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220 results on '"Bobik A"'

1. EUSO-SPB1 mission and science

Author

Abdellaoui, G., primary, Abe, S., additional, Adams, J.H., additional, Allard, D., additional, Alonso, G., additional, Anchordoqui, L., additional, Anzalone, A., additional, Arnone, E., additional, Asano, K., additional, Attallah, R., additional, Attoui, H., additional, Pernas, M. Ave, additional, Bachmann, R., additional, Bacholle, S., additional, Bagheri, M., additional, Bakiri, M., additional, Baláz, J., additional, Barghini, D., additional, Bartocci, S., additional, Battisti, M., additional, Bayer, J., additional, Beldjilali, B., additional, Belenguer, T., additional, Belkhalfa, N., additional, Bellotti, R., additional, Belov, A.A., additional, Benmessai, K., additional, Bertaina, M., additional, Bertone, P.F., additional, Biermann, P.L., additional, Bisconti, F., additional, Blaksley, C., additional, Blanc, N., additional, Blin-Bondil, S., additional, Bobik, P., additional, Bogomilov, M., additional, Bolmgren, K., additional, Bozzo, E., additional, Briz, S., additional, Bruno, A., additional, Caballero, K.S., additional, Cafagna, F., additional, Cambié, G., additional, Campana, D., additional, Capdevielle, J.N., additional, Capel, F., additional, Caramete, A., additional, Caramete, L., additional, Caruso, R., additional, Casolino, M., additional, Cassardo, C., additional, Castellina, A., additional, Catalano, O., additional, Cellino, A., additional, Černý, K., additional, Chikawa, M., additional, Chiritoi, G., additional, Christl, M.J., additional, Colalillo, R., additional, Conti, L., additional, Cotto, G., additional, Crawford, H.J., additional, Cremonini, R., additional, Creusot, A., additional, Cummings, A., additional, de Castro Gónzalez, A., additional, de la Taille, C., additional, del Peral, L., additional, Desiato, J., additional, Damian, A. Diaz, additional, Diesing, R., additional, Dinaucourt, P., additional, Djakonow, A., additional, Djemil, T., additional, Ebersoldt, A., additional, Ebisuzaki, T., additional, Eser, J., additional, Fenu, F., additional, Fernández-González, S., additional, Ferrarese, S., additional, Filippatos, G., additional, Finch, W., additional, Fornaro, C., additional, Fouka, M., additional, Franceschi, A., additional, Franchini, S., additional, Fuglesang, C., additional, Fujii, T., additional, Fukushima, M., additional, Galeotti, P., additional, García-Ortega, E., additional, Gardiol, D., additional, Garipov, G.K., additional, Gascón, E., additional, Gazda, E., additional, Genci, J., additional, Golzio, A., additional, Gorodetzky, P., additional, Gregg, R., additional, Green, A., additional, Guarino, F., additional, Guépin, C., additional, Guzmán, A., additional, Hachisu, Y., additional, Haungs, A., additional, Heigbes, T., additional, Carretero, J. Hernández, additional, Hulett, L., additional, Ikeda, D., additional, Inoue, N., additional, Inoue, S., additional, Isgrò, F., additional, Itow, Y., additional, Jammer, T., additional, Jeong, S., additional, Jochum, J., additional, Joven, E., additional, Judd, E.G., additional, Jung, A., additional, Kajino, F., additional, Kajino, T., additional, Kalli, S., additional, Kaneko, I., additional, Kasztelan, M., additional, Katahira, K., additional, Kawai, K., additional, Kawasaki, Y., additional, Kedadra, A., additional, Khales, H., additional, Khrenov, B.A., additional, Kim, Jeong-Sook, additional, Kim, Soon-Wook, additional, Kleifges, M., additional, Klimov, P.A., additional, Kreykenbohm, I., additional, Krizmanic, J.F., additional, Królik, K., additional, Kungel, V., additional, Kurihara, Y., additional, Kusenko, A., additional, Kuznetsov, E., additional, Lahmar, H., additional, Lakhdari, F., additional, Licandro, J., additional, Campano, L. López, additional, Martínez, F. López, additional, Mackovjak, S., additional, Mahdi, M., additional, Mandát, D., additional, Manfrin, M., additional, Marcelli, L., additional, Marcos, J.L., additional, Marszał, W., additional, Martín, Y., additional, Martinez, O., additional, Mase, K., additional, Mastafa, M., additional, Matthews, J.N., additional, Mebarki, N., additional, Medina-Tanco, G., additional, Menshikov, A., additional, Merino, A., additional, Mese, M., additional, Meseguer, J., additional, Meyer, S.S., additional, Mimouni, J., additional, Miyamoto, H., additional, Mizumoto, Y., additional, Monaco, A., additional, de los Ríos, J.A. Morales, additional, Nachtman, J.M., additional, Nagataki, S., additional, Naitamor, S., additional, Napolitano, T., additional, Neronov, A., additional, Nomoto, K., additional, Nonaka, T., additional, Ogawa, T., additional, Ogio, S., additional, Ohmori, H., additional, Olinto, A.V., additional, Onel, Y., additional, Osteria, G., additional, Otte, A.N., additional, Pagliaro, A., additional, Painter, W., additional, Panasyuk, M.I., additional, Panico, B., additional, Parizot, E., additional, Park, I.H., additional, Pastircak, B., additional, Paul, T., additional, Pech, M., additional, Pérez-Grande, I., additional, Perfetto, F., additional, Peter, T., additional, Picozza, P., additional, Pindado, S., additional, Piotrowski, L.W., additional, Piraino, S., additional, Plebaniak, Z., additional, Pollini, A., additional, Popescu, E.M., additional, Prevete, R., additional, Prévôt, G., additional, Prieto, H., additional, Przybylak, M., additional, Puehlhofer, G., additional, Putis, M., additional, Reardon, P., additional, Reno, M.H., additional, Reyes, M., additional, Ricci, M., additional, Frías, M.D. Rodríguez, additional, Matamala, O.F. Romero, additional, Ronga, F., additional, Sabau, M.D., additional, Saccá, G., additional, Sagawa, H., additional, Sahnoune, Z., additional, Saito, A., additional, Sakaki, N., additional, Salazar, H., additional, Sánchez, J.L., additional, Balanzar, J.C. Sanchez, additional, Santangelo, A., additional, Sanz-Andrés, A., additional, Saprykin, O.A., additional, Sarazin, F., additional, Sato, M., additional, Scagliola, A., additional, Schanz, T., additional, Schieler, H., additional, Schovánek, P., additional, Scotti, V., additional, Serra, M., additional, Sharakin, S.A., additional, Shimizu, H.M., additional, Shinozaki, K., additional, Soriano, J.F., additional, Sotgiu, A., additional, Stan, I., additional, Strharský, I., additional, Sugiyama, N., additional, Supanitsky, D., additional, Suzuki, M., additional, Szabelski, J., additional, Tajima, N., additional, Tajima, T., additional, Takahashi, Y., additional, Takeda, M., additional, Takizawa, Y., additional, Talai, M.C., additional, Tameda, Y., additional, Tenzer, C., additional, Thomas, S.B., additional, Tibolla, O., additional, Tkachev, L.G., additional, Tomida, T., additional, Tone, N., additional, Toscano, S., additional, Traïche, M., additional, Tsunesada, Y., additional, Tsuno, K., additional, Turriziani, S., additional, Uchihori, Y., additional, Valdés-Galicia, J.F., additional, Vallania, P., additional, Valore, L., additional, Vankova-Kirilova, G., additional, Venters, T.M., additional, Vigorito, C., additional, Villaseñor, L., additional, Vlcek, B., additional, von Ballmoos, P., additional, Vrabel, M., additional, Wada, S., additional, Watanabe, J., additional, Watts, J., additional, Muñoz, R. Weigand, additional, Weindl, A., additional, Wiencke, L., additional, Wille, M., additional, Wilms, J., additional, Yamamoto, T., additional, Yang, J., additional, Yano, H., additional, Yashin, I.V., additional, Yonetoku, D., additional, Yoshida, S., additional, Young, R., additional, Zgura, I.S., additional, Zotov, M.Yu., additional, and Marchi, A. Zuccaro, additional

Published
2024
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3. Targeting single inflammation marker IL-1Β does not alter development of advanced atherosclerotic plaques in high-fat diet-fed ApoE knockout mice

Author

Wallert, M., primary, Maluenda, A., additional, Chen, Y.-C., additional, Searle, A., additional, Ziegler, M., additional, Ying, Y.-L., additional, Wu, E., additional, Hosseini, H., additional, Noonan, J., additional, Zaldivia, M., additional, Börmel, L., additional, Eddy, E., additional, Bongcaron, V., additional, Witt, R., additional, Wang, X., additional, Lorkowski, S., additional, Bobik, A., additional, Robertson, A., additional, Drummond, G., additional, Mcfadyen, J., additional, and Peter, K., additional

Published
2023
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4. Impact of Additional Public Cord Blood Donation Sites on Racial/Ethnic Diversity of Bank Inventory, Cord Blood Units Distributed and Cord Blood Recipients

Author

Finney, Marcie, primary, Bobik-Kurz, Kathy, additional, Chase, JoAnn, additional, Boucher, Sue, additional, Laster, Candice, additional, Wood, Bridget, additional, Thut, Dawn, additional, Dedino, Faith, additional, Alemany, Angela, additional, Shields, Sara, additional, Vincent, Kim, additional, DiNello, Denise, additional, Adamo, Michelle, additional, Evans, Kara, additional, Walker, Molly, additional, Van’t Hof, Wouter, additional, and Laughlin, Mary J., additional

Published
2022
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7. Impact of Additional Public Cord Blood Donation Sites on Racial/Ethnic Diversity of Bank Inventory, Cord Blood Units Distributed and Cord Blood Recipients

Author

Marcie Finney, Kathy Bobik-Kurz, JoAnn Chase, Sue Boucher, Candice Laster, Bridget Wood, Dawn Thut, Faith Dedino, Angela Alemany, Sara Shields, Kim Vincent, Denise DiNello, Michelle Adamo, Kara Evans, Molly Walker, Wouter Van’t Hof, and Mary J. Laughlin

Subjects
Transplantation, Molecular Medicine, Immunology and Allergy, Cell Biology, Hematology
Published
2022

8. Killer cells in atherosclerosis

Author

Tin Kyaw, Ban-Hock Toh, Peter G. Tipping, and Alex Bobik

Subjects
0301 basic medicine, Pharmacology, Innate immune system, Lymphokine-activated killer cell, biology, Antigen presentation, CD28, chemical and pharmacologic phenomena, Atherosclerosis, Natural killer T cell, Killer Cells, Natural, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, Immune system, Granzyme, Immunology, biology.protein, Animals, Humans, Cytotoxic T cell, Molecular Targeted Therapy, 030215 immunology
Abstract

Cytotoxic lymphocytes (killer cells) play a critical role in host defence mechanisms, protecting against infections and in tumour surveillance. They can also exert detrimental effects in chronic inflammatory disorders and in autoimmune diseases. Tissue cell death and necrosis are prominent features of advanced atherosclerotic lesions including vulnerable/unstable lesions which are largely responsible for most heart attacks and strokes. Evidence for accumulation of killer cells in both human and mouse lesions together with their cytotoxic potential strongly suggest that these cells contribute to cell death and necrosis in lesions leading to vulnerable plaque development and potentially plaque rupture. Killer cells can be divided into two groups, adaptive and innate immune cells depending on whether they require antigen presentation for activation. Activated killer cells detect damaged or stressed cells and kill by cytotoxic mechanisms that include perforin, granzymes, TRAIL or FasL and in some cases TNF-α. In this review, we examine current knowledge on killer cells in atherosclerosis, including CD8 T cells, CD28- CD4 T cells, natural killer cells and γδ-T cells, mechanisms responsible for their activation, their migration to developing lesions and effector functions. We also discuss pharmacological strategies to prevent their deleterious vascular effects by preventing/limiting their cytotoxic effects within atherosclerotic lesions as well as potential immunomodulatory therapies that might better target lesion-resident killer cells, to minimise any compromise of the immune system, which could result in increased susceptibility to infections and reductions in tumour surveillance.

Published
2017

9. Ultra-violet imaging of the night-time earth by EUSO-Balloon towards space-based ultra-high energy cosmic ray observations

Author

Abdellaoui, G., primary, Abe, S., additional, Adams, J.H., additional, Ahriche, A., additional, Allard, D., additional, Allen, L., additional, Alonso, G., additional, Anchordoqui, L., additional, Anzalone, A., additional, Arai, Y., additional, Asano, K., additional, Attallah, R., additional, Attoui, H., additional, Ave Pernas, M., additional, Bacholle, S., additional, Bakiri, M., additional, Baragatti, P., additional, Barrillon, P., additional, Bartocci, S., additional, Bayer, J., additional, Beldjilali, B., additional, Belenguer, T., additional, Belkhalfa, N., additional, Bellotti, R., additional, Belov, A., additional, Belov, K., additional, Benmessai, K., additional, Bertaina, M., additional, Biermann, P.L., additional, Biktemerova, S., additional, Bisconti, F., additional, Blanc, N., additional, Błȩcki, J., additional, Blin-Bondil, S., additional, Bobik, P., additional, Bogomilov, M., additional, Bozzo, E., additional, Briz, S., additional, Bruno, A., additional, Caballero, K.S., additional, Cafagna, F., additional, Campana, D., additional, Capdevielle, J-N., additional, Capel, F., additional, Caramete, A., additional, Caramete, L., additional, Carlson, P., additional, Caruso, R., additional, Casolino, M., additional, Cassardo, C., additional, Castellina, A., additional, Catalano, C., additional, Catalano, O., additional, Cellino, A., additional, Chikawa, M., additional, Chiritoi, G., additional, Christl, M.J., additional, Connaughton, V., additional, Conti, L., additional, Cordero, G., additional, Cotto, G., additional, Crawford, H.J., additional, Cremonini, R., additional, Csorna, S., additional, Cummings, A., additional, Dagoret-Campagne, S., additional, de Castro, A.J., additional, De Donato, C., additional, de la Taille, C., additional, De Santis, C., additional, del Peral, L., additional, Di Martino, M., additional, Diaz Damian, A., additional, Djemil, T., additional, Dutan, I., additional, Ebersoldt, A., additional, Ebisuzaki, T., additional, Engel, R., additional, Eser, J., additional, Fenu, F., additional, Fernández-González, S., additional, Ferrarese, S., additional, Flamini, M., additional, Fornaro, C., additional, Fouka, M., additional, Franceschi, A., additional, Franchini, S., additional, Fuglesang, C., additional, Fujii, T., additional, Fujimoto, J., additional, Fukushima, M., additional, Galeotti, P., additional, García-Ortega, E., additional, Garipov, G., additional, Gascón, E., additional, Genci, J., additional, Giraudo, G., additional, González Alvarado, C., additional, Gorodetzky, P., additional, Greg, R., additional, Guarino, F., additional, Guzmán, A., additional, Hachisu, Y., additional, Haiduc, M., additional, Harlov, B., additional, Haungs, A., additional, Hernández Carretero, J., additional, Hidber Cruz, W., additional, Ikeda, D., additional, Inoue, N., additional, Inoue, S., additional, Isgrò, F., additional, Itow, Y., additional, Jammer, T., additional, Jeong, S., additional, Joven, E., additional, Judd, E.G., additional, Jung, A., additional, Jochum, J., additional, Kajino, F., additional, Kajino, T., additional, Kalli, S., additional, Kaneko, I., additional, Karadzhov, Y., additional, Karczmarczyk, J., additional, Katahira, K., additional, Kawai, K., additional, Kawasaki, Y., additional, Kedadra, A., additional, Khales, H., additional, Khrenov, B.A., additional, Kim, Jeong-Sook, additional, Kim, Soon-Wook, additional, Kleifges, M., additional, Klimov, P.A., additional, Kolev, D., additional, Krantz, H., additional, Kreykenbohm, I., additional, Krizmanic, J.F., additional, Kudela, K., additional, Kurihara, Y., additional, Kusenko, A., additional, Kuznetsov, E., additional, La Barbera, A., additional, Lachaud, C., additional, Lahmar, H., additional, Lakhdari, F., additional, Larsson, O., additional, Lee, J., additional, Licandro, J., additional, López Campano, L., additional, López, F., additional, Maccarone, M.C., additional, Mackovjak, S., additional, Mahdi, M., additional, Maravilla, D., additional, Marcelli, L., additional, Marcos, J.L., additional, Marini, A., additional, Marszał, W., additional, Martens, K., additional, Martín, Y., additional, Martinez, O., additional, Martucci, M., additional, Masciantonio, G., additional, Mase, K., additional, Mastafa, M., additional, Matev, R., additional, Matthews, J.N., additional, Mebarki, N., additional, Medina-Tanco, G., additional, Mendoza, M.A., additional, Menshikov, A., additional, Merino, A., additional, Meseguer, J., additional, Meyer, S.S., additional, Mimouni, J., additional, Miyamoto, H., additional, Mizumoto, Y., additional, Monaco, A., additional, Morales de los Ríos, J.A., additional, Moretto, C., additional, Nagataki, S., additional, Naitamor, S., additional, Napolitano, T., additional, Nava, R., additional, Neronov, A., additional, Nomoto, K., additional, Nonaka, T., additional, Ogawa, T., additional, Ogio, S., additional, Ohmori, H., additional, Olinto, A.V., additional, Orleański, P., additional, Osteria, G., additional, Pagliaro, A., additional, Painter, W., additional, Panasyuk, M.I., additional, Panico, B., additional, Parizot, E., additional, Park, I.H., additional, Pastircak, B., additional, Patzak, T., additional, Paul, T., additional, Pérez-Grande, I., additional, Perfetto, F., additional, Peter, T., additional, Picozza, P., additional, Pindado, S., additional, Piotrowski, L.W., additional, Piraino, S., additional, Placidi, L., additional, Plebaniak, Z., additional, Pliego, S., additional, Pollini, A., additional, Polonsky, Z., additional, Popescu, E.M., additional, Prat, P., additional, Prévôt, G., additional, Prieto, H., additional, Puehlhofer, G., additional, Putis, M., additional, Rabanal, J., additional, Radu, A.A., additional, Reyes, M., additional, Rezazadeh, M., additional, Ricci, M., additional, Rodríguez Frías, M.D., additional, Ronga, F., additional, Roudil, G., additional, Rusinov, I., additional, Rybczyński, M., additional, Sabau, M.D., additional, Sáez Cano, G., additional, Sagawa, H., additional, Sahnoune, Z., additional, Saito, A., additional, Sakaki, N., additional, Salazar, H., additional, Sanchez Balanzar, J.C., additional, Sánchez, J.L., additional, Santangelo, A., additional, Sanz-Andrés, A., additional, Sanz Palomino, M., additional, Saprykin, O., additional, Sarazin, F., additional, Sato, M., additional, Schanz, T., additional, Schieler, H., additional, Scotti, V., additional, Selmane, S., additional, Semikoz, D., additional, Serra, M., additional, Sharakin, S., additional, Shimizu, H.M., additional, Shinozaki, K., additional, Shirahama, T., additional, Spataro, B., additional, Stan, I., additional, Sugiyama, T., additional, Supanitsky, D., additional, Suzuki, M., additional, Szabelska, B., additional, Szabelski, J., additional, Tajima, N., additional, Tajima, T., additional, Takahashi, Y., additional, Takami, H., additional, Takeda, M., additional, Takizawa, Y., additional, Talai, M.C., additional, Tenzer, C., additional, Thomas, S.B., additional, Tibolla, O., additional, Tkachev, L., additional, Tokuno, H., additional, Tomida, T., additional, Tone, N., additional, Toscano, S., additional, Traïche, M., additional, Tsenov, R., additional, Tsunesada, Y., additional, Tsuno, K., additional, Tubbs, J., additional, Turriziani, S., additional, Uchihori, Y., additional, Vaduvescu, O., additional, Valdés-Galicia, J.F., additional, Vallania, P., additional, Vankova, G., additional, Vigorito, C., additional, Villaseñor, L., additional, Vlcek, B., additional, von Ballmoos, P., additional, Vrabel, M., additional, Wada, S., additional, Watanabe, J., additional, Watts, J., additional, Weber, M., additional, Weigand Muñoz, R., additional, Weindl, A., additional, Wiencke, L., additional, Wille, M., additional, Wilms, J., additional, Włodarczyk, Z., additional, Yamamoto, T., additional, Yang, J., additional, Yano, H., additional, Yashin, I.V., additional, Yonetoku, D., additional, Yoshida, S., additional, Young, R., additional, Zgura, I.S., additional, Zotov, M.Yu., additional, and Zuccaro Marchi, A., additional

Published
2019
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10. EUSO-TA – First results from a ground-based EUSO telescope

Author

Abdellaoui, G., primary, Abe, S., additional, Adams, J.H., additional, Ahriche, A., additional, Allard, D., additional, Allen, L., additional, Alonso, G., additional, Anchordoqui, L., additional, Anzalone, A., additional, Arai, Y., additional, Asano, K., additional, Attallah, R., additional, Attoui, H., additional, Ave Pernas, M., additional, Bacholle, S., additional, Bakiri, M., additional, Baragatti, P., additional, Barrillon, P., additional, Bartocci, S., additional, Bayer, J., additional, Beldjilali, B., additional, Belenguer, T., additional, Belkhalfa, N., additional, Bellotti, R., additional, Belov, A., additional, Belov, K., additional, Belz, J.W., additional, Benmessai, K., additional, Bertaina, M., additional, Biermann, P.L., additional, Biktemerova, S., additional, Bisconti, F., additional, Blanc, N., additional, Blecki, J., additional, Blin-Bondil, S., additional, Bobik, P., additional, Bogomilov, M., additional, Bozzo, E., additional, Bruno, A., additional, Caballero, K.S., additional, Cafagna, F., additional, Campana, D., additional, Capdevielle, J-N., additional, Capel, F., additional, Caramete, A., additional, Caramete, L., additional, Carlson, P., additional, Caruso, R., additional, Casolino, M., additional, Cassardo, C., additional, Castellina, A., additional, Catalano, O., additional, Cellino, A., additional, Chikawa, M., additional, Chiritoi, G., additional, Christl, M.J., additional, Connaughton, V., additional, Conti, L., additional, Cordero, G., additional, Cotto, G., additional, Crawford, H.J., additional, Cremonini, R., additional, Csorna, S., additional, Cummings, A., additional, Dagoret-Campagne, S., additional, De Donato, C., additional, de la Taille, C., additional, De Santis, C., additional, del Peral, L., additional, Di Martino, M., additional, Djemil, T., additional, Dutan, I., additional, Ebersoldt, A., additional, Ebisuzaki, T., additional, Engel, R., additional, Eser, J., additional, Fenu, F., additional, Fernández-González, S., additional, Fernández-Soriano, J., additional, Ferrarese, S., additional, Flamini, M., additional, Fornaro, C., additional, Fouka, M., additional, Franceschi, A., additional, Franchini, S., additional, Fuglesang, C., additional, Fujii, T., additional, Fujimoto, J., additional, Fukushima, M., additional, Galeotti, P., additional, García-Ortega, E., additional, Garipov, G., additional, Gascón, E., additional, Genci, J., additional, Giraudo, G., additional, González Alvarado, C., additional, Gorodetzky, P., additional, Greg, R., additional, Guarino, F., additional, Guzmán, A., additional, Hachisu, Y., additional, Haiduc, M., additional, Harlov, B., additional, Haungs, A., additional, Hernández Carretero, J., additional, Hidber Cruz, W., additional, Ikeda, D., additional, Inoue, N., additional, Inoue, S., additional, Isgrò, F., additional, Itow, Y., additional, Jammer, T., additional, Jeong, S., additional, Joven, E., additional, Judd, E.G., additional, Jung, A., additional, Jochum, J., additional, Kajino, F., additional, Kajino, T., additional, Kalli, S., additional, Kaneko, I., additional, Karadzhov, Y., additional, Karczmarczyk, J., additional, Katahira, K., additional, Kawai, K., additional, Kawasaki, Y., additional, Kedadra, A., additional, Khales, H., additional, Khrenov, B.A., additional, Kim, Jeong-Sook, additional, Kim, Soon-Wook, additional, Kleifges, M., additional, Klimov, P.A., additional, Kolev, D., additional, Krantz, H., additional, Kreykenbohm, I., additional, Kudela, K., additional, Kurihara, Y., additional, Kusenko, A., additional, Kuznetsov, E., additional, La Barbera, A., additional, Lachaud, C., additional, Lahmar, H., additional, Lakhdari, F., additional, Larsson, O., additional, Lee, J., additional, Licandro, J., additional, López Campano, L., additional, Maccarone, M.C., additional, Mackovjak, S., additional, Mahdi, M., additional, Maravilla, D., additional, Marcelli, L., additional, Marcos, J.L., additional, Marini, A., additional, Marszal, W., additional, Martens, K., additional, Martín, Y., additional, Martinez, O., additional, Martucci, M., additional, Masciantonio, G., additional, Mase, K., additional, Mustafa, M., additional, Matev, R., additional, Matthews, J.N., additional, Mebarki, N., additional, Medina-Tanco, G., additional, Mendoza, M.A., additional, Menshikov, A., additional, Merino, A., additional, Meseguer, J., additional, Meyer, S.S., additional, Mimouni, J., additional, Miyamoto, H., additional, Mizumoto, Y., additional, Monaco, A., additional, Morales de los Ríos, J.A., additional, Nagataki, S., additional, Naitamor, S., additional, Napolitano, T., additional, Nava, R., additional, Neronov, A., additional, Nomoto, K., additional, Nonaka, T., additional, Ogawa, T., additional, Ogio, S., additional, Ohmori, H., additional, Olinto, A.V., additional, Orleański, P., additional, Osteria, G., additional, Pagliaro, A., additional, Painter, W., additional, Panasyuk, M.I., additional, Panico, B., additional, Parizot, E., additional, Park, I.H., additional, Pastircak, B., additional, Patzak, T., additional, Paul, T., additional, Pérez-Grande, I., additional, Perfetto, F., additional, Peter, T., additional, Picozza, P., additional, Pindado, S., additional, Piotrowski, L.W., additional, Piraino, S., additional, Placidi, L., additional, Plebaniak, Z., additional, Pliego, S., additional, Pollini, A., additional, Polonski, Z., additional, Popescu, E.M., additional, Prat, P., additional, Prévôt, G., additional, Prieto, H., additional, Puehlhofer, G., additional, Putis, M., additional, Rabanal, J., additional, Radu, A.A., additional, Reyes, M., additional, Rezazadeh, M., additional, Ricci, M., additional, Rodríguez Frías, M.D., additional, Ronga, F., additional, Roudil, G., additional, Rusinov, I., additional, Rybczyński, M., additional, Sabau, M.D., additional, Sáez Cano, G., additional, Sagawa, H., additional, Sahnoune, Z., additional, Saito, A., additional, Sakaki, N., additional, Salazar, H., additional, Sanchez Balanzar, J.C., additional, Sánchez, J.L., additional, Santangelo, A., additional, Sanz-Andrés, A., additional, Sanz Palomino, M., additional, Saprykin, O., additional, Sarazin, F., additional, Sato, M., additional, Schanz, T., additional, Schieler, H., additional, Scotti, V., additional, Selmane, S., additional, Semikoz, D., additional, Serra, M., additional, Sharakin, S., additional, Shimizu, H.M., additional, Shin, H.S., additional, Shinozaki, K., additional, Shirahama, T., additional, Sokolsky, P., additional, Spataro, B., additional, Stan, I., additional, Sugiyama, T., additional, Supanitsky, D., additional, Suzuki, M., additional, Szabelska, B., additional, Szabelski, J., additional, Tajima, N., additional, Tajima, T., additional, Takahashi, Y., additional, Takami, H., additional, Takeda, M., additional, Takizawa, Y., additional, Talai, M.C., additional, Tameda, Y., additional, Tenzer, C., additional, Thomas, S.B., additional, Thomson, G.B., additional, Tibolla, O., additional, Tkachev, L., additional, Tokuno, H., additional, Tomida, T., additional, Tone, N., additional, Toscano, S., additional, Traïche, M., additional, Tsenov, R., additional, Tsunesada, Y., additional, Tsuno, K., additional, Tubbs, J., additional, Turriziani, S., additional, Uchihori, Y., additional, Vaduvescu, O., additional, Valdés-Galicia, J.F., additional, Vallania, P., additional, Vankova, G., additional, Vigorito, C., additional, Villaseñor, L., additional, Vlcek, B., additional, von Ballmoos, P., additional, Vrabel, M., additional, Wada, S., additional, Watanabe, J., additional, Watts, J., additional, Weber, M., additional, Weigand Muñoz, R., additional, Weindl, A., additional, Wiencke, L., additional, Wille, M., additional, Wilms, J., additional, Włodarczyk, Z., additional, Yamamoto, T., additional, Yang, J., additional, Yano, H., additional, Yashin, I.V., additional, Yonetoku, D., additional, Yoshida, S., additional, Young, R., additional, Zgura, I.S., additional, Zotov, M.Yu., additional, and Zuccaro Marchi, A., additional

Published
2018
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11. Effects of solar modulation on the cosmic ray positron fraction

Author

Matteo Boschini, Pavol Bobik, Mauro Tacconi, Pier-Giorgio Rancoita, Karel Kudela, S. Pensotti, D. Grandi, Stefano Della Torre, C. Consolandi, Massimo Gervasi, Davide Rozza, Della Torre, S, Bobik, P, Boschini, M, Consolandi, C, Gervasi, M, Grandi, D, Kudela, K, Pensotti, S, Rancoita, P, Rozza, D, and Tacconi, M

Subjects
Physics, Solar modulation, Atmospheric Science, PAMELA detector, Astrophysics::High Energy Astrophysical Phenomena, Monte Carlo method, Aerospace Engineering, Astronomy and Astrophysics, Cosmic ray, Astrophysics, Leptons, law.invention, Heliosphere, FIS/05 - ASTRONOMIA E ASTROFISICA, Geophysics, Positron, Space and Planetary Science, law, Physics::Space Physics, General Earth and Planetary Sciences, Ultra-high-energy cosmic ray, Diffusion (business), Convection–diffusion equation
Abstract

We implemented a 2D Monte Carlo model to simulate the solar modulation of galactic cosmic rays. The model is based on the Parker’s transport equation which contains diffusion, convection, particle drift and energy loss. Following the evolution in time of the solar activity, we are able to modulate a local interstellar spectrum (LIS), that we assumed isotropic beyond the termination shock, down to the Earth position inside the heliosphere. In this work we focused our attention to the cosmic ray positron fraction at energy below ∼10 GeV, showing how the particle drift processes could explain different results for AMS-01 and PAMELA. We compare our modulated spectra with observations at Earth, and then make a prediction of the cosmic ray positron fraction for the AMS-02 experiment.

Published
2012

12. Clostridium Difficile Colonization and Disease in Patients Undergoing Hematopoietic Stem Cell Transplantation

Author

Mark Weiss, Jackrapong Bruminhent, Ubaldo Martinez Outschoorn, John L. Wagner, Matthew Carabasi, Neal Flomenberg, Scott W. Keith, Joanne Filicko-O'Hara, Sarah E. Hegarty, Margaret Kasner, Carol Hu, Phyllis Flomenberg, Richard Sunday, Brent Bobik, Seyfettin Onder Alpdogan, and Zi-Xuan Wang

Subjects
Male, Colonization, medicine.medical_specialty, Transplantation Conditioning, medicine.medical_treatment, Clostridium difficile toxin A, Hematopoietic stem cell transplantation, Risk Factors, Internal medicine, Clostridium difficile infection, medicine, Humans, Typing, Transplantation, Clostridioides difficile, business.industry, Incidence (epidemiology), Odds ratio, Hematology, Middle Aged, Clostridium difficile, Immunology, Clostridium Infections, Multilocus sequence typing, Female, business
Abstract

s There was an increase in the Clostridium difficile infection (CDI) rate in our bone marrow transplantation unit. To evaluate the role of unit-based transmission, C. difficile screening was performed on adult patients admitted for hematopoietic stem cell transplantation (HSCT) over a 2-year period, and C. difficile isolates were typed. C. difficile testing was performed using a 2-step C. difficile glutamate dehydrogenase antigen plus toxin A/B enzyme immunoassay (EIA) and cytotoxin assay (or molecular toxin assay). Multilocus sequence typing (MLST) was performed on toxin-positive whole stool samples. A retrospective chart review was performed on all patients with a positive toxin assay. Sixteen of 150 patients (10.7%) had toxigenic C. difficile colonization (CDC) on admission. The overall incidence of CDI within 100 days after HSCT was 24.7% (37 of 150). The median time to diagnosis of CDI was 3.5 days after HSCT. In an adjusted logistic regression model, CDC on admission was a significant risk factor for CDI (odds ratio, 68.5; 95% confidence interval, 11.4 to 416.2). MLST on 22 unit patient toxin-positive stool specimens revealed 15 distinct strain types. Further analysis identified at least 1 potential cross-transmission event; some events may have been missed because of incomplete typing from other specimens. Despite aggressive infection control interventions, there was no decline in the number of CDI cases during the study period. These data suggest that prior CDC plays a major role in CDI rates in this high-risk patient population. It remains unclear if CDI was cross-transmitted in the unit.

Published
2014
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13. Alanine Scanning Mutagenesis Identifies an Asparagine–Arginine–Lysine Triad Essential to Assembly of the Shell of the Pdu Microcompartment

Author

Todd O. Yeates, Thomas A. Bobik, Sharmistha Sinha, Yea Won Sung, Dan E. McNamara, Michael R. Sawaya, and Shouqiang Cheng

Subjects
Models, Molecular, Salmonella typhimurium, Protein Conformation, DNA Mutational Analysis, Molecular Sequence Data, Mutant, Mutation, Missense, Mutagenesis (molecular biology technique), Biology, Crystallography, X-Ray, Article, Protein structure, Bacterial Proteins, Microscopy, Electron, Transmission, Structural Biology, Bacterial microcompartment, Amino Acid Sequence, Molecular Biology, Alanine, Dipeptides, Protein engineering, Alanine scanning, Carboxysome, Biochemistry, Mutagenesis, Site-Directed, Mutant Proteins, Asparagine, Protein Multimerization
Abstract

Bacterial microcompartments (MCPs) are the simplest organelles known. They function to enhance metabolic pathways by confining several related enzymes inside an all protein envelope called the shell. In this study, we investigated the factors that govern MCP assembly by performing scanning mutagenesis on the surface residues of PduA, a major shell protein of the MCP used for 1,2-propanediol degradation. Biochemical, genetic and structural analysis of 20 mutants allowed us to determine that PduA K26, N29 and R79 are crucial residues that stabilize the shell of the 1,2-propanediol MCP. In addition, we identify two PduA mutants (K37A and K55A) that impair MCP function most likely by altering the permeability of its protein shell. These are the first studies to examine the phenotypic effects of shell protein structural mutations in a microcompartment system. The findings reported here may be applicable to engineering protein containers with improved stability for biotechnology applications.

Published
2014

14. Structure of Dihydromethanopterin Reductase, a Cubic Protein Cage for Redox Transfer

Author

Julien Jorda, Duilio Cascio, Thomas A. Bobik, Tzu-Chi Wang, Dan E. McNamara, Cheene Bustos, Madeline E. Rasche, and Todd O. Yeates

Subjects
Burkholderia, Flavin Mononucleotide, Stereochemistry, Sequence Homology, Flavoprotein, Flavin mononucleotide, Flavin group, Crystallography, X-Ray, Biochemistry, Electron Transport, Electron transfer, chemistry.chemical_compound, Oxidoreductase, Catalytic Domain, Pterin, Molecular Biology, chemistry.chemical_classification, biology, Tetrahydromethanopterin, Active site, Cell Biology, Pterins, Molecular Docking Simulation, chemistry, Protein Structure and Folding, biology.protein, Oxidoreductases, Oxidation-Reduction
Abstract

Dihydromethanopterin reductase (Dmr) is a redox enzyme that plays a key role in generating tetrahydromethanopterin (H4MPT) for use in one-carbon metabolism by archaea and some bacteria. DmrB is a bacterial enzyme understood to reduce dihydromethanopterin (H2MPT) to H4MPT using flavins as the source of reducing equivalents, but the mechanistic details have not been elucidated previously. Here we report the crystal structure of DmrB from Burkholderia xenovorans at a resolution of 1.9 Å. Unexpectedly, the biological unit is a 24-mer composed of eight homotrimers located at the corners of a cubic cage-like structure. Within a homotrimer, each monomer-monomer interface exhibits an active site with two adjacently bound flavin mononucleotide (FMN) ligands, one deeply buried and tightly bound and one more peripheral, for a total of 48 ligands in the biological unit. Computational docking suggested that the peripheral site could bind either the observed FMN (the electron donor for the overall reaction) or the pterin, H2MPT (the electron acceptor for the overall reaction), in configurations ideal for electron transfer to and from the tightly bound FMN. On this basis, we propose that DmrB uses a ping-pong mechanism to transfer reducing equivalents from FMN to the pterin substrate. Sequence comparisons suggested that the catalytic mechanism is conserved among the bacterial homologs of DmrB and partially conserved in archaeal homologs, where an alternate electron donor is likely used. In addition to the mechanistic revelations, the structure of DmrB could help guide the development of anti-obesity drugs based on modification of the ecology of the human gut.

Published
2014

15. Solar modulation model with reentrant particles

Author

D. Grandi, Pavol Bobik, Karel Kudela, P. G. Rancoita, Massimo Gervasi, Matteo Boschini, Bobik, P, Kudela, K, Boschini, M, Grandi, D, Gervasi, M, and Rancoita, P

Subjects
Physics, Atmospheric Science, Work (thermodynamics), Mean free path, Aerospace Engineering, Astronomy and Astrophysics, Space (mathematics), Tracking (particle physics), Computational physics, Magnetic field, FIS/05 - ASTRONOMIA E ASTROFISICA, Geophysics, Classical mechanics, Reentrancy, Space and Planetary Science, Physics::Space Physics, Modulation (music), General Earth and Planetary Sciences, Cosmic rays, Heliosphere, Stochastic differential equation, FIS/04 - FISICA NUCLEARE E SUBNUCLEARE, Heliosphere
Abstract

We developed a one dimensional model of particle transport in the heliosphere. As opposite to widely used models, we apply a method where a quasi-particle is traced back in time. The model gives us the possibility to work on the possible existence of reentrant particles in the heliosphere that can be hardly solved by the traditional forward tracking method. Particles escape from the heliosphere and may reenter back. We estimate how these particles affect the modulation process in the heliosphere. Presented here are the results for different values of particles mean free path in the interstellar space and for different interstellar magnetic field values.

Published
2008

16. A High Salt Diet Accelerates Atherosclerosis By Modulating Hematopoiesis

Author

Annas Al-Sharea, Man K.S. Lee, Michael J Kraakman, Paul A. Baldock, P. Frings-Meuthen, John A. Hamilton, Prabhakara R Nagareddy, Gerard Pernes, Dragana Dragoljevic, Andrew J. Murphy, S. Naik, Seth L. Masters, Michelle C Flynn, Louise E. Purton, and Alex Bobik

Subjects
medicine.medical_specialty, Haematopoiesis, Endocrinology, Chemistry, Internal medicine, medicine, Cardiology and Cardiovascular Medicine, Salt diet
Published
2019

17. Heterogeneous catalysis on the phage surface: Display of active human enteropeptidase

Author

Natalia A. Ponomarenko, Alexander G. Gabibov, Yana V. Kim, Dmitry A. Dolgikh, Mikhail P. Kirpichnikov, T. V. Bobik, and Marine E. Gasparian

Subjects
Enteropeptidase, Phage display, Trypsinogen, Recombinant Fusion Proteins, Proteolysis, Phagemid, Genetic Vectors, Naphthalenes, Biology, Biochemistry, Catalysis, Substrate Specificity, chemistry.chemical_compound, Recognition sequence, Catalytic Domain, medicine, Humans, Bacteriophages, Cloning, Molecular, medicine.diagnostic_test, General Medicine, biology.organism_classification, Fusion protein, Kinetics, chemistry, Filamentous bacteriophage, Mutation, Cell Surface Display Techniques
Abstract

Enteropeptidase (EC 3.4.21.9) plays a key role in mammalian digestion as the enzyme that physiologically activates trypsinogen by highly specific cleavage of the trypsinogen activation peptide following the recognition sequence D4K. The high specificity of enteropeptidase makes it a powerful tool in modern biotechnology. Here we describe the application of phage display technology to express active human enteropeptidase catalytic subunits (L-HEP) on M13 filamentous bacteriophage. The L-HEP/C122S gene was cloned in the g3p-based phagemid vector pHEN2m upstream of the sequence encoding the phage g3p protein and downstream of the signal peptide-encoding sequence. Heterogeneous catalysis of the synthetic peptide substrate (GDDDDK-β-naphthylamide) cleavage by phage-bound L-HEP was shown to have kinetic parameters similar to those of soluble enzyme, with the respective Km values of 19 μM and 20 μM and kcat of 115 and 92 s(-1). Fusion proteins containing a D4K cleavage site were cleaved with phage-bound L-HEP/C122S as well as by soluble L-HEP/C122S, and proteolysis was inhibited by soybean trypsin inhibitor. Rapid large-scale phage production, one-step purification of phage-bound L-HEP, and easy removal of enzyme activity from reaction samples by PEG precipitation make our approach suitable for the efficient removal of various tag sequences fused to the target proteins. The functional phage display technology developed in this study can be instrumental in constructing libraries of mutants to analyze the effect of structural changes on the activity and specificity of the enzyme or generate its desired variants for biotechnological applications.

Published
2013

21. Protective Role of Natural IgM-Producing B1a Cells in Atherosclerosis

Author

Alex Bobik, Tin Kyaw, Ban-Hock Toh, and Peter G. Tipping

Subjects
Regulatory B cells, medicine.medical_treatment, Proinflammatory cytokine, Immune system, Animals, Humans, Medicine, B-Lymphocytes, biology, business.industry, Arteries, Atherosclerosis, Interleukin-10, Lipoproteins, LDL, Disease Models, Animal, Interleukin 10, Cytokine, Immunoglobulin M, Apoptosis, Immunology, biology.protein, Cytokines, Cardiology and Cardiovascular Medicine, business, Lipoprotein
Abstract

Atherosclerosis initiated by hyperlipidemia is modulated by immune cells in its development, progression, and rupture that results in thrombotic arterial occlusion leading to strokes and myocardial infarction. B cells initially thought to be atheroprotective provide opposing roles by their different subsets. Unlike B2 cells that are atherogenic, serosal B1a cells are atheroprotective by producing natural IgM antibodies that clear modified low-density lipoprotein and apoptotic and necrotic debris. In addition to natural IgM antibodies, B1a cells may act as regulatory B cells by producing the anti-inflammatory cytokine interleukin-10, which inhibits proinflammatory cytokines secreted by activated macrophages and T cells in atherosclerotic lesions. These findings suggest in vivo expansion of atheroprotective B1a cells as a potential therapeutic strategy to augment the benefits of lipid-lowering statin therapy.

Published
2012

22. Deletion of macrophage migration inhibitory factor protects the heart from severe ischemia–reperfusion injury: A predominant role of anti-inflammation

Author

Mark A. Febbraio, Yang Liu, Qi Xu, Anthony M. Dart, Xiao-Ming Gao, N. Jennings, Richard Bucala, Eric F Morand, David A. White, Brian G. Drew, Alex Bobik, Bronwyn A. Kingwell, Xiao-Jun Du, Yidan Su, Clinton R. Bruce, Helen Kiriazis, and Gunter Fingerle-Rowson

Subjects
Male, medicine.medical_treatment, Myocardial Infarction, Ischemia, Apoptosis, Inflammation, Pharmacology, Mice, Animals, Medicine, Myocytes, Cardiac, Macrophage Migration-Inhibitory Factors, Molecular Biology, Severe ischemia, Mice, Knockout, business.industry, Macrophages, Toll-Like Receptors, Hemodynamics, Anti inflammation, Metabolism, medicine.disease, Myocardial Contraction, Mice, Inbred C57BL, Cytokine, Gene Expression Regulation, Neutrophil Infiltration, Reperfusion Injury, Immunology, Macrophage migration inhibitory factor, Inflammation Mediators, medicine.symptom, Cardiology and Cardiovascular Medicine, business, Reperfusion injury, Signal Transduction
Abstract

Inflammation plays an important role in mediating and exacerbating myocardial ischemia-reperfusion (I/R) injury. Macrophage migration inhibitory factor (MIF), a pleiotropic cytokine, facilitates inflammation and modulates metabolism. However, the role of MIF in mediating local inflammation subsequent to ischemic myocardial injury has not been established. We hypothesized that genetic deletion of MIF protects the heart against severe I/R injury by suppressing inflammation and/or modulating energy metabolism. We showed in the mouse I/R model that duration of both ischemia and reperfusion is a determinant for the degree of regional inflammation and tissue damage. Following a prolonged cardiac I/R (60 min/24h) MIF KO mice had a significant reduction in both infarct size (26±3% vs. 45±4%, P0.05) and cardiomyocyte apoptosis (1.4±0.2% vs. 5.4±0.4%, P0.05) and preserved contractile function compared with WT. MIF KO mice with I/R had reduced expression of various inflammatory cytokines and mediators (P0.05), suppressed infiltration of neutrophils (-40%) and macrophages (-33%, both P0.05), and increased macrophage apoptosis (14.4±1.4% vs. 5.2±0.6%, P0.05). Expression of toll-like receptor-4 (TLR-4), phosphorylation of c-Jun N-terminal kinase (JNK), and nuclear fraction of NF-κB p65 were also significantly lower in MIF KO hearts with I/R. Further, MIF KO mice exhibited a lower glucose uptake but higher fatty acid oxidation rate than that in WT (both P0.05). In conclusion, MIF deficiency protected the heart from prolonged/severe I/R injury by suppressing inflammatory responses. We have identified a critical role of MIF in mediating severe I/R injury. Thus, MIF inhibitory therapy may be a novel strategy to protect the heart against severe I/R injury.

Published
2011

23. The protein shells of bacterial microcompartment organelles

Author

Michael C. Thompson, Thomas A. Bobik, and Todd O. Yeates

Subjects
Organelles, Protein Folding, Bacteria, Genomic data, Porins, Biological Transport, Biology, biology.organism_classification, Article, Enzymes, Structure and function, Metabolic pathway, Bacterial Proteins, Biochemistry, Structural Biology, Bacterial microcompartment, Organelle, Molecular Transport, Protein folding, Molecular Biology
Abstract

Details are emerging on the structure and function of a remarkable class of capsid-like protein assemblies that serve as simple metabolic organelles in many bacteria. These bacterial microcompartments consist of a few thousand shell proteins, which encapsulate two or more sequentially acting enzymes in order to enhance or sequester certain metabolic pathways, particularly those involving toxic or volatile intermediates. Genomic data indicate that bacterial microcompartment shell proteins are present in a wide range of bacterial species, where they encapsulate varied reactions. Crystal structures of numerous shell proteins from distinct types of microcompartments have provided keys for understanding how the shells are assembled and how they conduct molecular transport into and out of microcompartments. The structural data emphasize a high level of mechanistic sophistication in the protein shell, and point the way for further studies on this fascinating but poorly appreciated class of subcellular structures.

Published
2011

24. Investigation of a Clostridium difficile cluster by multilocus sequence typing in a bone marrow transplant unit

Author

Brent Bobik, Zi-Xuan Wang, Phyllis Flomenberg, Richard Sunday, Carol Hu, John L. Wagner, Mark Weiss, and Jackrapong Bruminhent

Subjects
Adult, Clostridioides difficile, Epidemiology, business.industry, Health Policy, Bone marrow transplant unit, Public Health, Environmental and Occupational Health, Middle Aged, Clostridium difficile, Disease cluster, Virology, Bacterial Typing Techniques, Disease Outbreaks, Microbiology, Feces, Infectious Diseases, Carrier State, Humans, Medicine, Multilocus sequence typing, business, Enterocolitis, Pseudomembranous, Bone Marrow Transplantation, Multilocus Sequence Typing
Published
2014

25. Kinetic and Functional Analysis of l-Threonine Kinase, the PduX Enzyme of Salmonella enterica

Author

Thomas A. Bobik, Herbert J. Fromm, and Chenguang Fan

Subjects
Threonine, Phosphomevalonate kinase, Homoserine kinase, Amino Acid Motifs, Molecular Sequence Data, Protein Serine-Threonine Kinases, Biology, MAP3K7, Biochemistry, MAP2K7, Adenosine Triphosphate, TANK-binding kinase 1, Enzyme Stability, Escherichia coli, Enzyme Inhibitors, Molecular Biology, Serine/threonine-specific protein kinase, Enzyme Catalysis and Regulation, Circular Dichroism, Salmonella enterica, Mevalonate kinase, Cell Biology, Galactokinase, Kinetics, Mutagenesis, Site-Directed, biology.protein, Mutant Proteins, Sequence Alignment
Abstract

The PduX enzyme of Salmonella enterica is an l-threonine kinase used for the de novo synthesis of coenzyme B(12) and the assimilation of cobyric acid. PduX with an N-terminal histidine tag (His(8)-PduX) was produced in Escherichiacoli and purified. The recombinant enzyme was soluble and active. Kinetic analysis indicated a steady-state Ordered Bi Bi complex mechanism in which ATP is the first substrate to bind. Based on a multiple sequence alignment of PduX homologues and other GHMP (galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) family members, 14 PduX variants having changes at 10 conserved serine/threonine and aspartate/glutamate sites were constructed by site-directed mutagenesis. Each variant was produced in E. coli and purified. Comparison of the circular dichroism spectra and kinetic properties of the PduX variants with those of the wild-type enzyme indicated that Glu-24 and Asp-135 are needed for proper folding, Ser-99 and Glu-132 are used for ATP binding, and Ser-253 and Ser-255 are critical to l-threonine binding whereas Ser-100 is essential to catalysis, but its precise role is uncertain. The studies reported here are the first to investigate the kinetic and catalytic mechanisms of l-threonine kinase from any organism.

Published
2009

26. A novel antioxidant 3,7-dihydroxy-isoflav-3-ene (DHIF) inhibits neointimal hyperplasia after vessel injury attenuating reactive oxygen species and nuclear factor-κB signaling

Author

Alan J. Husband, Jiu Li Huang, Catherine Walker, Paul J. Nestel, Giovanna Pomilio, Alex Bobik, Alex Agrotis, and Peter Kanellakis

Subjects
Neointima, Time Factors, Platelet-derived growth factor, Apoptosis, Pharmacology, Biology, medicine.disease_cause, Antioxidants, Muscle, Smooth, Vascular, Catheterization, chemistry.chemical_compound, Restenosis, Superoxides, medicine, Animals, Benzopyrans, Chemokine CCL2, Cell Proliferation, Platelet-Derived Growth Factor, chemistry.chemical_classification, Neointimal hyperplasia, Reactive oxygen species, Hyperplasia, Cell growth, Transcription Factor RelA, Balloon catheter, Anatomy, medicine.disease, Disease Models, Animal, Oxidative Stress, Carotid Arteries, chemistry, Cyclooxygenase 2, Cyclooxygenase 1, Rabbits, Carotid Artery Injuries, Reactive Oxygen Species, Tunica Intima, Cardiology and Cardiovascular Medicine, Oxidative stress, Signal Transduction
Abstract

Reactive oxygen species (ROS) contribute to neointimal smooth muscle proliferation by yet to be defined mechanisms. We examined the effects of a novel isoflavone 3,7-dihydroxy-isoflav-3-ene (DHIF) on development of neointimal lesions in relation to ROS elevations and cell signaling in injured arteries. Carotid arteries of rabbits treated with vehicle or DHIF were injured with a balloon catheter and effects on proliferation, apoptosis, vessel structure, ROS, NF-kappaB activation, cyclooxygenase and gene expression examined. Seven days after injury proliferating neointimal cells were reduced by 35% (P

Published
2009

27. Activation of Plant Plasma Membrane H+-ATPase by 14-3-3 Proteins Is Negatively Controlled by Two Phosphorylation Sites within the H+-ATPase C-terminal Region

Author

Dominik Piotrowiak, Krzysztof Bobik, Etienne Waelkens, Geoffrey Duby, Rita Derua, Marc Boutry, and Wojciech Pawel Poreba

Subjects
ATPase, Mutant, Saccharomyces cerevisiae, Gene Expression, Plasma protein binding, Biochemistry, Mass Spectrometry, Enzyme activator, Tobacco, Phosphorylation, Molecular Biology, Plant Proteins, chemistry.chemical_classification, biology, Mutagenesis, Cell Biology, biology.organism_classification, Molecular biology, Recombinant Proteins, Enzyme Activation, Proton-Translocating ATPases, Enzyme, 14-3-3 Proteins, Amino Acid Substitution, chemistry, biology.protein
Abstract

The proton pump ATPase (H(+)-ATPase) of the plant plasma membrane is regulated by an autoinhibitory C-terminal domain, which can be displaced by phosphorylation of the penultimate Thr residue and the subsequent binding of 14-3-3 proteins. We performed a mass spectrometric analysis of PMA2 (plasma membrane H(+)-ATPase isoform 2) isolated from Nicotiana tabacum suspension cells and identified two new phosphorylated residues in the enzyme 14-3-3 protein binding site: Thr(931) and Ser(938). When PMA2 was expressed in Saccharomyces cerevisiae, mutagenesis of each of these two residues into Asp prevented growth of a yeast strain devoid of its own H(+)-ATPases. When the Asp mutations were individually introduced in a constitutively activated mutant of PMA2 (E14D), they still allowed yeast growth but at a reduced rate. Purification of His-tagged PMA2 showed that the T931D or S938D mutation prevented 14-3-3 protein binding, although the penultimate Thr(955) was still phosphorylated, indicating that Thr(955) phosphorylation is not sufficient for full enzyme activation. Expression of PMA2 in an N. tabacum cell line also showed an absence of 14-3-3 protein binding resulting from the T931D or S938D mutation. Together, the data show that activation of H(+)-ATPase by the binding of 14-3-3 proteins is negatively controlled by phosphorylation of two residues in the H(+)-ATPase 14-3-3 protein binding site. The data also show that phosphorylation of the penultimate Thr and 14-3-3 binding each contribute in part to H(+)-ATPase activation.

Published
2009

28. On transmissivity of low energy cosmic rays in disturbed magnetosphere

Author

Karel Kudela, Pavol Bobik, and Radoslav Bučík

Subjects
Physics, Atmospheric Science, Ionospheric dynamo region, Neutron monitor, Geomagnetic secular variation, Astrophysics::High Energy Astrophysical Phenomena, Aerospace Engineering, Magnetosphere, Astronomy, Astronomy and Astrophysics, Cosmic ray, Astrophysics, Physics::Geophysics, Geophysics, Earth's magnetic field, Space and Planetary Science, Physics::Space Physics, General Earth and Planetary Sciences, Neutron, Ring current
Abstract

Access of low energy cosmic rays to any position on the Earth depends on the state of the magnetosphere. Anisotropy of cosmic rays, deduced from the neutron monitor network, must assume the variable transmissivity of the magnetosphere especially during the geomagnetic disturbances. We illustrate that computations based on different available models of geomagnetic field during selected strong geomagnetic disturbances in 2003 and 2004 imply different profiles of cut-off rigidities in time, different transmissivity functions and different asymptotic directions. Using of cosmic ray records by neutron monitors at middle and low latitudes during geomagnetically active periods, in addition to cosmic ray anisotropy in interplanetary space deduced from high and low energy cosmic ray ground based measurements, may be used for checking validity of geomagnetic field models.

Published
2008

29. Cosmic ray oriented performance studies for the JEM-EUSO first level trigger

Author

Abdellaoui, G., primary, Abe, S., additional, Acheli, A., additional, Adams, J.H., additional, Ahmad, S., additional, Ahriche, A., additional, Albert, J.-N., additional, Allard, D., additional, Alonso, G., additional, Anchordoqui, L., additional, Andreev, V., additional, Anzalone, A., additional, Aouimeur, W., additional, Arai, Y., additional, Arsene, N., additional, Asano, K., additional, Attallah, R., additional, Attoui, H., additional, Ave Pernas, M., additional, Bacholle, S., additional, Bakiri, M., additional, Baragatti, P., additional, Barrillon, P., additional, Bartocci, S., additional, Batsch, T., additional, Bayer, J., additional, Bechini, R., additional, Belenguer, T., additional, Bellotti, R., additional, Belov, A., additional, Belov, K., additional, Benadda, B., additional, Benmessai, K., additional, Berlind, A.A., additional, Bertaina, M., additional, Biermann, P.L., additional, Biktemerova, S., additional, Bisconti, F., additional, Blanc, N., additional, Błȩcki, J., additional, Blin-Bondil, S., additional, Bobik, P., additional, Bogomilov, M., additional, Bonamente, M., additional, Boudaoud, R., additional, Bozzo, E., additional, Briggs, M.S., additional, Bruno, A., additional, Caballero, K.S., additional, Cafagna, F., additional, Campana, D., additional, Capdevielle, J.-N., additional, Capel, F., additional, Caramete, A., additional, Caramete, L., additional, Carlson, P., additional, Caruso, R., additional, Casolino, M., additional, Cassardo, C., additional, Castellina, A., additional, Castellini, G., additional, Catalano, C., additional, Catalano, O., additional, Cellino, A., additional, Chikawa, M., additional, Chiritoi, G., additional, Christl, M.J., additional, Connaughton, V., additional, Conti, L., additional, Contino, G., additional, Cordero, G., additional, Cotto, G., additional, Crawford, H.J., additional, Cremonini, R., additional, Csorna, S., additional, Dagoret-Campagne, S., additional, De Donato, C., additional, de la Taille, C., additional, De Santis, C., additional, del Peral, L., additional, Di Martino, M., additional, Djemil, T., additional, Djenas, S.A., additional, Dulucq, F., additional, Dupieux, M., additional, Dutan, I., additional, Ebersoldt, A., additional, Ebisuzaki, T., additional, Engel, R., additional, Eser, J., additional, Fang, K., additional, Fenu, F., additional, Fernández-González, S., additional, Fernández-Soriano, J., additional, Ferrarese, S., additional, Finco, D., additional, Flamini, M., additional, Fornaro, C., additional, Forza, R., additional, Fouka, M., additional, Franceschi, A., additional, Franchini, S., additional, Fuglesang, C., additional, Fujimoto, J., additional, Fukushima, M., additional, Galeotti, P., additional, García-Ortega, E., additional, Garipov, G., additional, Gascón, E., additional, Geary, J., additional, Gelmini, G., additional, Genci, J., additional, Giraudo, G., additional, Gonchar, M., additional, González Alvarado, C., additional, Gorodetzky, P., additional, Guardone, N., additional, Guarino, F., additional, Guehaz, R., additional, Guzmán, A., additional, Hachisu, Y., additional, Haiduc, M., additional, Harlov, B., additional, Haungs, A., additional, Hernández Carretero, J., additional, Hidber, W., additional, Higashide, K., additional, Ikeda, D., additional, Ikeda, H., additional, Inoue, N., additional, Inoue, S., additional, Insolia, A., additional, Isgrò, F., additional, Itow, Y., additional, Jammer, T., additional, Joven, E., additional, Judd, E.G., additional, Jung, A., additional, Jochum, J., additional, Kajino, F., additional, Kajino, T., additional, Kalli, S., additional, Kaneko, I., additional, Kang, D., additional, Kanouni, F., additional, Karadzhov, Y., additional, Karczmarczyk, J., additional, Karus, M., additional, Katahira, K., additional, Kawai, K., additional, Kawasaki, Y., additional, Kedadra, A., additional, Khales, H., additional, Khrenov, B.A., additional, Kim, Jeong-Sook, additional, Kim, Soon-Wook, additional, Kim, Sug-Whan, additional, Kleifges, M., additional, Klimov, P.A., additional, Kolev, D., additional, Kreykenbohm, I., additional, Kudela, K., additional, Kurihara, Y., additional, Kusenko, A., additional, Kuznetsov, E., additional, Lacombe, M., additional, Lachaud, C., additional, Lahmar, H., additional, Lakhdari, F., additional, Larsson, O., additional, Lee, J., additional, Licandro, J., additional, Lim, H., additional, López Campano, L., additional, Maccarone, M.C., additional, Mackovjak, S., additional, Mahdi, M., additional, Manfrin, M., additional, Maravilla, D., additional, Marcelli, L., additional, Marcos, J.L., additional, Marini, A., additional, Martens, K., additional, Martín, Y., additional, Martinez, O., additional, Masciantonio, G., additional, Mase, K., additional, Matev, R., additional, Matthews, J.N., additional, Mebarki, N., additional, Medina-Tanco, G., additional, Mehrad, L., additional, Mendoza, M.A., additional, Merino, A., additional, Mernik, T., additional, Meseguer, J., additional, Messaoud, S., additional, Micu, O., additional, Mignone, M., additional, Mimouni, J., additional, Miyamoto, H., additional, Miyazaki, Y., additional, Mizumoto, Y., additional, Modestino, G., additional, Monaco, A., additional, Monnier-Ragaigne, D., additional, Morales de los Ríos, J.A., additional, Moretto, C., additional, Morozenko, V.S., additional, Mot, B., additional, Murakami, T., additional, Nadji, B., additional, Nagano, M., additional, Nagata, M., additional, Nagataki, S., additional, Nakamura, T., additional, Napolitano, T., additional, Naumov, D., additional, Nava, R., additional, Neronov, A., additional, Nomoto, K., additional, Nonaka, T., additional, Ogawa, T., additional, Ogio, S., additional, Ohmori, H., additional, Olinto, A.V., additional, Orleański, P., additional, Osteria, G., additional, Painter, W., additional, Panasyuk, M.I., additional, Panico, B., additional, Parizot, E., additional, Park, I.H., additional, Park, H.W., additional, Pastircak, B., additional, Patzak, T., additional, Paul, T., additional, Pennypacker, C., additional, Pérez-Grande, I., additional, Perfetto, F., additional, Peter, T., additional, Picozza, P., additional, Pierog, T., additional, Pindado, S., additional, Piotrowski, L.W., additional, Piraino, S., additional, Placidi, L., additional, Plebaniak, Z., additional, Pliego, S., additional, Pollini, A., additional, Popescu, E.M., additional, Prat, P., additional, Prévôt, G., additional, Prieto, H., additional, Putis, M., additional, Rabanal, J., additional, Radu, A.A., additional, Rahmani, M., additional, Reardon, P., additional, Reyes, M., additional, Rezazadeh, M., additional, Ricci, M., additional, Rodríguez Frías, M.D., additional, Ronga, F., additional, Roth, M., additional, Rothkaehl, H., additional, Roudil, G., additional, Rusinov, I., additional, Rybczyński, M., additional, Sabau, M.D., additional, Sáez Cano, G., additional, Sagawa, H., additional, Sahnoune, Z., additional, Saito, A., additional, Sakaki, N., additional, Sakata, M., additional, Salazar, H., additional, Sanchez, J.C., additional, Sánchez, J.L., additional, Santangelo, A., additional, Santiago Crúz, L., additional, Sanz-Andrés, A., additional, Sanz Palomino, M., additional, Saprykin, O., additional, Sarazin, F., additional, Sato, H., additional, Sato, M., additional, Schanz, T., additional, Schieler, H., additional, Scotti, V., additional, Segreto, A., additional, Selmane, S., additional, Semikoz, D., additional, Serra, M., additional, Sharakin, S., additional, Shibata, T., additional, Shimizu, H.M., additional, Shinozaki, K., additional, Shirahama, T., additional, Siemieniec-Oziȩbło, G., additional, Sledd, J., additional, Słomińska, K., additional, Sobey, A., additional, Stan, I., additional, Sugiyama, T., additional, Supanitsky, D., additional, Suzuki, M., additional, Szabelska, B., additional, Szabelski, J., additional, Tahi, H., additional, Tajima, F., additional, Tajima, N., additional, Tajima, T., additional, Takahashi, Y., additional, Takami, H., additional, Takeda, M., additional, Takizawa, Y., additional, Talai, M.C., additional, Tenzer, C., additional, Tibolla, O., additional, Tkachev, L., additional, Tokuno, H., additional, Tomida, T., additional, Tone, N., additional, Toscano, S., additional, Traïche, M., additional, Tsenov, R., additional, Tsunesada, Y., additional, Tsuno, K., additional, Tymieniecka, T., additional, Uchihori, Y., additional, Unger, M., additional, Vaduvescu, O., additional, Valdés-Galicia, J.F., additional, Vallania, P., additional, Vankova, G., additional, Vigorito, C., additional, Villaseñor, L., additional, Vlcek, B., additional, von Ballmoos, P., additional, Vrabel, M., additional, Wada, S., additional, Watanabe, J., additional, Watanabe, S., additional, Watts, J., additional, Weber, M., additional, Weigand Muñoz, R., additional, Weindl, A., additional, Weiler, T.J., additional, Wibig, T., additional, Wiencke, L., additional, Wille, M., additional, Wilms, J., additional, Włodarczyk, Z., additional, Yamamoto, T., additional, Yamamoto, Y., additional, Yang, J., additional, Yano, H., additional, Yashin, I.V., additional, Yonetoku, D., additional, Yoshida, S., additional, Young, R., additional, Zgura, I.S., additional, Zotov, M.Yu., additional, and Zuccaro Marchi, A., additional

Published
2017
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30. Potassium channel subunit Kv3.2 and the water channel aquaporin-4 are selectively localized to cerebellar pinceau

Author

Marketta Bobik, Mark H. Ellisman, Maryann E. Martone, and Bernardo Rudy

Subjects
Male, Cerebellum, Models, Neurological, Purkinje cell, Fluorescent Antibody Technique, Aquaporin, Biology, Aquaporins, Inhibitory postsynaptic potential, Rats, Sprague-Dawley, Purkinje Cells, Imaging, Three-Dimensional, Basket cell, medicine, Animals, Axon, Microscopy, Immunoelectron, Molecular Biology, Aquaporin 4, General Neuroscience, Potassium channel, Rats, medicine.anatomical_structure, Shaw Potassium Channels, nervous system, Potassium Channels, Voltage-Gated, Cerebellar cortex, Biophysics, Neurology (clinical), Neuroscience, Developmental Biology
Abstract

The pinceau is a cerebellar structure formed by descending GABA-ergic basket cell axonal terminals converging on the initial axonal segment of Purkinje cell. Although basket cells exert a powerful inhibitory influence on the output of the cerebellar cortex, the function and mode of action of the pinceau are not understood because the majority of basket cell axons fail to make identifiable synaptic contacts with the Purkinje cell axon. Several proteins were previously reported to cluster specifically in this area, including a number of voltage-activated potassium channel subunits. In this study, we used immunohistochemistry, electron microscopy, and electron tomography to examine the ultrastructural localization of a novel voltage-gated potassium channel subunit, Kv3.2, in the pinceau. We found strong, selective localization of Kv3.2 to basket cell axons. Additionally, because potassium buffering is often conducted through water channels, we studied the extent of a brain-specific water channel, aquaporin-4 (AQP4), using confocal and electron microscopy. As expected, we found AQP4 was heavily localized to astrocytic processes of the pinceau. The abundance of potassium channels and AQP4 in this area suggests rapid ionic dynamics in the pinceau, and the unusual, highly specialized morphology of this region implies that the structural features may combine with the molecular composition to regulate the microenvironment of the initial segment of the Purkinje cell axon.

Published
2004

31. Proliferation of Neointimal Smooth Muscle Cells after Arterial Injury

Author

Alex Bobik, Giovanna Di Vitto, Garry L. Jennings, Ross D. Hannan, Gina Kostolias, Chen Wei, Peter Kanellakis, and Alex Agrotis

Subjects
Neointima, medicine.medical_specialty, Fibroblast growth factor receptor 2, Growth factor, medicine.medical_treatment, Balloon catheter, Cell Biology, Biology, Fibroblast growth factor receptor 3, Fibroblast growth factor, Biochemistry, Cell biology, Endocrinology, Fibroblast growth factor receptor, Internal medicine, medicine, Extracellular, Molecular Biology
Abstract

The growth factor signaling mechanisms responsible for neointimal smooth muscle cell (SMC) proliferation and accumulation, a characteristic feature of many vascular pathologies that can lead to restenosis after angioplasty, remain to be identified. Here, we examined the contribution of fibroblast growth factor receptors (FGFRs) 2 and 3 as well as novel fibroblast growth factors (FGFs) to such proliferation. Balloon catheter injury to the rat carotid artery stimulated the expression of two distinctly spliced FGFR-2 isoforms, differing only by the presence or absence of the acidic box, and two distinctly spliced FGFR-3 isoforms containing the acidic box and differing only by the presence of either the IIIb or IIIc exon. Post-injury arterial administration of recombinant adenoviruses expressing dominant negative mutant forms of these FGFRs were used to assess the roles of the endogenous FGFR isoforms in neointimal SMC proliferation. Dominant negative FGFR-2 containing the acidic box inhibited such proliferation by 40%, whereas the dominant negative FGFR-3 forms had little effect. Expression of FGF-9, known to be capable of binding to all four neointimal FGFR-2/-3 isoforms, was abundant within the neointima. FGF-9 markedly stimulated both the proliferation of neointimal SMCs and the activation of extracellular signal-related kinases 1/2, effects which were abrogated by the administration of antisense FGF-9 oligonucleotides to injured arteries and the expression of the dominant negative FGFR-2 adenovirus in cultured neointimal SMCs. These studies demonstrate that, although multiple FGFRs are induced in neointimal SMCs following arterial injury, specific interactions between distinctly spliced FGFR-2 isoforms and FGF-9 contribute to the proliferation of these SMCs.

Published
2004

32. Relation of local platelet glycoprotein IIb/IIIa independent activation during coronary angioplasty in acute myocardial infarction to recovery of left ventricular function

Author

Andrew J. Taylor, Michael C. Berndt, Victor Kalff, Garry L. Jennings, Alexandra Michaelides, and Alex Bobik

Subjects
Male, medicine.medical_specialty, medicine.medical_treatment, Myocardial Infarction, Coronary Disease, Platelet Glycoprotein GPIIb-IIIa Complex, Ventricular Function, Left, Angioplasty, Internal medicine, medicine, Abciximab, Humans, Platelet, cardiovascular diseases, Myocardial infarction, Platelet activation, Angioplasty, Balloon, Coronary, Receptor, Coronary sinus, business.industry, Platelet Activation, medicine.disease, Blockade, Cardiology, Female, Cardiology and Cardiovascular Medicine, business, medicine.drug
Abstract

We assessed glycoprotein (GP) IIb/IIIa independent platelet activation in coronary sinus and peripheral blood from patients who underwent angioplasty for acute myocardial infarction and stable angina. Despite complete blockade of the activated GP IIb/IIIa receptor with abciximab in patients with acute myocardial infarction, unsuppressed local GP IIb/IIIa independent activation was associated with a lack of recovery of left ventricular function.

Published
2003

33. Identification of the Human and Bovine ATP:Cob(I)alamin Adenosyltransferase cDNAs Based on Complementation of a Bacterial Mutant

Author

Nicole A. Leal, Thomas A. Bobik, Peter E. Kima, and Sanghee D. Park

Subjects
DNA, Complementary, Time Factors, Recombinant Fusion Proteins, Blotting, Western, Molecular Sequence Data, Mutant, Biology, medicine.disease_cause, Models, Biological, Biochemistry, Catalysis, Adenosine Triphosphate, Mutase, Salmonella, Complementary DNA, Escherichia coli, medicine, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Amino Acid Metabolism, Inborn Errors, Molecular Biology, Gene, Cells, Cultured, Conserved Sequence, Gene Library, Oligonucleotide Array Sequence Analysis, Alkyl and Aryl Transferases, Sequence Homology, Amino Acid, Genetic Complementation Test, Structural gene, Methylmalonyl-CoA Mutase, nutritional and metabolic diseases, Sequence Analysis, DNA, Cell Biology, Fibroblasts, Molecular biology, Mitochondria, Complementation, Liver, Genes, Bacterial, Mutation, Cattle, Electrophoresis, Polyacrylamide Gel, CBLB, Cell Division
Abstract

In humans, deficiencies in coenzyme B12-dependent methylmalonyl-CoA mutase (MCM) lead to methylmalonyl aciduria, a rare disease that is often fatal in newborns. Such deficiencies can result from inborn errors in the MCM structural gene or from mutations that impair the assimilation of dietary cobalamins into coenzyme B12 (Ado-B12), the required cofactor for MCM. ATP:cob(I)alamin adenosyltransferase (ATR) catalyzes the terminal step in the conversion of cobalamins into Ado-B12. Substantial evidence indicates that inherited defects in this enzyme lead to methylmalonyl aciduria, but the corresponding ATR gene has not been identified. Here we report the identification of the bovine and human ATR cDNAs as well as the corresponding human gene. A bovine liver cDNA expression library was screened for clones that complemented an ATR-deficient bacterial strain for color formation on aldehyde indicator medium, and four positive clones were isolated. The DNA sequences of two clones were determined and found to be identical. Sequence similarity searching was then used to identify a homologous human cDNA (89% identity) and its corresponding gene that is located on chromosome XII. The bovine and human cDNAs were independently cloned and expressed in Escherichia coli. Enzyme assays showed that expression strains produced 87 and 98 nmol/min/mg ATR activity, respectively. These specific activities are in line with values reported previously for bacterial ATR enzymes. Subsequent studies showed that the human cDNA clone complemented an ATR-deficient bacterial mutant for Ado-B12-dependent growth on 1,2-propanediol. This demonstrated that the human ATR is active under physiological conditions albeit in a heterologous host. In addition, Western blots were used to show that ATR expression is altered in cell lines derived from cblB methylmalonyl aciduria patients compared with cell lines from normal individuals. We propose that inborn errors in the human ATR gene identified here result in methylmalonyl aciduria. The identification of genes involved in this disorder will allow improvements in the diagnosis and treatment of this serious disease.

Published
2003

34. Anti-DNA autoantibodies reveal toxicity to tumor cell lines

Author

N. A. Zelenova, Nikolai V. Gnuchev, T. V. Bobik, S. V. Khaidukov, A. V. Kozyr, S. V. Suchkov, Alexander G. Gabibov, Lidia P. Sashchenko, A. N. Ignatova, Alexander V. Kolesnikov, and Zemfira S. Alekberova

Subjects
Programmed cell death, Time Factors, Immunology, Cell, DNA Fragmentation, Biology, Immunoglobulin Fab Fragments, Tumor Cells, Cultured, medicine, Humans, Lupus Erythematosus, Systemic, Immunology and Allergy, Cytotoxic T cell, Cytotoxicity, Cell Death, Hydrolysis, Immune Sera, Autoantibody, DNA, Flow Cytometry, Caspase Inhibitors, Leukemia, Lymphocytic, Chronic, B-Cell, Molecular biology, medicine.anatomical_structure, Apoptosis, Cell culture, Antibodies, Antinuclear, Caspases, DNA fragmentation
Abstract

Cytotoxicity of anti-DNA autoantibodies from sera of SLE and CLL patients was assayed on permanent cell lines L929, HL-60, Raji, and K562. L929 cells appeared to be the most sensitive to antibody treatment. DNA-hydrolyzing properties of the same autoantibody preparations were analyzed in parallel. The data obtained outlined the correlation between cytotoxicity and DNA-hydrolyzing properties of these autoantibodies. It was shown that treatment of the cells with cytotoxic anti-DNA autoantibodies induced internucleosomal DNA fragmentation and Annexin V binding to the cell surface characteristic of apoptotic pathway of cell death. A time-dependent profile of antibody-mediated toxicity to L929 cells suggested recruitment of at least two distinct mechanisms of cell death. The first peak of cell death observed in 3 h of incubation was completely inhibited by preincubation of cells with caspase inhibitor YVAD-CHO, while the second increase in cell mortality (18-30 h) persisted. Possible mechanisms for anti-DNA autoantibody cytotoxicity are discussed.

Published
2002

35. Identification of the Human Methylmalonyl-CoA Racemase Gene Based on the Analysis of Prokaryotic Gene Arrangements

Author

Madeline E. Rasche and Thomas A. Bobik

Subjects
Genetics, Methylmalonyl-CoA racemase, Eukaryotic gene, Cell Biology, Biology, ENCODE, Biochemistry, Homology (biology), Mutase, Gene Arrangements, lipids (amino acids, peptides, and proteins), Human genome, Molecular Biology, Gene
Abstract

In this report, we identify the humandl-methylmalonyl-CoA racemase gene by analyzing prokaryotic gene arrangements and extrapolating the information obtained to human genes by homology searches. Sequence similarity searches were used to identify two groups of homologues that were frequently arranged with prokaryotic methylmalonyl-CoA mutase genes, and that were of unknown function. Both gene groups had homologues in the human genome. Because methylmalonyl-CoA mutases are involved in the metabolism of propionyl-CoA, we inferred that conserved neighbors of methylmalonyl-CoA mutase genes and their human homologues were also involved in this process. Subsequent biochemical studies confirmed this inference by showing that the prokaryotic gene PH0272 and its human homologue both encode dl-methylmalonyl-CoA racemases. To our knowledge this is the first report in which the function of a eukaryotic gene was determined based on the analysis of prokaryotic gene arrangements. Importantly, such analyses are rapid and may be generally applicable for the identification of human genes that lack homologues of known function or that have been misidentified on the basis of sequence similarity searches.

Published
2001

36. Sensitivity of a neutron monitor to galactic cosmic rays

Author

G. A. Kovaltsov, H. Kananen, Karel Kudela, Ilya Usoskin, P. Bobik, and O. G. Gladysheva

Subjects
Physics, Atmospheric Science, Neutron monitor, PAMELA detector, Astrophysics::High Energy Astrophysical Phenomena, Aerospace Engineering, Astronomy and Astrophysics, Cosmic ray, Astrophysics::Cosmology and Extragalactic Astrophysics, Astrophysics, Yield function, law.invention, Interstellar medium, Geophysics, Rigidity (electromagnetism), Space and Planetary Science, law, General Earth and Planetary Sciences, Ultra-high-energy cosmic ray
Abstract

We studied the sensitivity of a neutron monitor to Galactic cosmic rays depending on energy of cosmic ray particles in the interstellar medium. This is important for studying of the interstellar spectrum of cosmic rays and details of solar modulation by means of the world neutron monitor network. We calculated the expected response of a standard sea-level neutron monitor vs. energy of cosmic ray particles. First, we studied modulation of a monoenergetic flux of cosmic rays. Then the specific atmospheric yield function of a neutron monitor was applied to the calculated flux of cosmic rays at the Earth's orbit. The obtained response function, being convoluted with the model interstellar spectrum of cosmic rays, gives a maximum of neutron monitor sensitivity at around several GV of rigidity of cosmic ray particles. We performed calculations for weak (φ = 350 MV) and medium (φ = 750 MV) modulation strength. A normalisation of neutron monitor count rate is suggested which can give an experimental measure of the overall solar modulation of cosmic rays.

Published
2001

37. Response to balloon injury is vascular bed specificA consequence of de novo vessel structure?

Author

Alex Bobik, Michael R. Ward, Garry L. Jennings, Debbie Ramsey, and Peter Kanellakis

Subjects
Male, Intimal hyperplasia, Swine, medicine.medical_treatment, Coronary Angiography, Balloon, Iliac Artery, Catheterization, Restenosis, Angioplasty, Animals, Medicine, Rupture, Neointimal hyperplasia, Wound Healing, business.industry, Vascular disease, Angiography, Anatomy, medicine.disease, Coronary Vessels, Coronary arteries, medicine.anatomical_structure, Swine, Miniature, Wounds and Injuries, Tunica Intima, Cardiology and Cardiovascular Medicine, business, Compliance, Artery
Abstract

Relative contributions of remodelling and neointimal hyperplasia to restenosis after coronary angioplasty have been inferred from studies using iliofemoral arteries, despite differences in structure:function and smooth muscle cell lineage. We compared the response to balloon overstretch injury of coronary arteries (C, n 16) and similar sized branches of the iliac arteries (I, n18) using preinjury vessel diameter (P), inflated balloon size in vivo (B) and the manufacturer predicted inflated size (M) to examine arterial compliance, as well as resulting injury and morphology in perfusion fixed vessels. Despite similar degrees of oversizing (M:P) in the coronary and iliac arteries (C, 1.4490.04; I, 1.519 0.02), the compliance to overstretch (B P:MP) was significantly greater in the coronary than the iliac arteries (C, 0.719 0.05; I, 0.519 0.03) (PB 0.05) and was associated with a higher injury score (C, 1.6490.31; I, 0.3990.18 PB0.05)—only 5:18 iliac vessels had rupture of the IEL compared with 13:16 in the coronary bed. In a subgroup of animals whose vessels (C:n 7; I:n 8) were perfusion fixed 28 days after injury, coronary arteries had greater intimal area (C:1.0390.42; I:0.109 0.03 mm 2 , PB 0.05) but larger luminal area (C:1.619 0.71; I:0.7690.51, PB0.05) due to greater area within EEL (C:3.3890.49;I:1.499 0.54, PB 0.05) or less inward remodelling. The injuries resulting from similar strategies of balloon overstretch in the coronary and the iliac arteries are different and affect healing responses-iliac arteries remodel more while coronary arteries develop more intimal hyperplasia. These results indicate that caution is warranted when extrapolating results from the iliac to the coronary artery when investigating restenosis after angioplasty. © 2000 Elsevier Science Ireland Ltd. All rights reserved.

Published
2000

38. Fatty acid composition of the milk lipids of women in Nepal

Author

Robert H. Glew, B.L. Schmeits, Dorothy J. VanderJagt, Yung-Sheng Huang, Shree Krishna Bhatt, Julia A. Cook, Margaret A. Magnussen, and Emil G. Bobik

Subjects
chemistry.chemical_classification, education.field_of_study, Nutrition and Dietetics, Linolenic acid, Endocrinology, Diabetes and Metabolism, Linoleic acid, Population, Phospholipid, food and beverages, Fatty acid, Biology, chemistry.chemical_compound, Endocrinology, chemistry, Biochemistry, Docosahexaenoic acid, lipids (amino acids, peptides, and proteins), Arachidonic acid, Food science, education, Polyunsaturated fatty acid
Abstract

We analyzed the fatty acid composition of the triacylglycerol and phospholipid fractions of human milk samples obtained 2–4 weeks postpartum from 48 women living in rural Nepal. The most noteworthy aspects of the fatty acid composition of the triacylglycerol fraction were the proportions of the two essential fatty acids, linoleic acid (C18:2n-6) and α-linolenic acid (C18:3n-3). The proportion of linoleic acid was very low (7.91%), while that of α-linolenic acid was relatively high (1.93%). Together, the n-3 and n-6 polyunsaturated fatty acids accounted for 12.4% of the total fatty acids in the triacylglycerol fraction, and de novo fatty acids (C10:0–C14:0) accounted for 25.0% of the total, arachidonic acid 0.35%, and docosahexaenoic acid (DHA) 0.21% of the total. In the phospholipid fraction, the two essential fatty acids accounted for 6.38% of the fatty acid total. In the phospholipid fraction, 23.0% of the fatty acids were contributed by de novo fatty acids, 0.57% by arachidonic acid and 0.78% by DHA. The mean body mass index (BMI, kg/m 2 ) of the women in the Nepal study was in the middle range of other groups we have studied in Nigeria, yet the value of linoleic acid in the triacylglycerol fraction of their milk was lower than the value we found in the milk lipids of the Nigerian women. This leads us to speculate the low proportion of linoleic acid in the milk fat of the Nepalese women is due more to the diet of the population rather than the overall nutritional status of the mothers, as reflected in their BMI values.

Published
1999

39. Blocking IL-6 trans-Signaling Prevents High-Fat Diet-Induced Adipose Tissue Macrophage Recruitment but Does Not Improve Insulin Resistance

Author

Kraakman, Michael J., primary, Kammoun, Helene L., additional, Allen, Tamara L., additional, Deswaerte, Virginie, additional, Henstridge, Darren C., additional, Estevez, Emma, additional, Matthews, Vance B., additional, Neill, Bronwyn, additional, White, David A., additional, Murphy, Andrew J., additional, Peijs, Lone, additional, Yang, Christine, additional, Risis, Steve, additional, Bruce, Clinton R., additional, Du, Xiao-Jun, additional, Bobik, Alex, additional, Lee-Young, Robert S., additional, Kingwell, Bronwyn A., additional, Vasanthakumar, Ajithkumar, additional, Shi, Wei, additional, Kallies, Axel, additional, Lancaster, Graeme I., additional, Rose-John, Stefan, additional, and Febbraio, Mark A., additional

Published
2016
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40. Bordetella petrii recovered from chronic pansinusitis in an adult with cystic fibrosis

Author

Laura Biederman, Brent Bobik, Marc Rosen, and Amity L. Roberts

Subjects
MALDI-TOF, Pathology, medicine.medical_specialty, biology, business.industry, Antibiotic sensitivity, Case Report, Infectious and parasitic diseases, RC109-216, Chronic pansinusitis, biology.organism_classification, medicine.disease, Cystic fibrosis, Bordetella, Endoscopic sinus surgery, Infectious Diseases, Bordetella petrii, RNA Sequence, medicine, Pansinusitis, Adult cystic fibrosis, Sinusitis, business
Abstract

To date Bordetella petrii has infrequently been identified within the clinical setting likely due to the asaccharolytic nature of this organism. We present a case of B. petrii recovered on two separate events in a patient with adult cystic fibrosis experiencing chronic pansinusitis.

Published
2015
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41. A novel expression cassette delivers efficient production of exclusively tetrameric human butyrylcholinesterase with improved pharmacokinetics for protection against organophosphate poisoning

Author

Terekhov, Stanislav, primary, Smirnov, Ivan, additional, Bobik, Tatiana, additional, Shamborant, Olga, additional, Zenkova, Marina, additional, Chernolovskaya, Elena, additional, Gladkikh, Danil, additional, Murashev, Arkadii, additional, Dyachenko, Igor, additional, Palikov, Viktor, additional, Palikova, Yulia, additional, Knorre, Vera, additional, Belogurov, Alexey, additional, Ponomarenko, Natalie, additional, Blackburn, G. Michael, additional, Masson, Patrick, additional, and Gabibov, Alexander, additional

Published
2015
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42. Inhibitory effects of tranilast on expression of transforming growth factor-β isoforms and receptors in injured arteries

Author

Alex Bobik, Alex Agrotis, Rodney J. Dilley, Takayuki Sasahara, Garry L. Jennings, and Michael R. Ward

Subjects
Male, Integrins, Smooth muscle cell migration, Tranilast, medicine.medical_treatment, Arterial Occlusive Diseases, Pharmacology, Polymerase Chain Reaction, Muscle, Smooth, Vascular, Rats, Sprague-Dawley, Downregulation and upregulation, Cell Movement, Transforming Growth Factor beta, medicine, Animals, ortho-Aminobenzoates, RNA, Messenger, Receptor, Cells, Cultured, DNA Primers, Dose-Response Relationship, Drug, biology, business.industry, Growth factor, Balloon catheter, Anatomy, Rats, Carotid Arteries, biology.protein, Carotid Artery Injuries, Cardiology and Cardiovascular Medicine, business, Receptors, Transforming Growth Factor beta, Angioplasty, Balloon, Cell Division, Platelet Aggregation Inhibitors, Platelet-derived growth factor receptor, medicine.drug, Transforming growth factor
Abstract

Tranilast (N(3,4-dimethoxycinnamoyl)anthranilic acid), an agent which in cell culture inhibits transforming growth factor-beta (TGF-beta) secretion and antagonises the effects of TGF-beta and platelet-derived growth factor (PDGF) on cell migration and proliferation, has been reported to reduce the incidence of restenosis after angioplasty in angiographically validated human clinical trials. We investigated in a rat model of balloon angioplasty whether tranilast's effects in vivo could be attributed to inhibition of expression of TGF-beta and/or its receptor types. Using a standardised reverse transcriptase-polymerase chain reaction (RT-PCR) assay, we examined the effects of three doses of tranilast (25, 50 and 100 mg/kg) on the expression of two TGF-beta isoforms, the types I and II TGF-beta receptors and two putative TGF-beta responses, induction of integrins alpha(v) and beta3 mRNA, 2 h after oral administration and 26 h after vessel injury. Tranilast attenuated in a dose-dependent and reversible manner the injury-induced increases in mRNA levels encoding TGF-beta1, TGF-beta3, two type I TGF-beta receptors ALK-5 and ALK-2, and the type II receptor TbetaRII. At the highest dose mRNA levels encoding TGF-beta1 and TbetaRII were attenuated to levels approaching or below those observed in uninjured vessels. Messenger RNAs encoding TGF-beta3, ALK-5 and ALK-2 were all attenuated by between 70 and 74% (all P0.05). Tranilast also attenuated in a reversible manner the elevations in mRNA levels for integrins alpha(v) and beta3 observed after vessel injury, by 90 and 72%, respectively. We also investigated, in cultured smooth muscle cells derived from injured carotid arteries, the extent to which tranilast (300 mg/l) attenuated any increases in expression of type I and type II receptors stimulated by PDGF-BB and TGF-beta1, growth factors implicated in smooth muscle cell migration and proliferation in injured vessels. Increases in mRNA levels of the type I receptors ALK-5 and ALK-2 induced by PDGF-BB and TGF-beta1 were almost completely prevented by tranilast. Tranilast also prevented the PDGF-BB induced increases in TbetaRII but only partially inhibited the TGF-beta1 induced upregulation of TbetaRII. We conclude that tranilast can inhibit transcriptional mechanisms associated with the upregulation of TGF-beta and its receptor types in balloon catheter injured vessels. It is possible that these mechanisms contribute to its ability to reduce the frequency of restenosis after angioplasty.

Published
1998

43. Age-specific onset of β-amyloid in Beagle brains

Author

Marketta Bobik, Russell G. White, Yongjin Hou, James W. Geddes, Stephen A. Benjamin, and Michael J. Russell

Subjects
Aging, Pathology, medicine.medical_specialty, Hippocampal formation, Hippocampus, Beagle, Central nervous system disease, Silver stain, Dogs, medicine, Animals, Age of Onset, Brain Chemistry, Cerebral Cortex, Amyloid beta-Peptides, business.industry, General Neuroscience, Brain, medicine.disease, Immunohistochemistry, Staining, Cerebral Amyloid Angiopathy, Neurology (clinical), Geriatrics and Gerontology, Alzheimer's disease, Age of onset, business, Developmental Biology
Abstract

As part of an effort to characterize Alzheimer's disease-like neuropathy in the canine brain we have determined the age of onset of spontaneous beta-amyloid deposition in 103 laboratory-raised beagles. Tissue samples for each subject were obtained from hippocampal and cortical regions and examined for the incidence and density of beta-amyloid deposition after staining with modified Bielschowsky silver stain and immunohistochemistry. Amyloid deposition was characterized as diffuse plaque or cloud-like formation. The diffuse type of beta-amyloid plaque formation predominated in all brain regions examined. A threshold effect of plaque development was observed; no plaques were apparent in dogs before the age of 10 years, while 36% of dogs aged 11.1-12.9, 60% of dogs aged 13.0-15.0, and 73% of dogs aged 15.1-17.8 developed beta-amyloid deposits. Additionally, a significant increase in plaque density was observed with increasing age.

Published
1996

44. Vascular Smooth Muscle Cells Express Multiple Type I Receptors for TGF-β,Activin, and Bone Morphogenetic Proteins

Author

Alex Bobik, Melanie Samuel, Alex Agrotis, and Gina Prapas

Subjects
Receptor complex, DNA, Complementary, Vascular smooth muscle, Molecular Sequence Data, Receptor, Transforming Growth Factor-beta Type I, Biophysics, Gene Expression, Aorta, Thoracic, Protein Serine-Threonine Kinases, Biology, Bone morphogenetic protein, Polymerase Chain Reaction, Rats, Inbred WKY, Biochemistry, Bone morphogenetic protein 2, Muscle, Smooth, Vascular, Transforming Growth Factor beta, hemic and lymphatic diseases, Animals, Amino Acid Sequence, Growth Substances, Receptor, Molecular Biology, Cells, Cultured, DNA Primers, Base Sequence, RNA, Cell Biology, Molecular biology, Rats, Transmembrane domain, RNA splicing, Activin Receptors, Type I, Receptors, Transforming Growth Factor beta
Abstract

Vascular smooth muscle cells (VSMCs) are known to produce activins, bone morphogenetic proteins and transforming growth factor-betas (TGF-betas). To determine whether these TGF-beta superfamily members exert autocrine effects on VSMCs we examined whether specific type I receptors (ALKs) for such peptides were expressed by the cells. RNA from both quiescent or growth-factor-activated VSMCs was reverse transcribed then cDNAs encoding ALK-2, ALK-3, ALK-5, and ALK-6 were amplified and characterised using specific PCR primers. All four ALK mRNAs were abundantly expressed. The ALK-5 fragment harbored a deletion of 12 nucleotides, removing 4 extracellular amino acids (Gly-Pro-Ser-Val) adjacent to its transmembrane domain. This deletion, which may arise from anomalous splicing of heteronuclear RNA, is likely to influence formation of the ALK-5:type II receptor complex through conformational changes associated with removal of a putative hinge region containing proline. Our finding that multiple ALKs are expressed by VSMCs would account for the multiplicity of effects TGF-beta peptides exert on these cells.

Published
1996

45. Multiple Types of Ryanodine Receptor/Ca2+ Release Channels Are Expressed in Vascular Smooth Muscle

Author

Alex Bobik, Craig B. Neylon, A. Agrotis, Stephen M. Richards, and M.A. Larsen

Subjects
Cell type, DNA, Complementary, Vascular smooth muscle, Macromolecular Substances, Molecular Sequence Data, Restriction Mapping, Biophysics, Muscle Proteins, Aorta, Thoracic, Biology, Polymerase Chain Reaction, Rats, Inbred WKY, Biochemistry, Ryanodine receptor 2, Muscle, Smooth, Vascular, Restriction map, Complementary DNA, Animals, Molecular Biology, Cells, Cultured, DNA Primers, RYR1, Base Sequence, Ryanodine receptor, RNA, Ryanodine Receptor Calcium Release Channel, Cell Biology, musculoskeletal system, Molecular biology, Rats, cardiovascular system, Calcium Channels, tissues
Abstract

Functional studies on vascular smooth muscle suggest the presence of ryanodine receptors (RyRs) with differing properties. In an attempt to understand such differences we investigated, using reverse transcription-polymerase chain reaction (RT-PCR), the possibility that smooth muscle cells express multiple types of RyRs. RNA was extracted from rat aorta, superior and small mesenteric arterial vessels, purified aortic smooth muscle media, or cultured aortic smooth muscle cells for cDNA synthesis. The cDNAs encoding RyR1, RyR2, and RyR3 were amplified using PCR primers based on sequences close to the 3' coding region of the RyR genes and PCR products verified by restriction endonuclease analysis. All three members of the RyR gene family were found to be present in vascular smooth muscle. This finding of multiple types of RyRs expressed in the same cell type indicates a complex mechanism of RyR Ca2+ channel regulation involving the formation of homo- and/or heterotetrameric complexes.

Published
1995

46. Dihydropyridine Ca2+ channel antagonists inhibit the salvage pathway for DNA synthesis in human vascular smooth muscle cells

Author

Alex Bobik, Alex Agrotis, Peter J. Little, and John Saltis

Subjects
Dihydropyridines, Vascular smooth muscle, Immunoblotting, Nisoldipine, Pharmacology, Biology, Muscle, Smooth, Vascular, Diltiazem, chemistry.chemical_compound, Epidermal growth factor, medicine, Humans, Mammary Arteries, Nucleotide salvage, Cells, Cultured, Epidermal Growth Factor, Felodipine, DNA synthesis, Cell growth, Dihydropyridine, Genes, fos, DNA, Calcium Channel Blockers, Gene Expression Regulation, Verapamil, chemistry, Biochemistry, Thymidine, Cell Division, medicine.drug
Abstract

We examined the mechanisms by which Ca2+ channel antagonists inhibit the growth of smooth muscle cells by determining their effect on epidermal growth factor (EGF)-stimulated (i) induction of the early signalling gene, c-fos, (ii) incorporation of [3H]thymidine into cells as a measure of DNA synthesis, and (iii) increase in cell number. Verapamil, diltiazem, and the dihydropyridines felodipine, MDL 72892 A-15 (MDL) and nisoldipine had no effect on EGF-stimulated c-fos mRNA induction. Furthermore, only small inhibitory effects were observed on EGF-stimulated increases in cell number; felodipine, MDL, and nisoldipine at 0.3 microM inhibited EGF-stimulated cell proliferation by 9, 11, and 15%, respectively. In contrast, the dihydropyridine Ca2+ channel antagonists were found to be potent inhibitors of [3H]thymidine incorporation suggesting that they inhibit DNA synthesis. However, further examination revealed that the potent effects of dihydropyridine Ca2+ channel antagonists on [3H]thymidine incorporation were due not to an effect on incorporation of [3H]thymidine into DNA, but to a marked inhibitory effect on the cellular uptake of [3H]thymidine. Thus, we conclude that the small antiproliferative effects of the dihydropyridine antagonists are predominantly due to their ability to inhibit the activity of the salvage pathway for thymidylate synthesis in human vascular smooth muscle cells.

Published
1993

47. Obesity in Youth with Type 1 Diabetes in Germany, Austria, and the United States

Author

DuBose, Stephanie N., primary, Hermann, Julia M., additional, Tamborlane, William V., additional, Beck, Roy W., additional, Dost, Axel, additional, DiMeglio, Linda A., additional, Schwab, Karl Otfried, additional, Holl, Reinhard W., additional, Hofer, Sabine E., additional, Maahs, David M., additional, Willi, Steven, additional, Lipman, Terri, additional, Calvano, Tammy, additional, Kucheruk, Olena, additional, Minnock, Pantea, additional, Nguyen, Chau, additional, Klingensmith, Georgeanna, additional, Banion, Carolyn, additional, Barker, Jennifer, additional, Cain, Cindy, additional, Chase, Peter, additional, Hoops, Sandy, additional, Kelsy, Megan, additional, Maahs, David, additional, Mowry, Cathy, additional, Nadeau, Kristen, additional, Raymond, Jennifer, additional, Rewers, Marian, additional, Rewers, Arleta, additional, Slover, Robert, additional, Steck, Andrea, additional, Wadwa, Paul, additional, Walravens, Philippe, additional, Zeitler, Philip, additional, Haro, Heidi, additional, Manseau, Katherine, additional, Weinstock, Ruth, additional, Izquierdo, Roberto, additional, Sheikh, Umair, additional, Conboy, Patricia, additional, Bulger, Jane, additional, Bzdick, Suzan, additional, Goland, Robin, additional, Gandica, Rachelle, additional, Weiner, Lindsay, additional, Cook, Steve, additional, Greenberg, Ellen, additional, Kohm, Kevin, additional, Pollack, Sarah, additional, Lee, Joyce, additional, Gregg, Brigid, additional, Tan, Meng, additional, Burgh, Kimberly, additional, Eason, Ashley, additional, Garg, Satish, additional, Michels, Aaron, additional, Myers, Lisa, additional, DiMeglio, Linda, additional, Hannon, Tamara, additional, Orr, Donald, additional, Cruz, Christy, additional, Woerner, Stephanie, additional, Wolfsdorf, Joseph, additional, Quinn, Maryanne, additional, Tawa, Olivia, additional, Ahmann, Andrew, additional, Castle, Jessica, additional, Joarder, Farahnaz, additional, Bogan, Chris, additional, Cady, Nancy, additional, Cox, Jennifer, additional, Pitts, Amy, additional, Fitch, Rebecca, additional, White, Brad, additional, Wollam, Bethany, additional, Bode, Bruce, additional, Lindmark, Katie, additional, Hosey, RaShonda, additional, Bethin, Kathleen, additional, Quattrin, Teresa, additional, Ecker, Michelle, additional, Wood, Jamie, additional, Chao, Lily, additional, Cheung, Clement, additional, Fisher, Lynda, additional, Jeandron, Debra, additional, Kaufman, Francine, additional, Kim, Mimi, additional, Miyazaki, Brian, additional, Monzavi, Roshanak, additional, Patel, Payal, additional, Pitukcheewanont, Pisit, additional, Sandstrom, Anna, additional, Cohen, Marisa, additional, Ichihara, Brian, additional, Lipton, Megan, additional, Cemeroglu, Ayse, additional, Appiagyei-Dankah, Yaw, additional, Daniel, Maala, additional, Postellon, Daniel, additional, Racine, Michael, additional, Wood, Michael, additional, Kleis, Lora, additional, Hirsch, Irl, additional, DeSantis, Anthony, additional, Dugdale, D.C., additional, Failor, R. Alan, additional, Gilliam, Lisa, additional, Greenbaum, Carla, additional, Janci, Mary, additional, Odegard, Peggy, additional, Trence, Dace, additional, Wisse, Brent, additional, Batts, Emily, additional, Dove, Angela, additional, Hefty, Deborah, additional, Khakpour, Dori, additional, Klein, Jani, additional, Kuhns, Kristen, additional, McCulloch-Olson, Marli, additional, Peterson, Christina, additional, Ramey, Mary, additional, Marie, Marissa St., additional, Thomson, Pam, additional, Webber, Christine, additional, Liljenquist, David, additional, Sulik, Mark, additional, Vance, Carl, additional, Coughenour, Tiffany, additional, Brown, Chris, additional, Halford, Jean, additional, Prudent, Andrea, additional, Rigby, Shanda, additional, Robison, Brandon, additional, Starkman, Harold, additional, Berry, Tymara, additional, Cerame, Barbara, additional, Chin, Daisy, additional, Ebner-Lyon, Laurie, additional, Guevarra, Frances, additional, Sabanosh, Kristen, additional, Silverman, Lawrence, additional, Wagner, Christine, additional, Fox, Marie, additional, Buckingham, Bruce, additional, Shah, Avni, additional, Caswell, Kimberly, additional, Harris, Breanne, additional, Bergenstal, Richard, additional, Criego, Amy, additional, Damberg, Greg, additional, Matfin, Glenn, additional, Powers, Margaret, additional, Tridgell, David, additional, Burt, Cassie, additional, Olson, Beth, additional, Thomas, LeeAnn, additional, Mehta, Sanjeev, additional, Katz, Michelle, additional, Laffel, Lori, additional, Hathway, Joanne, additional, Phillips, Roxanne, additional, Cengiz, Eda, additional, Tamborlane, William, additional, Cappiello, Darryll, additional, Steffen, Amy, additional, Zgorski, Melinda, additional, Peters, Anne, additional, Ruelas, Valerie, additional, Benjamin, Robert, additional, Adkins, Deanna, additional, Cuffee, Juanita, additional, Spruill, Amber, additional, Aleppo-Kacmarek, Grazia, additional, Derby, Teresa, additional, Massaro, Elaine, additional, Webb, Kimberly, additional, Burt Solorzano, Christine, additional, DeBoer, Mark, additional, Madison, Helen, additional, McGill, Janet, additional, Buechler, Lori, additional, Clifton, Mary Jane, additional, Hurst, Stacy, additional, Kissel, Sarah, additional, Recklein, Carol, additional, Tsalikian, Eva, additional, Tansey, Michael, additional, Cabbage, Joanne, additional, Coffey, Julie, additional, Salamati, Sarah, additional, Clements, Mark, additional, Raman, Sripriya, additional, Turpin, Angela, additional, Bedard, Jennifer, additional, Cohoon, Cyndy, additional, Elrod, Aliza, additional, Fridlington, Amanda, additional, Hester, Lois, additional, Kruger, Davida, additional, Schatz, Desmond, additional, Clare-Salzler, Michael, additional, Cusi, Kenneth, additional, Digman, Colleen, additional, Fudge, Becky, additional, Haller, Mike, additional, Meehan, Collette, additional, Rohrs, Henry, additional, Silverstein, Janet, additional, Wagh, Sujata, additional, Cintron, Miriam, additional, Sheehan, Eleni, additional, Thomas, Jamie, additional, Daniels, Mark, additional, Clark, Susan, additional, Flannery, Timothy, additional, Forghani, Nikta, additional, Naidu, Ajanta, additional, Reh, Christina, additional, Scoggin, Peggy, additional, Trinh, Lien, additional, Ayala, Natalie, additional, Quintana, Rebeca, additional, Speer, Heather, additional, Zipf, William, additional, Seiple, Diane, additional, Kittelsrud, Julie, additional, Gupta, Ashutosh, additional, Peterson, Vikki, additional, Stoker, Ashley, additional, Gottschalk, Michael, additional, Hashiguchi, Marla, additional, Smith, Katheryn, additional, Rodriguez, Henry, additional, Bobik, Craig, additional, Henson, Danielle, additional, Simmons, Jill, additional, Potter, Amy, additional, Black, Margo, additional, Brendle, Faith, additional, Gubitosi-Klug, Rose, additional, Kaminski, Beth, additional, Bergant, Susan, additional, Campbell, Wendy, additional, Tasi, Catherine, additional, Copeland, Kenneth, additional, Beck, Joni, additional, Less, Joane, additional, Schanuel, Jill, additional, Tolbert, Jennifer, additional, Adi, Saleh, additional, Gerard-Gonzalez, Andrea, additional, Gitelman, Stephen, additional, Chettout, Nassim, additional, Torok, Christine, additional, Pihoker, Catherine, additional, Yi-Frazier, Joyce, additional, Kearns, Susan, additional, Libman, Ingrid, additional, Bills, Vicky, additional, Diaz, Ana, additional, Duke, Julie, additional, Nathan, Brandon, additional, Moran, Antoinette, additional, Bellin, Melena, additional, Beasley, Shannon, additional, Kogler, Anne, additional, Leschyshyn, Janice, additional, Schmid, Kara, additional, Street, Anne, additional, Nelson, Bryce, additional, Frost, Carrie, additional, Reifeis, Erin, additional, Haymond, Morey, additional, Bacha, Fida, additional, Caldas-Vasquez, Maria, additional, Klinepeter, Sara, additional, Redondo, Maria, additional, Berlanga, Rosa, additional, Falk, Teresa, additional, Garnes, Elizabeth, additional, Gonzalez, Janette, additional, Martinez, Cecilia, additional, Pontifes, Mariam, additional, Yulatic, Ronald, additional, Arnold, Kathleen, additional, Evans, Traci, additional, Sellers, Sharon, additional, Raman, Vandana, additional, Foster, Carol, additional, Murray, Mary, additional, Brown, Trina, additional, Slater, Hillarie, additional, Wheeler, Karen, additional, Harlan, David, additional, Lee, Mary, additional, Lock, John-Paul, additional, Hartigan, Celia, additional, Hubacz, Lisa, additional, Buse, John, additional, Calikoglu, Ali, additional, Largay, Joseph, additional, Young, Laura, additional, Brown, Helen, additional, Duncan, Vinnie, additional, Duclos, Michelle, additional, Tricome, Julie, additional, Brandenburg, Verdayne, additional, Blehm, Julie, additional, Hallanger-Johnson, Julie, additional, Hanson, Dawn, additional, Miller, Corliss, additional, Weiss, Jennifer, additional, Hoffman, Robert, additional, Chaudhari, Monika, additional, Repaske, David, additional, Gilson, Elizabeth, additional, Haines, Jesse, additional, Rudolph, Justen, additional, McClave, Charles, additional, Biersdorf, Doris, additional, Tello, Anthony, additional, Amundson, Donna, additional, Ward, Rhonda, additional, Rickels, Michael, additional, Dalton-Bakes, Cornelia, additional, Markman, Eileen, additional, Peleckis, Amy, additional, Rosenfeld, Nora, additional, Dolan, Lawrence, additional, Corathers, Sarah, additional, Kichler, Jessica, additional, Baugh, Holly, additional, Standiford, Debbie, additional, Hassing, Jeanne, additional, Jones, Jennifer, additional, Willis, Stephen, additional, Wysham, Carol, additional, Davis, Lisa, additional, Blackman, Scott, additional, Abel, Kimber-Lee, additional, Clark, Loretta, additional, Jonas, Andrea, additional, Kagan, Ellie, additional, Sosenko, Jay, additional, Blashke, Carlos, additional, Matheson, Della, additional, Edelen, Rachel, additional, Repas, Thomas, additional, Baldwin, Denise, additional, Borgwardt, Trista, additional, Conroy, Christina, additional, DeGrote, Kelly, additional, Marchiando, Rod, additional, Wasson, Michelle, additional, Fox, Larry, additional, Mauras, Nelly, additional, Damaso, Ligeia, additional, Englert, Kim, additional, Hamaty, Marwan, additional, Kennedy, Laurence, additional, Schweiger, Michelle, additional, Konstantinopoulos, Pantelis, additional, Mawhorter, Carolyn, additional, Orasko, Amy, additional, Rose, Denise, additional, Deeb, Larry, additional, Rohrbacher, Kim, additional, Schroeder, Leroy, additional, Roark, Amanda, additional, Ali, Omar, additional, Kramer, Joanna, additional, Whitson-Jones, Donna, additional, Gassner, Heidi, additional, Kollipara, Sobha, additional, Harwood, Katerina, additional, Prasad, Vijaya, additional, and Brault, Judy, additional

Published
2015
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48. Blocking IL-6 trans-Signaling Prevents High-Fat Diet-Induced Adipose Tissue Macrophage Recruitment but Does Not Improve Insulin Resistance

Author

Kraakman, Michael J., primary, Kammoun, Helene L., additional, Allen, Tamara L., additional, Deswaerte, Virginie, additional, Henstridge, Darren C., additional, Estevez, Emma, additional, Matthews, Vance B., additional, Neill, Bronwyn, additional, White, David A., additional, Murphy, Andrew J., additional, Peijs, Lone, additional, Yang, Christine, additional, Risis, Steve, additional, Bruce, Clinton R., additional, Du, Xiao-Jun, additional, Bobik, Alex, additional, Lee-Young, Robert S., additional, Kingwell, Bronwyn A., additional, Vasanthakumar, Ajithkumar, additional, Shi, Wei, additional, Kallies, Axel, additional, Lancaster, Graeme I., additional, Rose-John, Stefan, additional, and Febbraio, Mark A., additional

Published
2015
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