner

Author: Laura Hinte, Katrien De Bock, Tatiane Gorski, Ori Bar-Nur, Gommaar D'Hulst, Evi Masschelein, Inés Soro-Arnaiz, Joel Zvick, and Ferdinand von Meyenn
Subjects: lcsh:Diseases of the musculoskeletal system, Satellite Cells, Skeletal Muscle, Dependent manner, Muscle Fibers, Skeletal, Cell, Muscular Contractions, Plantar flexion, Running, Muscle hypertrophy, Cell Fusion, Myonuclei, Mice, medicine, Animals, Fusion, Exercise, Cells, Cultured, Cell Nucleus, Mechanical load, biology, Chemistry, Research, biology.organism_classification, Fate tracing, Cell biology, Mice, Inbred C57BL, medicine.anatomical_structure, Wheel running, Load, Satellite (biology), lcsh:RC925-935, Satellite cell
Abstract: Background Satellite cells (SCs) are required for muscle repair following injury and are involved in muscle remodeling upon muscular contractions. Exercise stimulates SC accumulation and myonuclear accretion. To what extent exercise training at different mechanical loads drive SC contribution to myonuclei however is unknown. Results By performing SC fate tracing experiments, we show that 8 weeks of voluntary wheel running increased SC contribution to myofibers in mouse plantar flexor muscles in a load-dependent, but fiber type-independent manner. Increased SC fusion however was not exclusively linked to muscle hypertrophy as wheel running without external load substantially increased SC fusion in the absence of fiber hypertrophy. Due to nuclear propagation, nuclear fluorescent fate tracing mouse models were inadequate to quantify SC contribution to myonuclei. Ultimately, by performing fate tracing at the DNA level, we show that SC contribution mirrors myonuclear accretion during exercise. Conclusions Collectively, mechanical load during exercise independently promotes SC contribution to existing myofibers. Also, due to propagation of nuclear fluorescent reporter proteins, our data warrant caution for the use of existing reporter mouse models for the quantitative evaluation of satellite cell contribution to myonuclei., Skeletal Muscle, 10, ISSN:2044-5040
Published: 2020
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40. Electrochemical Assays and Immunoassays of the Myeloperoxidase/SCN–/H2O2 System

Author: Waldemar Gorski and Michael Bekhit
Subjects: chemistry.chemical_classification, Saliva, Chromatography, biology, animal diseases, 010401 analytical chemistry, Kinetics, Dipstick, 010402 general chemistry, Electrochemistry, 01 natural sciences, Enzyme assay, 0104 chemical sciences, Analytical Chemistry, Enzyme, chemistry, Myeloperoxidase, biology.protein, Antibody
Abstract: Strategies to detect and characterize myeloperoxidase (MPO) are needed, given that this "split personality" enzyme kills harmful microorganisms but also damages a host tissue. Here, we describe electrochemical approaches to measure MPO by using the pseudohalogenation (MPO/SCN-/H2O2) and catalase-like (MPO/H2O2) cycles. Their kinetics were determined by monitoring the consumption of H2O2 with a nitrogen-doped carbon nanotubes (N-CNT) electrode, which could detect 0.50 μM H2O2 at -0.20 V. The unique design of internally calibrated electrochemical continuous enzyme assay (ICECEA) and electrode stability allowed use of one N-CNT electrode for over half a year to reliably determine MPO. The kinetic measurements showed that (a) SCN- did not affect the affinity of MPO for H2O2, (b) catalase-like cycle was slower, and (c) MPO retained enzymatically active conformation after complexation with its antibody Ab both in a solution and on the surface of an antibody dipstick (d/Ab). The homogeneous assays could detect 5.2 μg L-1 MPO (35 pM) via a faster cycle. The heterogeneous immunoassays with the capture of MPO on d/Ab could detect 60 μg L-1, which was suitable for the accurate detection of MPO in human saliva (101% recovery). Replacing a detection antibody of ELISA with ICECEA as a signal transducer for immunoassays offers a rapid method for the selective determination of enzymes; for example, time of MPO quantification was cut from 3-4 h (sandwich ELISA) to ∼20 min (ICECEA-dipstick).
Published: 2019
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41. Low temperature stable mineral recrystallization of foraminiferal tests and implications for the fidelity of geochemical proxies

Author: Christopher A. Gorski, Piyali Chanda, Matthew S. Fantle, and Rosie L. Oakes
Subjects: Calcite, Recrystallization (geology), 010504 meteorology & atmospheric sciences, biology, Mineralogy, 010502 geochemistry & geophysics, biology.organism_classification, 01 natural sciences, Diagenesis, Foraminifera, chemistry.chemical_compound, Geophysics, chemistry, Space and Planetary Science, Geochemistry and Petrology, Earth and Planetary Sciences (miscellaneous), Carbonate, Seawater, Chemical composition, Dissolution, Geology, 0105 earth and related environmental sciences
Abstract: Fossilized foraminiferal tests are widely used as proxies to constrain paleoenvironments, including past sea surface and bottom water temperatures and the chemical composition of ancient seawater. However, relatively little is known about the extent to which calcareous foraminiferal tests exchange with seawater prior to burial. In this study, we used a 45Ca radiotracer approach to quantify the extent and rate of foraminiferal calcite–fluid exchange over a three-month period. Modern foraminiferal tests exhibited faster exchange with a 45Ca-spiked solution (2.6⋅10−4 to 2.0⋅10−5 mol/m2/d) than fossil foraminiferal tests (7.6⋅10−5 to 5.3⋅10−6 mol/m2/d) from ODP Site 807. The impact of dissolved Si on the exchange rate of modern foraminifera was minimal (2.6⋅10−4 to 9.2⋅10−6 mol/m2/d). Unlike foraminiferal calcite, inorganic calcite exchanged at remarkably slow rates (6.6⋅10−6 to 5.9⋅10−7 mol/m2/d) suggesting that biogenic calcite is more reactive than inorganic calcite. Increased Ca2+, Mg2+, and Sr2+ concentrations in fluids from parallel tracer-free reactors indicated preferential dissolution of tests, though there was no overt change in test morphology during experiments (as imaged by scanning electron microscopy and micro-CT scanning). Time-dependent box model simulations of 45Ca, as well as aqueous elemental chemistry, support the hypothesis that calcite–fluid exchange occurred via dissolution–reprecipitation of foraminiferal tests that was induced by intra-test chemical heterogeneity. The short-term exchange reactions investigated in this study are comparable to the reactions that can occur in the seawater column and at the sediment–seawater interface. This work suggests that dissolution–reprecipitation in such settings has the potential to overprint the chemistry of foraminiferal tests without overt physical alteration, which can lead to a potential bias in paleoenvironmental reconstructions. Model-based estimates suggest a maximum of 2–3 °C alteration of Mg/Ca-based temperatures over experimental time scales. Model efforts also suggest that the diagenetic trajectories in Mg/Ca– δ 18 O space, for instance, are impacted by the partition coefficient of Mg in calcite (λMg) as well as by the mechanism of alteration. This is demonstrated for (i) the ratio of exchange to dissolution and (ii) the relative rate of high-Mg-calcite to low-Mg-calcite reaction. We have illustrated that the mechanism of alteration, in addition to water-rock ratios, determine diagenetic trajectories. Finally, surface reaction has implications for our ability to constrain fractionation factors in experimental and natural systems. The experimental observations suggest that exchange between tests and solution is nominal over ∼100 days. Experiments aimed at deducing fractionation factors rely on the equilibration of bulk solid and fluid, since these are the readily analyzed reservoirs. We quantify the fraction of carbonate (>5%) that must react so that surface reaction does not impact the interpretation of Ca isotopic fractionation factors, and discuss the implications for more “fluid-dominated” elements such as Mg and O.
Published: 2019
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42. Complete Genomic Sequences of Three Salmonella enterica subsp. enterica Serovar Muenchen Strains from an Orchard in San Joaquin County, California

Author: Steven Huynh, Thao Dang-Hien Tran, Craig T. Parker, Jeffery A. McGarvey, Lisa Gorski, Sat Darshan S. Khalsa, Robert Hnasko, Patrick O. Brown, and Newton, Irene LG
Subjects: Serotype, Genetics, 0303 health sciences, biology, 030306 microbiology, Genome Sequences, Human Genome, Genomics, biology.organism_classification, Genome, Vaccine Related, 03 medical and health sciences, Immunology and Microbiology (miscellaneous), Salmonella enterica, Salmonella enterica subsp. enterica, San Joaquin, Orchard, Molecular Biology, 030304 developmental biology, Biotechnology
Abstract: We present here the complete genome sequences of three Salmonella enterica subsp. enterica serovar Muenchen strains, LG24, LG25, and LG26. All three strains were isolated from almond drupes grown in an orchard in San Joaquin County, California, in 2016. These genomic sequences are nonidentical and will contribute to our understanding of S. enterica genomics.
Published: 2020

43. Diverse mechanisms of autophagy dysregulation and their therapeutic implications: does the shoe fit?

Author: Courtney Choutka, Cally J Ho, Jing Xu, Svetlana Bortnik, Katharina Rothe, Xiaoyan Jiang, Norman S. Chow, Sharon M. Gorski, Paalini Sathiyaseelan, and Kevin C. Yang
Subjects: 0301 basic medicine, Huntingtin, Apoptosis, Meeting Report, Endoplasmic-reticulum-associated protein degradation, Biology, 03 medical and health sciences, Neoplasms, Mitophagy, Autophagy, medicine, Animals, Humans, Molecular Biology, 030102 biochemistry & molecular biology, Neurodegeneration, Proteins, Cell Biology, medicine.disease, 3. Good health, 030104 developmental biology, HIF1A, Imatinib mesylate, Cancer research, MAP1LC3B
Abstract: In its third edition, the Vancouver Autophagy Symposium presented a platform for vibrant discussion on the differential roles of macroautophagy/autophagy in disease. This one-day symposium was held at the BC Cancer Research Centre in Vancouver, BC, bringing together experts in cell biology, protein biochemistry and medicinal chemistry across several different disease models and model organisms. The Vancouver Autophagy Symposium featured 2 keynote speakers that are well known for their seminal contributions to autophagy research, Dr. David Rubinsztein (Cambridge Institute for Medical Research) and Dr. Kay F. Macleod (University of Chicago). Key discussions included the context-dependent roles and mechanisms of dysregulation of autophagy in diseases and the corresponding need to consider context-dependent autophagy modulation strategies. Additional highlights included the differential roles of bulk autophagy versus selective autophagy, novel autophagy regulators, and emerging chemical tools to study autophagy inhibition. Interdisciplinary discussions focused on addressing questions such as which stage of disease to target, which type of autophagy to target and which component to target for autophagy modulation. Abbreviations: AD: Alzheimer disease; AMFR/Gp78: autocrine motility factor receptor; CCCP: carbonyl cyanide m-chlorophenylhydrazone; CML: chronic myeloid leukemia; CVB3: coxsackievirus B3; DRPLA: dentatorubral-pallidoluysian atrophy; ER: endoplasmic reticulum; ERAD: ER-associated degradation; FA: focal adhesion; HCQ: hydroxychloroquine; HD: Huntingtin disease; HIF1A/Hif1α: hypoxia inducible factor 1 subunit alpha; HTT: huntingtin; IM: imatinib mesylate; MAP1LC3B: microtubule associated protein 1 light chain 3 beta; NBR1: neighbour of BRCA1; OGA: O-GlcNAcase; PDAC: pancreatic ductal adenocarcinoma; PLEKHM1: pleckstrin homology and RUN domain containing M1; polyQ: poly-glutamine; ROS: reactive oxygen species; RP: retinitis pigmentosa; SNAP29: synaptosome associated protein 29; SPCA3: spinocerebellar ataxia type 3; TNBC: triple-negative breast cancer.
Published: 2018
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44. IgA Fc-folate conjugate activates and recruits neutrophils to directly target triple-negative breast cancer cells

Author: Dana L Schalk, Tracey J Guerin-Edbauer, Manohar Ratnam, Cecilia L. Speyer, David H. Gorski, Lauren E Leakan, Eric D Frontera, and Rafa M. Khansa
Subjects: 0301 basic medicine, Folate Receptor Alpha, Cancer Research, Neutrophils, medicine.medical_treatment, Cell, Triple Negative Breast Neoplasms, Receptors, Fc, Article, Targeted therapy, 03 medical and health sciences, Folic Acid, 0302 clinical medicine, Cell Line, Tumor, medicine, Humans, Folate Receptor 1, Receptor, Triple-negative breast cancer, Peroxidase, Antibody-dependent cell-mediated cytotoxicity, biology, Chemistry, Antibody-Dependent Cell Cytotoxicity, Cancer, medicine.disease, Immunoglobulin A, 030104 developmental biology, medicine.anatomical_structure, Oncology, 030220 oncology & carcinogenesis, Myeloperoxidase, biology.protein, Cancer research, Female
Abstract: PURPOSE: According to the American Cancer Society, 1 in 8 women in the U.S. will develop breast cancer, with triple negative breast cancer (TNBC) comprising 15-20% of all breast cancer cases. TNBC is an aggressive subtype due to its high metastatic potential and lack of targeted therapy. Recently, folate receptor alpha (FRA) is found to be expressed on 80% of TNBC with high expression correlating with poor prognosis. In this study, we examined whether binding IgA Fc-folate molecules to FRA receptors on TNBC cells can elicit and induce neutrophils (PMNs), by binding their FcαR1 receptors, to destroy TNBC cells. METHODS: FRA was analyzed on TNBC cells and binding assays were performed using (3)H-folate. Fc-folate was synthesized by linking Fc-fragments of IgA via amine groups to folate. Binding specificity and antibody dependent cellular cytotoxicity (ADCC) potential of Fc-folate to FcαR1 was confirmed by measuring PMN adhesion and myeloperoxidase (MPO) release in a cell-based ELISA. Fc-folate binding to FRA-expressing TNBC cells inducing PMNs to destroy these cells was determined using (51)Cr-release and calcein-labeling assays. RESULTS: Our results demonstrate expression of FRA on TNBC cells at levels consistent with folate binding. Fc-folate binds with high affinity to FRA compared to whole IgA-folate and induces MPO release from PMN when bound to FcαR1. Fc-folate inhibited binding of (3)H-folate to TNBC cells and induced significant cell lysis of TNBC cells when incubated in the presence of PMNs. CONCLUSION: These findings support the hypothesis that an IgA Fc-folate conjugate can destroy TNBC cells by eliciting PMN-mediated ADCC.
Published: 2018
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45. Bacterial RNA Biology on a Genome Scale

Author: Jörg Vogel, Stanislaw A. Gorski, Jens Hör, and HIRI, Helmholtz-Institut für RNA-basierte Infektionsforschung, Josef-Schneider-Strasse 2, 97080 Würzburg, Germany.
Subjects: 0301 basic medicine, Riboswitch, Small RNA, RNA Stability, 030106 microbiology, RNA-binding protein, Computational biology, Biology, Structure-Activity Relationship, 03 medical and health sciences, Bacterial Proteins, Transcription (biology), CRISPR, RNA Processing, Post-Transcriptional, Molecular Biology, Post-transcriptional regulation, Bacteria, Sequence Analysis, RNA, Gene Expression Profiling, RNA, Gene Expression Regulation, Bacterial, Cell Biology, Non-coding RNA, RNA, Bacterial, 030104 developmental biology, Protein Biosynthesis, Nucleic Acid Conformation, Transcriptome, Genome, Bacterial
Abstract: Bacteria are an exceedingly diverse group of organisms whose molecular exploration is experiencing a renaissance. While the classical view of bacterial gene expression was relatively simple, the emerging view is more complex, encompassing extensive post-transcriptional control involving riboswitches, RNA thermometers, and regulatory small RNAs (sRNAs) associated with the RNA-binding proteins CsrA, Hfq, and ProQ, as well as CRISPR/Cas systems that are programmed by RNAs. Moreover, increasing interest in members of the human microbiota and environmental microbial communities has highlighted the importance of understudied bacterial species with largely unknown transcriptome structures and RNA-based control mechanisms. Collectively, this creates a need for global RNA biology approaches that can rapidly and comprehensively analyze the RNA composition of a bacterium of interest. We review such approaches with a focus on RNA-seq as a versatile tool to investigate the different layers of gene expression in which RNA is made, processed, regulated, modified, translated, and turned over.
Published: 2018
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46. A biochemical framework for anaerobic oxidation of methane driven by Fe(III)-dependent respiration

Author: James G. Ferry, Christopher A. Gorski, Prachi Joshi, and Zhen Yan
Subjects: 0301 basic medicine, Science, 030106 microbiology, General Physics and Astronomy, Ferric Compounds, Article, General Biochemistry, Genetics and Molecular Biology, Methane, Metabolic engineering, 03 medical and health sciences, chemistry.chemical_compound, Respiration, Anaerobiosis, Methanosarcina acetivorans, lcsh:Science, Multidisciplinary, biology, Endergonic reaction, General Chemistry, biology.organism_classification, 030104 developmental biology, chemistry, 13. Climate action, Environmental chemistry, Methanosarcina, Anaerobic oxidation of methane, lcsh:Q, Oxidation-Reduction, Anaerobic exercise, Metabolic Networks and Pathways, Archaea
Abstract: Consumption of methane by aerobic and anaerobic microbes governs the atmospheric level of this powerful greenhouse gas. Whereas a biochemical understanding of aerobic methanotrophy is well developed, a mechanistic understanding of anaerobic methanotrophy has been prevented by the unavailability of pure cultures. Here we report a biochemical investigation of Methanosarcina acetivorans, a methane-producing species capable of anaerobic methanotrophic growth dependent on reduction of Fe(III). Our findings support a pathway anchored by Fe(III)-dependent mechanisms for energy conservation driving endergonic reactions that are key to methanotrophic growth. The pathway is remarkably similar to pathways hypothesized for uncultured anaerobic methanotrophic archaea. The results contribute to an improved understanding of the methane cycle that is paramount to understanding human interventions influencing Earth’s climate. Finally, the pathway enables advanced development and optimization of biotechnologies converting methane to value-added products through metabolic engineering of M. acetivorans., The unavailability of pure cultures has prevented a mechanistic understanding of anaerobic methanotrophy. Here the authors report a biochemical investigation of Methanosarcina acetivorans that supports a pathway anchored by Fe(III)-dependent mechanisms for energy conservation and driving endergonic reactions.
Published: 2018

47. DANCE THERAPY-METHOD MARIA FUX CONTRIBUTIONS IN THE LIFE OF MODERN WOMAN

Author: Weliton Augusto Gorski da Luz, Gildasio Jose Dos Santos, Cassio Hartmann, Cristian Eduardo Gorski da Luz, and Eliana da Silva Chaves
Subjects: Literature, biology, business.industry, Aesthetics, media_common.quotation_subject, Self-esteem, Curitiba, Psychology, business, biology.organism_classification, The good life, media_common, Dance therapy
Abstract: This article refers to the work on stage in dance therapy - method Maria Fux, whose objective is to pay attention to theimpact of dance therapy practices and whether they can already be observed in the short term the life of the modern woman. Wasgiven by choice, adaptation and application of slogans stimulus that State network of teachers from Curitiba / PR, vivenciassem intheir bodies the effects of this practice which consists of a self resource, which benefits focuses on allowing the individual find thereal causes of their difficulties, thus enabling the act in order to transform them, a contributing factor to the development of selfesteem,so necessary for the good life.
Published: 2017
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48. Determination of sorbitol dehydrogenase in microsamples of human serum

Author: Waldemar Gorski and Michael Bekhit
Subjects: L-Iditol 2-Dehydrogenase, Chromatography, medicine.diagnostic_test, biology, Sorbitol dehydrogenase, Fructose, macromolecular substances, NAD, Amperometry, Cofactor, Analytical Chemistry, Kinetics, chemistry.chemical_compound, Glucose, chemistry, medicine, biology.protein, Humans, Sorbitol, Glucose test, Enzyme kinetics, NAD+ kinase
Abstract: The enzyme sorbitol dehydrogenase (SDH) is an emerging biomarker of drug-induced liver injury (DILI). This paper introduces determination of SDH in microliter samples of human serum at commercial glucose test strips. The determination relies on the oxidation of NADH cofactor, which is used by SDH reacting with its substrates. The strips could detect NADH down to 5.0 μM (5 pmol), which was two orders of magnitude better than the prior relevant limit of detection. The concentration of cofactors (NADH, NAD+) and substrates (fructose, sorbitol) for SDH determination at a strip was optimized via internally-calibrated amperometric assays at a chitosan/nitrogen-doped carbon nanotube electrode. Such an electrode provided reliable assay data for over 3 months with no need for its reactivation. The assays yielded kinetic parameters Km and kcat and demonstrated higher apparent affinity of SDH for NADH and fructose than NAD+ and sorbitol. The glucose strips detected SDH down to 98 pM (98 amol) in buffers and 200 pM (200 amol) in human serum after 20-min incubation with an optimized (c ≥ 10Km) mixture of cofactor + substrate. The charge ΔQ flowing through a strip was linear (R2, 0.994) up to 6.0 nM SDH, which covered enzyme's clinical range. The ΔQ was selective for SDH, independent of sample matrix, and free of interferences from indigenous glucose. The use of glucose strip as an electrolytic microcell to detect picomoles of NADH and attomoles of SDH is a step toward a point-of-care monitoring of DILI.
Published: 2021
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49. Drought influences biodiversity in a semi-arid shortgrass prairie in southeastern Colorado

Author: Jason Fender, Angeline Canney, Jessica Gorski, Clark D. Jones, Morgan Kester, Marie Gomez, Brian Vanden Heuvel, Delania Klinger, Elizabeth K. Peterson, Kevin Healey, Franziska C. Sandmeier, Cody Allyn Back, Adam Liao, Nathan Heintzelman, Andrea P. Arellano Rivas, and Claire W. Varian-Ramos
Subjects: Habitat fragmentation, Ecology, biology, Biodiversity, Prairie dog, medicine.disease, Ecosystem services, Sylvatic plague, Geography, Abundance (ecology), biology.animal, medicine, Species richness, Keystone species, Ecology, Evolution, Behavior and Systematics, Earth-Surface Processes
Abstract: Prairie dogs are a keystone species that provide ecosystem services in endangered grasslands in North America. They have been extirpated throughout their range due to sylvatic plague, habitat fragmentation, lethal control, and drought. There are competing drivers of biodiversity between herbivorous rodents and drought in semi-arid grasslands. Therefore, prairie dogs may be unable to provide the ecosystem services needed for grasslands during periods of drought. We sought to determine the impact of prairie dog herbivory on biodiversity in a semi-arid shortgrass prairie by using a paired design to compare active colonies with extirpated colonies. Abundance, richness, and diversity were measured in vegetation, arthropods, herptiles, birds, and small mammals during a drought year and the following year. We found that drought reduced vegetation and bird abundance, vegetation richness and diversity, and diversity in arthropods and birds. We did not find a difference between colonies and extirpated colonies. Our results indicate that the ecosystem services provided by prairie dogs, e.g., improving biodiversity, did not occur at detectable levels during periods of drought in semi-arid grasslands. Given the sharp decline of prairie dogs, the ecosystem services provided by prairie dogs will continue to plummet as climate change increases the frequency of droughts in the Front Range.
Published: 2021
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50. Genome-wide association meta-analyses and fine-mapping elucidate pathways influencing albuminuria

Author: Tobias Hermle, Holger Kirsten, Karsten B. Sieber, Aiko P. J. de Vries, Su Chi Lim, Peter Kovacs, Charumathi Sabanayagam, Carl D. Langefeld, Bernhard K. Krämer, Kent D. Taylor, Janine F. Felix, Belen Ponte, Markus Loeffler, Mary F. Feitosa, Kai-Uwe Eckardt, Jianjun Liu, Katalin Dittrich, Charlene A. Wong, Uwe Völker, Adriana M. Hung, Thomas Meitinger, Anubha Mahajan, Anselm Hoppmann, Erik Ingelsson, Martin H. de Borst, Oscar H. Franco, Niek Verweij, Kai-Uwe Saum, Vilmundur Gudnason, Bram P. Prins, Carsten A. Böger, Terho Lehtimäki, Andrew A. Hicks, Todd L. Edwards, Olivier Devuyst, Peter P. Pramstaller, Katrin Horn, Leslie A. Lange, Johanne Tremblay, Jin-Fang Chai, Sahar Ghasemi, Kjell Nikus, Tanja Poulain, Massimiliano Cocca, Anna Köttgen, Eric Boerwinkle, Barry I. Freedman, Miao-Ling Chee, Man Li, Stephan J. L. Bakker, Tamara B. Harris, Albert V. Smith, Ton J. Rabelink, Dennis O. Mook-Kanamori, Iris M. Heid, Jasmin Divers, Chaolong Wang, Kathleen A. Ryan, Pavel Hamet, Silke Szymczak, Shih-Jen Hwang, Hauke Thomsen, Rainer Rettig, Ayush Giri, Fernando Rivadeneira, Leo-Pekka Lyytikäinen, Cristian Pattaro, Andrej Teren, Valencia Hui Xian Foo, Myriam Rheinberger, Audrey Y. Chu, Barbara McMullen, Franziska Grundner-Culemann, Masayuki Yasuda, Murielle Bochud, Martin Gögele, Anke Tönjes, Jeannette Lee, Adrienne Tin, Kevin Ho, Konstantin Strauch, Josef Coresh, Renée de Mutsert, Sandra Freitag-Wolf, Gardar Sveinbjornsson, Yizhe Xu, Katalin Susztak, Tien Yin Wong, Mary L. Biggs, Isleifur Olafsson, Qiong Yang, Antje Körner, Chengxiang Qiu, E-Shyong Tai, Martina Müller-Nurasyid, Ben Schöttker, Jeffrey O' Connell, Mengmeng Chen, Daniel F. Gudbjartsson, Dermot F. Reilly, Vincent W. V. Jaddoe, Damia Noce, Pim van der Harst, Sanaz Sedaghat, Chiea Chuen Khor, Adam S. Butterworth, Mathias Gorski, Robert J. Carroll, James G. Wilson, Johan Ärnlöv, Christa Meisinger, Kenneth Rice, Bettina Jung, Christian M. Shaffer, Unnur Thorsteinsdottir, Matthias Nauck, Shreeram Akilesh, Mika Kähönen, Johanna Jakobsdottir, Melanie Waldenberger, Ralph Burkhardt, Daniela Baptista, John Danesh, Benjamin B. Sun, Karlhans Endlich, Holly Kramer, Frauke Degenhardt, Wolfgang Lieb, Kari Stefansson, Joachim Thiery, Lars Lind, Nicholette D. Palmer, Sarah A. Pendergrass, Suzanne Vogelezang, Peter J. van der Most, Afshin Parsa, Markus Scholz, Florian Kronenberg, Joseph C. Maranville, Laura M. Raffield, Hermann Brenner, Wieland Kiess, Anna I. Podgornaia, Yuan Shi, Tanguy Corre, Miao-Li Chee, Deborah Mascalzoni, Bamidele O. Tayo, Navya Shilpa Josyula, Ching-Yu Cheng, Lea Gerstner, Nisha Bansal, Jerome I. Rotter, Alexander Teumer, Vilmantas Giedraitis, Raymond Noordam, Ron T. Gansevoort, Lihua Wang, Andrew P. Morris, Bruce M. Psaty, Boting Ning, Zhi Yu, Christian Fuchsberger, Matthias Wuttke, Heiko Runz, Annette Peters, Yih Chung Tham, James P. Cook, Yong Li, Chris H. L. Thio, Hilma Holm, Alessandro De Grandi, Jonathan Marten, André G. Uitterlinden, Andre Franke, Nicholas Y. Q. Tan, Otis D. Wilson, Georg Ehret, Cecilia M. Lindgren, Josyf C. Mychaleckyj, Wolfgang Koenig, Harold Snieder, Michael Stumvoll, Kozeta Miliku, M. Arfan Ikram, Teresa Nutile, Læknadeild (HÍ), Faculty of Medicine (UI), School of Health Sciences (UI), Heilbrigðisvísindasvið (HÍ), Háskóli Íslands, University of Iceland, Teumer, Alexander [0000-0002-8309-094X], Li, Yong [0000-0003-2651-8791], Wuttke, Matthias [0000-0003-3420-5082], Giri, Ayush [0000-0002-7786-4670], Qiu, Chengxiang [0000-0002-6346-8669], Kirsten, Holger [0000-0002-3126-7950], Tin, Adrienne [0000-0002-4207-5866], Feitosa, Mary F. [0000-0002-0933-2410], Chai, Jin-Fang [0000-0003-3770-1137], Cocca, Massimiliano [0000-0002-1127-7596], Gorski, Mathias [0000-0002-9103-5860], Horn, Katrin [0000-0002-5307-6936], Li, Man [0000-0002-3839-0281], Marten, Jonathan [0000-0001-6916-2014], van der Most, Peter J. [0000-0001-8450-3518], Burkhardt, Ralph [0000-0003-1924-1202], Coresh, Josef [0000-0002-4598-0669], de Borst, Martin H. [0000-0002-4127-8733], Ehret, Georg [0000-0002-5730-0675], Endlich, Karlhans [0000-0001-6052-6061], Felix, Janine F. [0000-0002-9801-5774], Franke, Andre [0000-0003-1530-5811], Freedman, Barry I. [0000-0003-0275-5530], Freitag-Wolf, Sandra [0000-0002-1069-7740], Giedraitis, Vilmantas [0000-0003-3423-2021], Grundner-Culemann, Franziska [0000-0001-9649-281X], Gudnason, Vilmundur [0000-0001-5696-0084], Hicks, Andrew A. [0000-0001-6320-0411], Ikram, M. Arfan [0000-0003-0372-8585], Ingelsson, Erik [0000-0003-2256-6972], Jaddoe, Vincent W. V. [0000-0003-2939-0041], Josyula, Navya Shilpa [0000-0003-2782-8812], Khor, Chiea-Chuen [0000-0002-1128-4729], Koenig, Wolfgang [0000-0002-2064-9603], Kovacs, Peter [0000-0002-0290-5423], Kronenberg, Florian [0000-0003-2229-1120], Lindgren, Cecilia M. [0000-0002-4903-9374], Liu, Jianjun [0000-0002-3255-3019], Lyytikäinen, Leo-Pekka [0000-0002-7200-5455], Mahajan, Anubha [0000-0001-5585-3420], Mascalzoni, Deborah [0000-0003-4156-1464], Miliku, Kozeta [0000-0002-9614-7191], Müller-Nurasyid, Martina [0000-0003-3793-5910], Mychaleckyj, Josyf C. [0000-0003-2595-0005], Palmer, Nicholette D. [0000-0001-8883-2511], Poulain, Tanja [0000-0003-3825-5829], Raffield, Laura M. [0000-0002-7892-193X], Rice, Kenneth M. [0000-0002-3071-7278], Rivadeneira, Fernando [0000-0001-9435-9441], Sabanayagam, Charumathi [0000-0002-4042-4719], Smith, Albert V. [0000-0003-1942-5845], Sun, Benjamin B. [0000-0001-6347-2281], Szymczak, Silke [0000-0002-8897-9035], Taylor, Kent D. [0000-0002-2756-4370], Thio, Chris H. L. [0000-0003-2623-7172], Uitterlinden, André G. [0000-0002-7276-3387], van der Harst, Pim [0000-0002-2713-686X], Verweij, Niek [0000-0002-4303-7685], Völker, Uwe [0000-0002-5689-3448], Wang, Chaolong [0000-0003-3945-1012], Yang, Qiong [0000-0002-3658-1375], Devuyst, Olivier [0000-0003-3744-4767], Edwards, Todd L. [0000-0003-4318-6119], Ho, Kevin [0000-0002-3054-8697], Morris, Andrew P. [0000-0002-6805-6014], Pendergrass, Sarah A. [0000-0002-0565-6522], Rotter, Jerome I. [0000-0001-7191-1723], Stefansson, Kari [0000-0003-1676-864X], Susztak, Katalin [0000-0002-1005-3726], Scholz, Markus [0000-0002-4059-1779], Butterworth, Adam S. [0000-0002-6915-9015], Hung, Adriana M. [0000-0002-3203-1608], Pattaro, Cristian [0000-0002-4119-0109], Köttgen, Anna [0000-0002-4671-3714], Apollo - University of Cambridge Repository, Groningen Institute for Organ Transplantation (GIOT), Lifestyle Medicine (LM), Groningen Kidney Center (GKC), Cardiovascular Centre (CVC), Life Course Epidemiology (LCE), Epidemiology, Erasmus MC other, Pediatrics, Internal Medicine, Feitosa, Mary F [0000-0002-0933-2410], van der Most, Peter J [0000-0001-8450-3518], de Borst, Martin H [0000-0002-4127-8733], Felix, Janine F [0000-0002-9801-5774], Freedman, Barry I [0000-0003-0275-5530], Hicks, Andrew A [0000-0001-6320-0411], Ikram, M Arfan [0000-0003-0372-8585], Jaddoe, Vincent WV [0000-0003-2939-0041], Lindgren, Cecilia M [0000-0002-4903-9374], Mychaleckyj, Josyf C [0000-0003-2595-0005], Palmer, Nicholette D [0000-0001-8883-2511], Raffield, Laura M [0000-0002-7892-193X], Rice, Kenneth M [0000-0002-3071-7278], Smith, Albert V [0000-0003-1942-5845], Sun, Benjamin B [0000-0001-6347-2281], Taylor, Kent D [0000-0002-2756-4370], Thio, Chris HL [0000-0003-2623-7172], Uitterlinden, André G [0000-0002-7276-3387], Edwards, Todd L [0000-0003-4318-6119], Morris, Andrew P [0000-0002-6805-6014], Pendergrass, Sarah A [0000-0002-0565-6522], Rotter, Jerome I [0000-0001-7191-1723], Butterworth, Adam S [0000-0002-6915-9015], and Hung, Adriana M [0000-0002-3203-1608]
Subjects: 0301 basic medicine, Drosophila melanogaster/genetics, Diabetes Mellitus/genetics, LD SCORE REGRESSION, 030232 urology & nephrology, 45/43, General Physics and Astronomy, Genome-wide association study, BLOOD-PRESSURE, Bioinformatics, GLOMERULAR-FILTRATION-RATE, Genome-wide association studies, Diabetes mellitus genetics, 0302 clinical medicine, Creatinine/urine, Risk Factors, Genome-wide, Phenomics, lcsh:Science, ddc:616, Regulation of gene expression, RISK, Gene knockdown, Kidney diseases, Multidisciplinary, HERITABILITY, Albuminuria/genetics, article, Chromosome Mapping, Kidney disease, ddc, 3. Good health, Drosophila melanogaster, Creatinine, Nýrnasjúkdómar, 692/4022/1585, Slit diaphragm, Medical genetics, medicine.symptom, Erfðarannsóknir, Medical Genetics, medicine.medical_specialty, Science, 631/208/205/2138, 610 Medicine & health, Biology, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Meta-Analysis as Topic, 360 Social problems & social services, Diabetes Mellitus, medicine, Animals, Humans, Albuminuria, Genetic Predisposition to Disease, ddc:610, EXCRETION RATE, CARDIOVASCULAR EVENTS, Genetic association, Medicinsk genetik, TRANS-EQTLS, KIDNEY-DISEASE, General Chemistry, 030104 developmental biology, Gene Expression Regulation, Genetic Loci, COLLABORATIVE METAANALYSIS, lcsh:Q, Genome-Wide Association Study
Abstract: Publisher's version (útgefin grein)., Increased levels of the urinary albumin-to-creatinine ratio (UACR) are associated with higher risk of kidney disease progression and cardiovascular events, but underlying mechanisms are incompletely understood. Here, we conduct trans-ethnic (n = 564,257) and European-ancestry specific meta-analyses of genome-wide association studies of UACR, including ancestry- and diabetes-specific analyses, and identify 68 UACR-associated loci. Genetic correlation analyses and risk score associations in an independent electronic medical records database (n = 192,868) reveal connections with proteinuria, hyperlipidemia, gout, and hypertension. Fine-mapping and trans-Omics analyses with gene expression in 47 tissues and plasma protein levels implicate genes potentially operating through differential expression in kidney (including TGFB1, MUC1, PRKCI, and OAF), and allow coupling of UACR associations to altered plasma OAF concentrations. Knockdown of OAF and PRKCI orthologs in Drosophila nephrocytes reduces albumin endocytosis. Silencing fly PRKCI further impairs slit diaphragm formation. These results generate a priority list of genes and pathways for translational research to reduce albuminuria., Competing interests: Karsten B. Sieber is full-time employee of GlaxoSmithKline. Gardar Sveinbjornsson, Daniel F. Gudbjartsson, Hilma Holm, Unnur Thorsteinsdottir and Kari Stefansson are full-time employees of deCODE genetics, Amgen Inc. John Danesh is member of the Novartis Cardiovascular and Metabolic Advisory Board, received grant support from Novartis. Oscar H. Franco works in ErasmusAGE, a center for aging research across the life course funded by Nestlé Nutrition (Nestec Ltd.), Metagenics Inc., and AXA. Wolfgang Koenig received modest consultation fees for advisory board meetings from Amgen, DalCor, Kowa, Novartis, Pfizer and Sanofi, and modest personal fees for lectures from Amgen, AstraZeneca, Novartis, Pfizer and Sanofi. Anna I. Podgornaia and Dermot F. Reilly are employees of Merck Sharp Dohme Corp., Whitehouse Station, NJ, USA. Kevin Ho disclosed a research and financial relationship with Sanofi-Genzyme. Bruce M. Psaty serves on the DSMB of a clinical trial funded by the manufacturer (Zoll LifeCor) and on the Steering Committee of the Yale Open Data Access Project funded by Johnson & Johnson. Markus Scholz: Consultancy of and grant support from Merck Serono not related to this project. Adam S. Butterworth received grants from MSD, Pfizer, Novartis, Biogen and Bioverativ and personal fees from Novartis. Anna Köttgen received grant support from Gruenenthal not related to this project. The other authors declare no competing interests.
Published: 2019
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