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1. Phosphatidylserine-exposing extracellular vesicles in body fluids are an innate defence against apoptotic mimicry viral pathogens

Author

Groß, Rüdiger, Reßin, Hanna, von Maltitz, Pascal, Albers, Dan, Schneider, Laura, Bley, Hanna, Hoffmann, Markus, Cortese, Mirko, Gupta, Dhanu, Deniz, Miriam, Choi, Jae-Yeon, Jansen, Jenny, Preußer, Christian, Seehafer, Kai, Pöhlmann, Stefan, Voelker, Dennis R., Goffinet, Christine, Pogge-von Strandmann, Elke, Bunz, Uwe, Bartenschlager, Ralf, El Andaloussi, Samir, Sparrer, Konstantin M. J., Herker, Eva, Becker, Stephan, Kirchhoff, Frank, Münch, Jan, and Müller, Janis A.

Published
2024
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3. Glycerophospholipid remodeling is critical for orthoflavivirus infection.

Author

Hehner, Julia, Schneider, Laura, Woitalla, Anna, Ott, Benjamin, Vu, Kim Chi Thi, Schöbel, Anja, Hain, Torsten, Schwudke, Dominik, and Herker, Eva

Subjects
TICK-borne encephalitis viruses, FLAVIVIRAL diseases, LIPID metabolism, YELLOW fever, ZIKA virus infections, FLAVIVIRUSES
Abstract

Flavivirus infection is tightly connected to host lipid metabolism. Here, we performed shotgun lipidomics of cells infected with neurotropic Zika, West Nile, and tick-borne encephalitis virus, as well as dengue and yellow fever virus. Early in infection specific lipids accumulate, e.g., neutral lipids in Zika and some lysophospholipids in all infections. Ceramide levels increase following infection with viruses that cause a cytopathic effect. In addition, fatty acid desaturation as well as glycerophospholipid metabolism are significantly altered. Importantly, depletion of enzymes involved in phosphatidylserine metabolism as well as phosphatidylinositol biosynthesis reduce orthoflavivirus titers and cytopathic effects while inhibition of fatty acid monounsaturation only rescues from virus-induced cell death. Interestingly, interfering with ceramide synthesis has opposing effects on virus replication and cytotoxicity depending on the targeted enzyme. Thus, lipid remodeling by orthoflaviviruses includes distinct changes but also common patterns shared by several viruses that are needed for efficient infection and replication. Viruses need host cell lipids for multiplication. Here, the authors use lipidomics to show that lipid remodeling by orthoflaviviruses includes distinct changes but also shared patterns, some of which are needed for efficient viral replication. [ABSTRACT FROM AUTHOR]

Published
2024
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5. The Hepatitis C Virus Core Protein Inhibits Adipose Triglyceride Lipase (ATGL)-mediated Lipid Mobilization and Enhances the ATGL Interaction with Comparative Gene Identification 58 (CGI-58) and Lipid Droplets*

Author

Camus, Gregory, Schweiger, Martina, Herker, Eva, Harris, Charles, Kondratowicz, Andrew S, Tsou, Chia-Lin, Farese, Robert V, Herath, Kithsiri, Previs, Stephen F, Roddy, Thomas P, Pinto, Shirly, Zechner, Rudolf, and Ott, Melanie

Subjects
Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Biological Sciences, Emerging Infectious Diseases, Infectious Diseases, Chronic Liver Disease and Cirrhosis, Liver Disease, Hepatitis, Digestive Diseases, Hepatitis - C, Aetiology, 2.1 Biological and endogenous factors, Good Health and Well Being, 1-Acylglycerol-3-Phosphate O-Acyltransferase, Animals, COS Cells, Cell Line, Tumor, Chlorocebus aethiops, HEK293 Cells, Humans, Hydrolysis, Lipase, Lipid Droplets, Lipid Metabolism, Male, Mice, Mice, Inbred C57BL, Mice, Knockout, NIH 3T3 Cells, Triglycerides, Viral Core Proteins, Adipose Triglyceride Lipase, Hepatitis C Virus, Lipid Droplet, Lipolysis, Triglyceride, Chemical Sciences, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Chemical sciences
Abstract

Liver steatosis is a common health problem associated with hepatitis C virus (HCV) and an important risk factor for the development of liver fibrosis and cancer. Steatosis is caused by triglycerides (TG) accumulating in lipid droplets (LDs), cellular organelles composed of neutral lipids surrounded by a monolayer of phospholipids. The HCV nucleocapsid core localizes to the surface of LDs and induces steatosis in cultured cells and mouse livers by decreasing intracellular TG degradation (lipolysis). Here we report that core at the surface of LDs interferes with the activity of adipose triglyceride lipase (ATGL), the key lipolytic enzyme in the first step of TG breakdown. Expressing core in livers or mouse embryonic fibroblasts of ATGL(-/-) mice no longer decreases TG degradation as observed in LDs from wild-type mice, supporting the model that core reduces lipolysis by engaging ATGL. Core must localize at LDs to inhibit lipolysis, as ex vivo TG hydrolysis is impaired in purified LDs coated with core but not when free core is added to LDs. Coimmunoprecipitation experiments revealed that core does not directly interact with the ATGL complex but, unexpectedly, increased the interaction between ATGL and its activator CGI-58 as well as the recruitment of both proteins to LDs. These data link the anti-lipolytic activity of the HCV core protein with altered ATGL binding to CGI-58 and the enhanced association of both proteins with LDs.

Published
2014

6. Interactions Between KIR3DS1 and HLA-F Activate Natural Killer Cells to Control HCV Replication in Cell Culture

Author

Lunemann, Sebastian, Schöbel, Anja, Kah, Janine, Fittje, Pia, Hölzemer, Angelique, Langeneckert, Annika E., Hess, Leonard U., Poch, Tobias, Martrus, Gloria, Garcia-Beltran, Wilfredo F., Körner, Christian, Ziegler, Annerose E., Richert, Laura, Oldhafer, Karl J., Schulze zur Wiesch, Julian, Schramm, Christoph, Dandri, Maura, Herker, Eva, and Altfeld, Marcus

Published
2018
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7. Acetylation of RNA Polymerase II Regulates Growth-Factor-Induced Gene Transcription in Mammalian Cells

Author

Schröder, Sebastian, Herker, Eva, Itzen, Friederike, He, Daniel, Thomas, Sean, Gilchrist, Daniel A, Kaehlcke, Katrin, Cho, Sungyoo, Pollard, Katherine S, Capra, John A, Schnölzer, Martina, Cole, Philip A, Geyer, Matthias, Bruneau, Benoit G, Adelman, Karen, and Ott, Melanie

Subjects
Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Biological Sciences, Genetics, Human Genome, Underpinning research, 1.1 Normal biological development and functioning, Aetiology, 2.1 Biological and endogenous factors, Acetylation, Animals, Early Growth Response Protein 2, Embryonic Stem Cells, Gene Expression Regulation, Genes, fos, Histones, Humans, Lysine, Promoter Regions, Genetic, RNA Polymerase II, Transcription, Genetic, p300-CBP Transcription Factors, Medical and Health Sciences, Developmental Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Lysine acetylation regulates transcription by targeting histones and nonhistone proteins. Here we report that the central regulator of transcription, RNA polymerase II, is subject to acetylation in mammalian cells. Acetylation occurs at eight lysines within the C-terminal domain (CTD) of the largest polymerase subunit and is mediated by p300/KAT3B. CTD acetylation is specifically enriched downstream of the transcription start sites of polymerase-occupied genes genome-wide, indicating a role in early stages of transcription initiation or elongation. Mutation of lysines or p300 inhibitor treatment causes the loss of epidermal growth-factor-induced expression of c-Fos and Egr2, immediate-early genes with promoter-proximally paused polymerases, but does not affect expression or polymerase occupancy at housekeeping genes. Our studies identify acetylation as a new modification of the mammalian RNA polymerase II required for the induction of growth factor response genes.

Published
2013

8. Diacylglycerol Acyltransferase-1 Localizes Hepatitis C Virus NS5A Protein to Lipid Droplets and Enhances NS5A Interaction with the Viral Capsid Core*

Author

Camus, Gregory, Herker, Eva, Modi, Ankit A, Haas, Joel T, Ramage, Holly R, Farese, Robert V, and Ott, Melanie

Subjects
Biochemistry and Cell Biology, Medical Microbiology, Biomedical and Clinical Sciences, Biological Sciences, Hepatitis - C, Infectious Diseases, Liver Disease, Emerging Infectious Diseases, Hepatitis, Chronic Liver Disease and Cirrhosis, Digestive Diseases, 2.2 Factors relating to the physical environment, Aetiology, Infection, Good Health and Well Being, Animals, Antiviral Agents, Capsid, Cell Line, Diacylglycerol O-Acyltransferase, Gene Expression Regulation, Viral, Genes, Dominant, HEK293 Cells, Hepacivirus, Hepatitis C, Humans, Lentivirus, Lipids, Mice, Microscopy, Fluorescence, Mutation, Plasmids, Protein Binding, Triglycerides, Viral Nonstructural Proteins, Chemical Sciences, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Chemical sciences
Abstract

The triglyceride-synthesizing enzyme acyl CoA:diacylglycerol acyltransferase 1 (DGAT1) plays a critical role in hepatitis C virus (HCV) infection by recruiting the HCV capsid protein core onto the surface of cellular lipid droplets (LDs). Here we find a new interaction between the non-structural protein NS5A and DGAT1 and show that the trafficking of NS5A to LDs depends on DGAT1 activity. DGAT1 forms a complex with NS5A and core and facilitates the interaction between both viral proteins. A catalytically inactive mutant of DGAT1 (H426A) blocks the localization of NS5A, but not core, to LDs in a dominant-negative manner and impairs the release of infectious viral particles, underscoring the importance of DGAT1-mediated translocation of NS5A to LDs in viral particle production. We propose a model whereby DGAT1 serves as a cellular hub for HCV core and NS5A proteins, guiding both onto the surface of the same subset of LDs, those generated by DGAT1. These results highlight the critical role of DGAT1 as a host factor for HCV infection and as a potential drug target for antiviral therapy.

Published
2013

9. Rapid Intracellular Competition between Hepatitis C Viral Genomes as a Result of Mitosis

Author

Webster, Brian, Wissing, Silke, Herker, Eva, Ott, Melanie, and Greene, Warner C

Subjects
Medical Microbiology, Biomedical and Clinical Sciences, Biological Sciences, Immunology, Hepatitis, Hepatitis - C, Digestive Diseases, Genetics, Emerging Infectious Diseases, Liver Disease, Infectious Diseases, Chronic Liver Disease and Cirrhosis, 2.2 Factors relating to the physical environment, Aetiology, Infection, Good Health and Well Being, Cell Line, Hepacivirus, Hepatocytes, Host-Pathogen Interactions, Humans, Mitosis, Viral Interference, Agricultural and Veterinary Sciences, Medical and Health Sciences, Virology, Agricultural, veterinary and food sciences, Biological sciences, Biomedical and clinical sciences
Abstract

Cells infected with hepatitis C virus (HCV) become refractory to further infection by HCV (T. Schaller et al., J. Virol. 81:4591-4603, 2007; D. M. Tscherne et al., J. Virol. 81:3693-3703, 2007). This process, termed superinfection exclusion, does not involve downregulation of surface viral receptors but instead occurs inside the cell at the level of RNA replication. The originally infecting virus may occupy replication niches or sequester host factors necessary for viral growth, preventing effective growth of viruses that enter the cell later. However, there appears to be an additional level of intracellular competition between viral genomes that occurs at or shortly following mitosis. In the setting of cellular division, when two viral replicons of equivalent fitness are present within a cell, each has an equal opportunity to exclude the other. In a population of dividing cells, the competition between viral genomes proceeds apace, randomly clearing one or the other genome from cells in the span of 9 to 12 days. These findings demonstrate a new mechanism of intracellular competition between HCV strains, which may act to further limit HCV's genetic diversity and ability to recombine in vivo.

Published
2013

12. Efficient hepatitis C virus particle formation requires diacylglycerol acyltransferase-1.

Author

Herker, Eva, Harris, Charles, Hernandez, Céline, Carpentier, Arnaud, Kaehlcke, Katrin, Rosenberg, Arielle R, Farese, Robert V, and Ott, Melanie

Subjects
Humans, Hepacivirus, Virion, Transfection, Immunoprecipitation, Virus Assembly, Diacylglycerol O-Acyltransferase, HEK293 Cells, Immunology, Medical and Health Sciences
Abstract

Hepatitis C virus (HCV) infection is closely tied to the lipid metabolism of liver cells. Here we identify the triglyceride-synthesizing enzyme diacylglycerol acyltransferase-1 (DGAT1) as a key host factor for HCV infection. DGAT1 interacts with the viral nucleocapsid core and is required for the trafficking of core to lipid droplets. Inhibition of DGAT1 activity or RNAi-mediated knockdown of DGAT1 severely impairs infectious virion production, implicating DGAT1 as a new target for antiviral therapy.

Published
2010

13. An AIF Orthologue Regulates Apoptosis in Yeast

Author

Wissing, Silke, Ludovico, Paula, Herker, Eva, Büttner, Sabrina, Engelhardt, Silvia M., Decker, Thorsten, Link, Alexander, Proksch, Astrid, Rodrigues, Fernando, Corte-Real, Manuela, Fröhlich, Kai-Uwe, Manns, Joachim, Candé, Céline, Sigrist, Stephan J., Kroemer, Guido, and Madeo, Frank

Published
2004

14. Chronological Aging Leads to Apoptosis in Yeast

Author

Herker, Eva, Jungwirth, Helmut, Lehmann, Katharina A., Maldener, Corinna, Fröhlich, Kai-Uwe, Wissing, Silke, Büttner, Sabrina, Fehr, Markus, Sigrist, Stephan, and Madeo, Frank

Published
2004

15. Unique human immune signature of Ebola virus disease in Guinea

Author

Ruibal, Paula, Oestereich, Lisa, Ldtke, Anja, Becker-Ziaja, Beate, Wozniak, David M., Kerber, Romy, Korva, Mia, Cabeza-Cabrerizo, Mar, Bore, Joseph A., Koundouno, Fara Raymond, Duraffour, Sophie, Weller, Romy, Thorenz, Anja, Cimini, Eleonora, Viola, Domenico, Agrati, Chiara, Repits, Johanna, Afrough, Babak, Cowley, Lauren A., Ngabo, Didier, Hinzmann, Julia, Mertens, Marc, Vitoriano, Ins, Logue, Christopher H., Boettcher, Jan Peter, Pallasch, Elisa, Sachse, Andreas, Bah, Amadou, Nitzsche, Katja, Kuisma, Eeva, Michel, Janine, Holm, Tobias, Zekeng, Elsa-Gayle, Garca-Dorival, Isabel, Wlfel, Roman, Stoecker, Kilian, Fleischmann, Erna, Strecker, Thomas, Di Caro, Antonino, Avi-upanc, Tatjana, Kurth, Andreas, Meschi, Silvia, Mly, Stephane, Newman, Edmund, Bocquin, Anne, Kis, Zoltan, Kelterbaum, Anne, Molkenthin, Peter, Carletti, Fabrizio, Portmann, Jasmine, Wolff, Svenja, Castilletti, Concetta, Schudt, Gordian, Fizet, Alexandra, Ottowell, Lisa J., Herker, Eva, Jacobs, Thomas, Kretschmer, Birte, Severi, Ettore, Ouedraogo, Nobila, Lago, Mar, Negredo, Anabel, Franco, Leticia, Anda, Pedro, Schmiedel, Stefan, Kreuels, Benno, Wichmann, Dominic, Addo, Marylyn M., Lohse, Ansgar W., De Clerck, Hilde, Nanclares, Carolina, Jonckheere, Sylvie, Van Herp, Michel, Sprecher, Armand, Xiaojiang, Gao, Carrington, Mary, Miranda, Osvaldo, Castro, Carlos M., Gabriel, Martin, Drury, Patrick, Formenty, Pierre, Diallo, Boubacar, Koivogui, Lamine, Magassouba, NFaly, Carroll, Miles W., Gnther, Stephan, and Muoz-Fontela, Csar

Subjects
Ebola hemorrhagic fever -- Physiological aspects, Medical research, Immune response -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Paula Ruibal [1, 2, 3, 4]; Lisa Oestereich [2, 3, 4]; Anja Ldtke [1, 2, 3, 4]; Beate Becker-Ziaja [2, 3, 4]; David M. Wozniak [2, 3, 4]; Romy [...]

Published
2016
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18. Hepatitis E virus persists in the ejaculate of chronically infected men

Author

Horvatits, Thomas, primary, Wißmann, Jan-Erik, additional, Johne, Reimar, additional, Groschup, Martin H., additional, Gadicherla, Ashish K., additional, Schulze zur Wiesch, Julian, additional, Eiden, Martin, additional, Todt, Daniel, additional, Reimer, Rudolph, additional, Dähnert, Lisa, additional, Schöbel, Anja, additional, Horvatits, Karoline, additional, Lübke, Rabea, additional, Wolschke, Christine, additional, Ayuk, Francis, additional, Rybczynski, Meike, additional, Lohse, Ansgar W., additional, Addo, Marylyn M., additional, Herker, Eva, additional, Lütgehetmann, Marc, additional, Steinmann, Eike, additional, and Pischke, Sven, additional

Published
2021
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25. Hepatitis E virus shedding in semen of chronically, but not acute HEV infected individuals

Author

Horvatits, Thomas, primary, Groschup, Martin, additional, Grönmeyer, Johanna, additional, Eiden, Martin, additional, Dähnert, Lisa, additional, Rutter, Karoline, additional, Lübke, Rabea, additional, Ayuk, Francis, additional, Sabranski, Michael, additional, Rybczynski, Meike, additional, Lohse, Ansgar, additional, Addo, Marylyn, additional, Herker, Eva, additional, zur Wiesch, Julian Schulze, additional, Luetgehetmann, Marc, additional, and Pischke, Sven, additional

Published
2020
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27. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andres, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Büttner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Corte-Real, Manuela, Costa, Vitor, Cullin, Christophe, Dawes, Ian, Dengjel, Jorn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Frohlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jimenez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stephen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystrom, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polcic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria Joao, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, Madeo, Frank, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andres, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Büttner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Corte-Real, Manuela, Costa, Vitor, Cullin, Christophe, Dawes, Ian, Dengjel, Jorn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Frohlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jimenez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stephen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystrom, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polcic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria Joao, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, and Madeo, Frank

Abstract

Elucidating the biology of yeast in its full complexity has major implications for science, medicine and industry. One of the most critical processes determining yeast life and physiology is cellular demise. However, the investigation of yeast cell death is a relatively young field, and a widely accepted set of concepts and terms is still missing. Here, we propose unified criteria for the definition of accidental, regulated, and programmed forms of cell death in yeast based on a series of morphological and biochemical criteria. Specifically, we provide consensus guidelines on the differential definition of terms including apoptosis, regulated necrosis, and autophagic cell death, as we refer to additional cell death routines that are relevant for the biology of (at least some species of) yeast. As this area of investigation advances rapidly, changes and extensions to this set of recommendations will be implemented in the years to come. Nonetheless, we strongly encourage the authors, reviewers and editors of scientific articles to adopt these collective standards in order to establish an accurate framework for yeast cell death research and, ultimately, to accelerate the progress of this vibrant field of research.

Published
2018
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28. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, D, Bauer, M, Zimmermann, A, Aguilera, A, Austriaco, N, Ayscough, K, Balzan, R, Bar-Nun, S, Barrientos, A, Belenky, P, Blondel, M, Braun, R, Breitenbach, M, Burhans, W, Buettner, S, Cavalieri, D, Chang, M, Cooper, K, Côrte-Real, M, Costa, V, Cullin, C, Dawes, I, Dengjel, J, Dickman, M, Eisenberg, T, Fahrenkrog, B, Fasel, N, Froehlich, K, Gargouri, A, Giannattasio, S, Goffrini, P, Gourlay, C, Grant, C, Greenwood, M, Guaragnella, N, Heger, T, Heinisch, J, Herker, E, Herrmann, J, Hofer, S, Jiménez-Ruiz, A, Jungwirth, H, Kainz, K, Kontoyiannis, D, Ludovico, P, Manon, S, Martegani, E, Mazzoni, C, Megeney, L, Meisinger, C, Nielsen, J, Nystroem, T, Osiewacz, H, Outeiro, T, Park, H, Pendl, T, Petranovic, D, Picot, S, Polčic, P, Powers, T, Ramsdale, M, Rinnerthaler, M, Rockenfeller, P, Ruckenstuhl, C, Schaffrath, R, Segovia, M, Severin, F, Sharon, A, Sigrist, S, Sommer-Ruck, C, Sousa, M, Thevelein, J, Thevissen, K, Titorenko, V, Toledano, M, Tuite, M, Voegtle, F, Westermann, B, Winderickx, J, Wissing, S, Woelfl, S, Zhang, Z, Zhao, R, Zhou, B, Galluzzi, L, Kroemer, G, Madeo, F, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andrés, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Buettner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Côrte-Real, Manuela, Costa, Vítor, Cullin, Christophe, Dawes, Ian, Dengjel, Jörn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Froehlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jiménez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stéphen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystroem, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polčic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria João, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, Madeo, Frank, Carmona-Gutierrez, D, Bauer, M, Zimmermann, A, Aguilera, A, Austriaco, N, Ayscough, K, Balzan, R, Bar-Nun, S, Barrientos, A, Belenky, P, Blondel, M, Braun, R, Breitenbach, M, Burhans, W, Buettner, S, Cavalieri, D, Chang, M, Cooper, K, Côrte-Real, M, Costa, V, Cullin, C, Dawes, I, Dengjel, J, Dickman, M, Eisenberg, T, Fahrenkrog, B, Fasel, N, Froehlich, K, Gargouri, A, Giannattasio, S, Goffrini, P, Gourlay, C, Grant, C, Greenwood, M, Guaragnella, N, Heger, T, Heinisch, J, Herker, E, Herrmann, J, Hofer, S, Jiménez-Ruiz, A, Jungwirth, H, Kainz, K, Kontoyiannis, D, Ludovico, P, Manon, S, Martegani, E, Mazzoni, C, Megeney, L, Meisinger, C, Nielsen, J, Nystroem, T, Osiewacz, H, Outeiro, T, Park, H, Pendl, T, Petranovic, D, Picot, S, Polčic, P, Powers, T, Ramsdale, M, Rinnerthaler, M, Rockenfeller, P, Ruckenstuhl, C, Schaffrath, R, Segovia, M, Severin, F, Sharon, A, Sigrist, S, Sommer-Ruck, C, Sousa, M, Thevelein, J, Thevissen, K, Titorenko, V, Toledano, M, Tuite, M, Voegtle, F, Westermann, B, Winderickx, J, Wissing, S, Woelfl, S, Zhang, Z, Zhao, R, Zhou, B, Galluzzi, L, Kroemer, G, Madeo, F, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andrés, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Buettner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Côrte-Real, Manuela, Costa, Vítor, Cullin, Christophe, Dawes, Ian, Dengjel, Jörn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Froehlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jiménez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stéphen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystroem, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polčic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria João, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, and Madeo, Frank

Abstract

Elucidating the biology of yeast in its full complexity has major implications for science, medicine and industry. One of the most critical processes determining yeast life and physiology is cellular demise. However, the investigation of yeast cell death is a relatively young field, and a widely accepted set of concepts and terms is still missing. Here, we propose unified criteria for the definition of accidental, regulated, and programmed forms of cell death in yeast based on a series of morphological and biochemical criteria. Specifically, we provide consensus guidelines on the differential definition of terms including apoptosis, regulated necrosis, and autophagic cell death, as we refer to additional cell death routines that are relevant for the biology of (at least some species of) yeast. As this area of investigation advances rapidly, changes and extensions to this set of recommendations will be implemented in the years to come. Nonetheless, we strongly encourage the authors, reviewers and editors of scientific articles to adopt these collective standards in order to establish an accurate framework for yeast cell death research and, ultimately, to accelerate the progress of this vibrant field of research.

Published
2018

32. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, Didac, primary, Bauer, Maria Anna, additional, Zimmermann, Andreas, additional, Aguilera, Andrés, additional, Austriaco, Nicanor, additional, Ayscough, Kathryn, additional, Balzan, Rena, additional, Bar-Nun, Shoshana, additional, Barrientos, Antonio, additional, Belenky, Peter, additional, Blondel, Marc, additional, Braun, Ralf J., additional, Breitenbach, Michael, additional, Burhans, William C., additional, Buettner, Sabrina, additional, Cavalieri, Duccio, additional, Chang, Michael, additional, Cooper, Katrina F., additional, Côrte-Real, Manuela, additional, Costa, Vítor, additional, Cullin, Christophe, additional, Dawes, Ian, additional, Dengjel, Jörn, additional, Dickman, Martin B., additional, Eisenberg, Tobias, additional, Fahrenkrog, Birthe, additional, Fasel, Nicolas, additional, Froehlich, Kai-Uwe, additional, Gargouri, Ali, additional, Giannattasio, Sergio, additional, Goffrini, Paola, additional, Gourlay, Campbell W., additional, Grant, Chris M., additional, Greenwood, Michael T., additional, Guaragnella, Nicoletta, additional, Heger, Thomas, additional, Heinisch, Juergen, additional, Herker, Eva, additional, Herrmann, Johannes M., additional, Hofer, Sebastian, additional, Jiménez-Ruiz, Antonio, additional, Jungwirth, Helmut, additional, Kainz, Katharina, additional, Kontoyiannis, Dimitrios P., additional, Ludovico, Paula, additional, Manon, Stéphen, additional, Martegani, Enzo, additional, Mazzoni, Cristina, additional, Megeney, Lynn A., additional, Meisinger, Chris, additional, Nielsen, Jens, additional, Nystroem, Thomas, additional, Osiewacz, Heinz D., additional, Outeiro, Tiago F., additional, Park, Hay-Oak, additional, Pendl, Tobias, additional, Petranovic, Dina, additional, Picot, Stephane, additional, Polčic, Peter, additional, Powers, Ted, additional, Ramsdale, Mark, additional, Rinnerthaler, Mark, additional, Rockenfeller, Patrick, additional, Ruckenstuhl, Christoph, additional, Schaffrath, Raffael, additional, Segovia, Maria, additional, Severin, Fedor F., additional, Sharon, Amir, additional, Sigrist, Stephan J., additional, Sommer-Ruck, Cornelia, additional, Sousa, Maria João, additional, Thevelein, Johan M., additional, Thevissen, Karin, additional, Titorenko, Vladimir, additional, Toledano, Michel B., additional, Tuite, Mick, additional, Voegtle, F.-Nora, additional, Westermann, Benedikt, additional, Winderickx, Joris, additional, Wissing, Silke, additional, Woelfl, Stefan, additional, Zhang, Zhaojie J., additional, Zhao, Richard Y., additional, Zhou, Bing, additional, Galluzzi, Lorenzo, additional, Kroemer, Guido, additional, and Madeo, Frank, additional

Published
2018
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35. Human liver chimeric mice as a new model of chronic hepatitis E virus infection and preclinical drug evaluation

Author

Allweiss, Lena, primary, Gass, Sofia, additional, Giersch, Katja, additional, Groth, Anne, additional, Kah, Janine, additional, Volz, Tassilo, additional, Rapp, Gianna, additional, Schöbel, Anja, additional, Lohse, Ansgar W., additional, Polywka, Susanne, additional, Pischke, Sven, additional, Herker, Eva, additional, Dandri, Maura, additional, and Lütgehetmann, Marc, additional

Published
2016
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36. Hepatitis C Virus Core Protein Decreases Lipid Droplet Turnover: A MECHANISM FOR CORE-INDUCED STEATOSIS*

Author

Harris, Charles, Herker, Eva, Farese, Robert V., and Ott, Melanie

Subjects
viruses, Lipolysis, Viral Core Proteins, Lentivirus, virus diseases, Mice, Transgenic, Hepacivirus, Fibroblasts, Lipids, digestive system diseases, Cell Line, Fatty Liver, Mice, Microscopy, Fluorescence, Centrifugation, Density Gradient, Animals, Humans, Diacylglycerol O-Acyltransferase, Triglycerides, Plasmids
Abstract

Steatosis is a frequent complication of hepatitis C virus infection. In mice, this condition is recapitulated by the expression of a single viral protein, the nucleocapsid core. Core localizes to the surface of lipid droplets (LDs) in infected liver cells through a process dependent on host diacylglycerol acyltransferase 1 (DGAT1), an enzyme that synthesizes triglycerides in the endoplasmic reticulum. Whether DGAT1 also plays a role in core-induced steatosis is uncertain. Here, we show that mouse embryonic fibroblasts isolated from DGAT1(-/-) mice are protected from core-induced steatosis, as are livers of DGAT1(-/-) mice expressing core, demonstrating that the steatosis is DGAT1-dependent. Surprisingly, core expression did not increase DGAT1 activity or triglyceride synthesis, thus excluding the possibility that core activates DGAT1 to cause steatosis. Instead, we find that DGAT1-dependent localization of core to LDs is a prerequisite for the steatogenic properties of the core. Using biochemical and immunofluorescence microscopy techniques, we show that the turnover of lipids in core-coated droplets is decreased, providing a physiological mechanism for core-induced steatosis. Our results support a bipartite model in which core first requires DGAT1 to gain access to LDs, and then LD-localized core interferes with triglyceride turnover, thus stabilizing lipid droplets and leading to steatosis.

Published
2011

37. Altruistic cell death and new ways of caspase-dependent apoptosis in Saccharomyces cerevisiae

Author

Herker, Eva and Madeo, Frank

Subjects
Apoptosis , Saccharomyces cerevisiae , aging , YCA1, Apoptosis , Saccharomyces cerevisiae , Altern, YCA1
Abstract

In den letzten Jahren konnte der Einzeller Saccharomyces cerevisiae als Modellorganismus für apoptotische Prozesse etabliert werden. Im Rahmen dieser Arbeit wurde ein altruistischer Aspekt des apoptotischen Zelltodes der Hefe aufgeklärt. Im chronologischen Altern, also unter physiologischen Bedingungen, sterben die meisten Zellen einer klonalen Kultur mit den phänotypischen Markern der Apoptose. Dieser apoptotische Zelltod ist abhängig von der Hefecaspase Yca1p und reaktiven Sauerstoffspezies (ROS). Verhindert bzw. verzögert man aber den Zelltod im chronologischen Altern durch die Deletion der Hefecaspase Yca1p birgt dies auf lange Sicht Selektionsnachteile für die Population, denn gealterte Mutantenzellen sind im adaptiven Wachstum behindert. Außerdem überlebt der Wildtyp die Mutanten in einem kompetitiven Überlebensassay, hat also im direkten Vergleich langfristig Selektionsvorteile. Es konnte zudem gezeigt werden, dass alternde Hefezellen Substanzen sezernieren, die das Überleben von anderen alten Zellen fördern. Des Weiteren konnte die durch Lsm4p Mutation ausgelöste Apoptose mechanistisch näher charakterisiert werden. Da Lsm Proteine beim mRNA splicing und decapping involviert sind, wurde untersucht, welche von beiden Funktionen bei einer Fehlregulation Apoptose auslöst. Störungen im mRNA decapping durch Mutationen oder Disruptionen der beteiligten Proteine führen zu einem Zelltod, der mit den klassischen Marken der Apoptose einhergeht. Dieser Zelltod, nicht aber die mRNA Stoffwechselstörung kann durch die Disruption der Hefecaspase Yca1p verhindert werden. During the past years, yeast has been successfully established as a model organism to study mechanisms of apoptotic regulation. In this thesis an altruistic aspect of apoptotic cell death of yeast is elucidated. During chronological aging, which represents a physiological scenario, most yeast cells of a monoclonal culture die exhibiting the phenotypic markers of apoptotic cell death. Age-induced cell death is dependent on the yeast caspase Yca1p and ROS. Disruption of age-induced apoptosis through deletion of yeast caspase YCA1 is disadvantageous for the monoclonal population, due to the fact that aged mutant cells lose the ability of regrowth. Moreover wild type cells outlast yca1 disruptants in direct competition assays indicating an evolutional advantage for wild type cells. It could be also shown that old yeast cells release substances into the medium that stimulate survival of other old cells. In addition apoptosis induced by mutation of Lsm4p was characterized further in its mechanism. As Lsm proteins have functions in mRNA splicing and decapping mechanisms, it was analyzed which process can cause apoptotic cell death. Interferences of mRNA decapping through deletion or mutation of proteins involved in this process lead to cell death accompanied by the classical markers of apoptosis. This cell death but not the disturbances in mRNA metabolism are dependent on yeast caspase Yca1p.

Published
2005

40. Induction of autophagy by spermidine promotes longevity

Author

Eisenberg, Tobias, Knauer, Heide, Schauer, Alexandra, Büttner, Sabrina, Ruckenstuhl, Christoph, Carmona-Gutierrez, Didac, Ring, Julia, Schroeder, Sabrina, Magnes, Christoph, Antonacci, Lucia, Fussi, Heike, Deszcz, Luiza, Hartl, Regina, Schraml, Elisabeth, Criollo, Alfredo, Megalou, Evgenia, Weiskopf, Daniela, Laun, Peter, Heeren, Gino, Breitenbach, Michael, Grubeck-Loebenstein, Beatrix, Herker, Eva, Fahrenkrog, Birthe, Fröhlich, Kai-Uwe, Sinner, Frank, Tavernarakis, Nektarios, Minois, Nadege, Kroemer, Guido, Madeo, Frank, Eisenberg, Tobias, Knauer, Heide, Schauer, Alexandra, Büttner, Sabrina, Ruckenstuhl, Christoph, Carmona-Gutierrez, Didac, Ring, Julia, Schroeder, Sabrina, Magnes, Christoph, Antonacci, Lucia, Fussi, Heike, Deszcz, Luiza, Hartl, Regina, Schraml, Elisabeth, Criollo, Alfredo, Megalou, Evgenia, Weiskopf, Daniela, Laun, Peter, Heeren, Gino, Breitenbach, Michael, Grubeck-Loebenstein, Beatrix, Herker, Eva, Fahrenkrog, Birthe, Fröhlich, Kai-Uwe, Sinner, Frank, Tavernarakis, Nektarios, Minois, Nadege, Kroemer, Guido, and Madeo, Frank

Abstract

info:eu-repo/semantics/published

Published
2009

45. Induction of autophagy by spermidine promotes longevity

Author

Eisenberg, Tobias, primary, Knauer, Heide, additional, Schauer, Alexandra, additional, Büttner, Sabrina, additional, Ruckenstuhl, Christoph, additional, Carmona-Gutierrez, Didac, additional, Ring, Julia, additional, Schroeder, Sabrina, additional, Magnes, Christoph, additional, Antonacci, Lucia, additional, Fussi, Heike, additional, Deszcz, Luiza, additional, Hartl, Regina, additional, Schraml, Elisabeth, additional, Criollo, Alfredo, additional, Megalou, Evgenia, additional, Weiskopf, Daniela, additional, Laun, Peter, additional, Heeren, Gino, additional, Breitenbach, Michael, additional, Grubeck-Loebenstein, Beatrix, additional, Herker, Eva, additional, Fahrenkrog, Birthe, additional, Fröhlich, Kai-Uwe, additional, Sinner, Frank, additional, Tavernarakis, Nektarios, additional, Minois, Nadege, additional, Kroemer, Guido, additional, and Madeo, Frank, additional

Published
2009
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46. Apoptosis in yeast

Author

Madeo, Frank, primary, Herker, Eva, additional, Wissing, Silke, additional, Jungwirth, Helmut, additional, Eisenberg, Tobias, additional, and Fröhlich, Kai-Uwe, additional

Published
2004
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48. A Caspase-Related Protease Regulates Apoptosis in Yeast

Author

Madeo, Frank, primary, Herker, Eva, additional, Maldener, Corinna, additional, Wissing, Silke, additional, Lächelt, Stephan, additional, Herlan, Mark, additional, Fehr, Markus, additional, Lauber, Kirsten, additional, Sigrist, Stephan J, additional, Wesselborg, Sebastian, additional, and Fröhlich, Kai-Uwe, additional

Published
2002
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49. Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells.

Author

Sungyoo Cho, Schroeder, Sebastian, Kaehlcke, Katrin, Hye-Sook Kwon, Pedal, Angelika, Herker, Eva, Schnoelzer, Martina, and Ott, Melanie

Subjects
ACETYLATION, CYCLINS, GROWTH factors, CELLS, RNA polymerases
Abstract

The elongation competence of the RNA polymerase II complex is critically dependent on the positive transcription elongation factor b (P-TEFb). P-TEFb exists in two forms in cells, an active form composed of cyclin T1 and CDK9 and an inactive form, in which cyclin T1/CDK9 is sequestered by Hexim1 and 7SK snRNA. Here, we report that partitioning of active and inactive P-TEFb is regulated by acetylation of cyclin T1. Cyclin T1 acetylation triggers dissociation of Hexim1 and 7SK snRNA from cyclin T1/CDK9 and activates the transcriptional activity of P-TEFb. This activation is lost in P-TEFb complexes containing cyclin T1 that can no longer be acetylated. An acetylation-deficient cyclin T1 mutant dominantly suppresses NF-κB-mediated activation of the interleukin-8 promoter but continues to synergize normally with the HIV Tat protein to transactivate the HIV long terminal repeat. These findings support the model that acetylation of cyclin T1 serves as a physiological switch that liberates P-TEFb from its endogenous inhibitors Hexim1 and 7SK snRNA, but is not required for the cooperative action with HIV Tat. [ABSTRACT FROM AUTHOR]

Published
2009
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50. A comparison of the aging and apoptotic transcriptome of Saccharomyces cerevisiae

Author

Laun, Peter, Ramachandran, Lakshmi, Jarolim, Stefanie, Herker, Eva, Liang, Ping, Wang, Jianxin, Weinberger, Martin, Burhans, Debra T., Suter, Bernhard, Madeo, Frank, Burhans, William C., and Breitenbach, Michael

Subjects
YEAST, APOPTOSIS, GENES, MITOCHONDRIA, CENTRIFUGATION
Abstract

Abstract: In this paper, we present the results of global transcript analysis by the microarray technique of senescent and apoptotic yeast cells. We compared young daughter and old mother cells isolated by elutriation centrifugation, and non-apoptotic and apoptotic cells induced either by a temperature shift of the cdc48 S565G temperature-sensitive mutant or of the orc2-1 temperature-sensitive mutant. The majority of all genes found to be differentially regulated in these three physiological situations was upregulated, indicating that a cellular death process was initiated rather than an unspecific shut-down of gene expression due to immediate killing. The functional classes of genes upregulated in all three conditions were largely the same, although individual genes were in many cases not identical. The largest group of genes involved were nuclear genes coding for mitochondrial components or functions, which is understandable given the fact that apoptosis can be triggered by mitochondrially generated oxygen radicals and that mitochondria play an important role in the execution of apoptosis. Other functional classes consisted of genes involved in DNA damage response, in cell cycle regulation and checkpoints, in DNA repair, and in membrane lipid and cell wall synthesis. These functional classes represent the response of the cell to the known cellular insults, which occur during aging and apoptosis. As we have shown previously, final-stage senescent yeast mother cells (of the wild-type) are apoptotic. [Copyright &y& Elsevier]

Published
2005
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