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565 results on '"Kitsis, Richard N."'

2. Priorities in Cardio-Oncology Basic and Translational Science: GCOS 2023 Symposium Proceedings: JACC: CardioOncology State-of-the-Art Review

Author

Salloum, Fadi N., Tocchetti, Carlo G., Ameri, Pietro, Ardehali, Hossein, Asnani, Aarti, de Boer, Rudolf A., Burridge, Paul, Cabrera, José-Ángel, de Castro, Javier, Córdoba, Raúl, Costa, Ambra, Dent, Susan, Engelbertsen, Daniel, Fernández-Velasco, María, Fradley, Mike, Fuster, José J., Galán-Arriola, Carlos, García-Lunar, Inés, Ghigo, Alessandra, González-Neira, Anna, Hirsch, Emilio, Ibáñez, Borja, Kitsis, Richard N., Konety, Suma, Lyon, Alexander R., Martin, Pilar, Mauro, Adolfo G., Mazo Vega, Manuel M., Meijers, Wouter C., Neilan, Tomas G., Rassaf, Tienush, Ricke-Hoch, Melanie, Sepulveda, Pilar, Thavendiranathan, Paaladinesh, van der Meer, Peter, Fuster, Valentin, Ky, Bonnie, and López-Fernández, Teresa

Published
2023
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3. Apoptotic cell death in disease—Current understanding of the NCCD 2023

Author

Vitale, Ilio, Pietrocola, Federico, Guilbaud, Emma, Aaronson, Stuart A., Abrams, John M., Adam, Dieter, Agostini, Massimiliano, Agostinis, Patrizia, Alnemri, Emad S., Altucci, Lucia, Amelio, Ivano, Andrews, David W., Aqeilan, Rami I., Arama, Eli, Baehrecke, Eric H., Balachandran, Siddharth, Bano, Daniele, Barlev, Nickolai A., Bartek, Jiri, Bazan, Nicolas G., Becker, Christoph, Bernassola, Francesca, Bertrand, Mathieu J. M., Bianchi, Marco E., Blagosklonny, Mikhail V., Blander, J. Magarian, Blandino, Giovanni, Blomgren, Klas, Borner, Christoph, Bortner, Carl D., Bove, Pierluigi, Boya, Patricia, Brenner, Catherine, Broz, Petr, Brunner, Thomas, Damgaard, Rune Busk, Calin, George A., Campanella, Michelangelo, Candi, Eleonora, Carbone, Michele, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K. -M., Chen, Guo-Qiang, Chen, Quan, Chen, Youhai H., Cheng, Emily H., Chipuk, Jerry E., Cidlowski, John A., Ciechanover, Aaron, Ciliberto, Gennaro, Conrad, Marcus, Cubillos-Ruiz, Juan R., Czabotar, Peter E., D’Angiolella, Vincenzo, Daugaard, Mads, Dawson, Ted M., Dawson, Valina L., De Maria, Ruggero, De Strooper, Bart, Debatin, Klaus-Michael, Deberardinis, Ralph J., Degterev, Alexei, Del Sal, Giannino, Deshmukh, Mohanish, Di Virgilio, Francesco, Diederich, Marc, Dixon, Scott J., Dynlacht, Brian D., El-Deiry, Wafik S., Elrod, John W., Engeland, Kurt, Fimia, Gian Maria, Galassi, Claudia, Ganini, Carlo, Garcia-Saez, Ana J., Garg, Abhishek D., Garrido, Carmen, Gavathiotis, Evripidis, Gerlic, Motti, Ghosh, Sourav, Green, Douglas R., Greene, Lloyd A., Gronemeyer, Hinrich, Häcker, Georg, Hajnóczky, György, Hardwick, J. Marie, Haupt, Ygal, He, Sudan, Heery, David M., Hengartner, Michael O., Hetz, Claudio, Hildeman, David A., Ichijo, Hidenori, Inoue, Satoshi, Jäättelä, Marja, Janic, Ana, Joseph, Bertrand, Jost, Philipp J., Kanneganti, Thirumala-Devi, Karin, Michael, Kashkar, Hamid, Kaufmann, Thomas, Kelly, Gemma L., Kepp, Oliver, Kimchi, Adi, Kitsis, Richard N., Klionsky, Daniel J., Kluck, Ruth, Krysko, Dmitri V., Kulms, Dagmar, Kumar, Sharad, Lavandero, Sergio, Lavrik, Inna N., Lemasters, John J., Liccardi, Gianmaria, Linkermann, Andreas, Lipton, Stuart A., Lockshin, Richard A., López-Otín, Carlos, Luedde, Tom, MacFarlane, Marion, Madeo, Frank, Malorni, Walter, Manic, Gwenola, Mantovani, Roberto, Marchi, Saverio, Marine, Jean-Christophe, Martin, Seamus J., Martinou, Jean-Claude, Mastroberardino, Pier G., Medema, Jan Paul, Mehlen, Patrick, Meier, Pascal, Melino, Gerry, Melino, Sonia, Miao, Edward A., Moll, Ute M., Muñoz-Pinedo, Cristina, Murphy, Daniel J., Niklison-Chirou, Maria Victoria, Novelli, Flavia, Núñez, Gabriel, Oberst, Andrew, Ofengeim, Dimitry, Opferman, Joseph T., Oren, Moshe, Pagano, Michele, Panaretakis, Theocharis, Pasparakis, Manolis, Penninger, Josef M., Pentimalli, Francesca, Pereira, David M., Pervaiz, Shazib, Peter, Marcus E., Pinton, Paolo, Porta, Giovanni, Prehn, Jochen H. M., Puthalakath, Hamsa, Rabinovich, Gabriel A., Rajalingam, Krishnaraj, Ravichandran, Kodi S., Rehm, Markus, Ricci, Jean-Ehrland, Rizzuto, Rosario, Robinson, Nirmal, Rodrigues, Cecilia M. P., Rotblat, Barak, Rothlin, Carla V., Rubinsztein, David C., Rudel, Thomas, Rufini, Alessandro, Ryan, Kevin M., Sarosiek, Kristopher A., Sawa, Akira, Sayan, Emre, Schroder, Kate, Scorrano, Luca, Sesti, Federico, Shao, Feng, Shi, Yufang, Sica, Giuseppe S., Silke, John, Simon, Hans-Uwe, Sistigu, Antonella, Stephanou, Anastasis, Stockwell, Brent R., Strapazzon, Flavie, Strasser, Andreas, Sun, Liming, Sun, Erwei, Sun, Qiang, Szabadkai, Gyorgy, Tait, Stephen W. G., Tang, Daolin, Tavernarakis, Nektarios, Troy, Carol M., Turk, Boris, Urbano, Nicoletta, Vandenabeele, Peter, Vanden Berghe, Tom, Vander Heiden, Matthew G., Vanderluit, Jacqueline L., Verkhratsky, Alexei, Villunger, Andreas, von Karstedt, Silvia, Voss, Anne K., Vousden, Karen H., Vucic, Domagoj, Vuri, Daniela, Wagner, Erwin F., Walczak, Henning, Wallach, David, Wang, Ruoning, Wang, Ying, Weber, Achim, Wood, Will, Yamazaki, Takahiro, Yang, Huang-Tian, Zakeri, Zahra, Zawacka-Pankau, Joanna E., Zhang, Lin, Zhang, Haibing, Zhivotovsky, Boris, Zhou, Wenzhao, Piacentini, Mauro, Kroemer, Guido, and Galluzzi, Lorenzo

Published
2023
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5. Beth Levine in memoriam

Author

An, Zhenyi, Ballabio, Andrea, Bennett, Lynda, Boya, Patricia, Cecconi, Francesco, Chiang, Wei-Chung, Codogno, Patrice, Colombo, Maria Isabel, Cuervo, Ana Maria, Debnath, Jayanta, Deretic, Vojo, Dikic, Ivan, Dionne, Keith, Dong, Xiaonan, Elazar, Zvulun, Galluzzi, Lorenzo, Gentile, Frank, Griffin, Diane E, Hansen, Malene, Hardwick, J Marie, He, Congcong, Huang, Shu-Yi, Hurley, James, Jackson, William T, Jozefiak, Cindy, Kitsis, Richard N, Klionsky, Daniel J, Kroemer, Guido, Meijer, Alfred J, Melendez, Alicia, Melino, Gerry, Mizushima, Noboru, Murphy, Leon O, Nixon, Ralph, Orvedahl, Anthony, Pattingre, Sophie, Piacentini, Mauro, Reggiori, Fulvio, Ross, Theodora, Rubinsztein, David C, Ryan, Kevin, Sadoshima, Junichi, Schreiber, Stuart L, Scott, Frederick, Sebti, Salwa, Shiloh, Michael, Shoji, Sanae, Simonsen, Anne, Smith, Haley, Sumpter, Kathryn M, Thompson, Craig B, Thorburn, Andrew, Thumm, Michael, Tooze, Sharon, Vaccaro, Maria I, Virgin, Herbert W, Wang, Fei, White, Eileen, Xavier, Ramnik J, Yoshimori, Tamotsu, Yuan, Junying, Yue, Zhenyu, and Zhong, Qing

Subjects
Biochemistry and Cell Biology, Biological Sciences, Biochemistry & Molecular Biology, Biochemistry and cell biology
Published
2020

6. Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018

Author

Galluzzi, Lorenzo, Vitale, Ilio, Aaronson, Stuart A, Abrams, John M, Adam, Dieter, Agostinis, Patrizia, Alnemri, Emad S, Altucci, Lucia, Amelio, Ivano, Andrews, David W, Annicchiarico-Petruzzelli, Margherita, Antonov, Alexey V, Arama, Eli, Baehrecke, Eric H, Barlev, Nickolai A, Bazan, Nicolas G, Bernassola, Francesca, Bertrand, Mathieu JM, Bianchi, Katiuscia, Blagosklonny, Mikhail V, Blomgren, Klas, Borner, Christoph, Boya, Patricia, Brenner, Catherine, Campanella, Michelangelo, Candi, Eleonora, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K-M, Chandel, Navdeep S, Cheng, Emily H, Chipuk, Jerry E, Cidlowski, John A, Ciechanover, Aaron, Cohen, Gerald M, Conrad, Marcus, Cubillos-Ruiz, Juan R, Czabotar, Peter E, D’Angiolella, Vincenzo, Dawson, Ted M, Dawson, Valina L, De Laurenzi, Vincenzo, De Maria, Ruggero, Debatin, Klaus-Michael, DeBerardinis, Ralph J, Deshmukh, Mohanish, Di Daniele, Nicola, Di Virgilio, Francesco, Dixit, Vishva M, Dixon, Scott J, Duckett, Colin S, Dynlacht, Brian D, El-Deiry, Wafik S, Elrod, John W, Fimia, Gian Maria, Fulda, Simone, García-Sáez, Ana J, Garg, Abhishek D, Garrido, Carmen, Gavathiotis, Evripidis, Golstein, Pierre, Gottlieb, Eyal, Green, Douglas R, Greene, Lloyd A, Gronemeyer, Hinrich, Gross, Atan, Hajnoczky, Gyorgy, Hardwick, J Marie, Harris, Isaac S, Hengartner, Michael O, Hetz, Claudio, Ichijo, Hidenori, Jäättelä, Marja, Joseph, Bertrand, Jost, Philipp J, Juin, Philippe P, Kaiser, William J, Karin, Michael, Kaufmann, Thomas, Kepp, Oliver, Kimchi, Adi, Kitsis, Richard N, Klionsky, Daniel J, Knight, Richard A, Kumar, Sharad, Lee, Sam W, Lemasters, John J, Levine, Beth, Linkermann, Andreas, Lipton, Stuart A, Lockshin, Richard A, López-Otín, Carlos, Lowe, Scott W, Luedde, Tom, Lugli, Enrico, MacFarlane, Marion, Madeo, Frank, Malewicz, Michal, Malorni, Walter, and Manic, Gwenola

Subjects
Biochemistry and Cell Biology, Biological Sciences, Animals, Cell Death, Humans, Lysosomes, Mitochondrial Membrane Transport Proteins, Mitochondrial Permeability Transition Pore, Necrosis, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract

Over the past decade, the Nomenclature Committee on Cell Death (NCCD) has formulated guidelines for the definition and interpretation of cell death from morphological, biochemical, and functional perspectives. Since the field continues to expand and novel mechanisms that orchestrate multiple cell death pathways are unveiled, we propose an updated classification of cell death subroutines focusing on mechanistic and essential (as opposed to correlative and dispensable) aspects of the process. As we provide molecularly oriented definitions of terms including intrinsic apoptosis, extrinsic apoptosis, mitochondrial permeability transition (MPT)-driven necrosis, necroptosis, ferroptosis, pyroptosis, parthanatos, entotic cell death, NETotic cell death, lysosome-dependent cell death, autophagy-dependent cell death, immunogenic cell death, cellular senescence, and mitotic catastrophe, we discuss the utility of neologisms that refer to highly specialized instances of these processes. The mission of the NCCD is to provide a widely accepted nomenclature on cell death in support of the continued development of the field.

Published
2018

7. Modulating mitofusins to control mitochondrial function and signaling

Author

Zacharioudakis, Emmanouil, Agianian, Bogos, Kumar MV, Vasantha, Biris, Nikolaos, Garner, Thomas P., Rabinovich-Nikitin, Inna, Ouchida, Amanda T., Margulets, Victoria, Nordstrøm, Lars Ulrik, Riley, Joel S., Dolgalev, Igor, Chen, Yun, Wittig, Andre J. H., Pekson, Ryan, Mathew, Chris, Wei, Peter, Tsirigos, Aristotelis, Tait, Stephen W. G., Kirshenbaum, Lorrie A., Kitsis, Richard N., and Gavathiotis, Evripidis

Published
2022
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12. A small-molecule allosteric inhibitor of BAX protects against doxorubicin-induced cardiomyopathy

Author

Amgalan, Dulguun, Garner, Thomas P., Pekson, Ryan, Jia, Xiaotong F., Yanamandala, Mounica, Paulino, Victor, Liang, Felix G., Corbalan, J. Jose, Lee, Jaehoon, Chen, Yun, Karagiannis, George S., Sanchez, Luis Rivera, Liang, Huizhi, Narayanagari, Swathi-Rao, Mitchell, Kelly, Lopez, Andrea, Margulets, Victoria, Scarlata, Marco, Santulli, Gaetano, Asnani, Aarti, Peterson, Randall T., Hazan, Rachel B., Condeelis, John S., Oktay, Maja H., Steidl, Ulrich, Kirshenbaum, Lorrie A., Gavathiotis, Evripidis, and Kitsis, Richard N.

Published
2020
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14. PDCD5 says no to NO

Author

Riascos-Bernal, Dario F., Sibinga, Nicholas E. S., and Kitsis, Richard N.

Published
2018

18. SNAP23 regulates BAX-dependent adipocyte programmed cell death independently of canonical macroautophagy

Author

Feng, Daorong, Amgalan, Dulguun, Singh, Rajat, Wei, Jianwen, Wen, Jennifer, Wei, Tszki Peter, McGraw, Timothy E., Kitsis, Richard N., and Pessin, Jeffrey E.

Subjects
Apoptotic proteins -- Physiological aspects -- Health aspects, Adipocytes -- Physiological aspects -- Health aspects, Autophagy (Cytology) -- Health aspects, Membrane proteins -- Physiological aspects -- Health aspects, Health care industry
Abstract

The t-SNARE protein SNAP23 conventionally functions as a component of the cellular machinery required for intracellular transport vesicle fusion with target membranes and has been implicated in the regulation of fasting glucose levels, BMI, and type 2 diabetes. Surprisingly, we observed that adipocyte-specific KO of SNAP23 in mice resulted in a temporal development of severe generalized lipodystrophy associated with adipose tissue inflammation, insulin resistance, hyperglycemia, liver steatosis, and early death. This resulted from adipocyte cell death associated with an inhibition of macroautophagy and lysosomal degradation of the proapoptotic regulator BAX, with increased BAX activation. BAX colocalized with LC3- positive autophagic vacuoles and was increased upon treatment with lysosome inhibitors. Moreover, BAX deficiency suppressed the lipodystrophic phenotype in the adipocyte-specific SNAP23-KO mice and prevented cell death. In addition, ATG9 deficiency phenocopied SNAP23 deficiency, whereas ATG7 deficiency had no effect on BAX protein levels, BAX activation, or apoptotic cell death. These data demonstrate a role for SNAP23 in the control of macroautophagy and programmed cell death through an ATG9-dependent, but ATG7-independent, pathway regulating BAX protein levels and BAX activation., Introduction SNARE complexes are a large group of membrane-bound proteins that regulate the fusion of intracellular transport vesicles with their target membranes (1-3). All SNAREs contain a characteristic coiled-coil SNARE [...]

Published
2018
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20. Osteocalcin Signaling in Myofibers Is Necessary and Sufficient for Optimum Adaptation to Exercise

Author

Mera, Paula, Laue, Kathrin, Ferron, Mathieu, Confavreux, Cyril, Wei, Jianwen, Galán-Díez, Marta, Lacampagne, Alain, Mitchell, Sarah J., Mattison, Julie A., Chen, Yun, Bacchetta, Justine, Szulc, Pawel, Kitsis, Richard N., de Cabo, Rafael, Friedman, Richard A., Torsitano, Christopher, McGraw, Timothy E., Puchowicz, Michelle, Kurland, Irwin, and Karsenty, Gerard

Published
2016
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21. Immune checkpoint inhibitor-associated myocarditis: manifestations and mechanisms

Author

Moslehi, Javid, Lichtman, Andrew H., Sharpe, Arlene H., Galluzzi, Lorenzo, and Kitsis, Richard N.

Subjects
Enzyme inhibitors -- Complications and side effects, Myocarditis -- Development and progression -- Drug therapy, Health care industry
Abstract

Immune checkpoint inhibitors (ICIs) have transformed the treatment of various cancers, including malignancies once considered untreatable. These agents, however, are associated with inflammation and tissue damage in multiple organs. Myocarditis has emerged as a serious ICI-associated toxicity, because, while seemingly infrequent, it is often fulminant and lethal. The underlying basis of ICI-associated myocarditis is not completely understood. While the importance of T cells is clear, the inciting antigens, why they are recognized, and the mechanisms leading to cardiac cell injury remain poorly characterized. These issues underscore the need for basic and clinical studies to define pathogenesis, identify predictive biomarkers, improve diagnostic strategies, and develop effective treatments. An improved understanding of ICI- associated myocarditis will provide insights into the equilibrium between the immune and cardiovascular systems., Introduction Immune checkpoint inhibitors (ICIs) have emerged as highly effective therapies for many cancers (1, 2). Thus far, all approved ICIs are monoclonal antibodies that block cytotoxic T lymphocyte-associated protein [...]

Published
2021
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22. Unlocking the Secrets of Mitochondria in the Cardiovascular System: Path to a Cure in Heart Failure—A Report from the 2018 National Heart, Lung, and Blood Institute Workshop

Author

Tian, Rong, Colucci, Wilson S., Arany, Zoltan, Bachschmid, Markus M., Ballinger, Scott W., Boudina, Sihem, Bruce, James E., Busija, David W., Dikalov, Sergey, Dorn, Gerald W., II, Galis, Zorina S., Gottlieb, Roberta A., Kelly, Daniel P., Kitsis, Richard N., Kohr, Mark J., Levy, Daniel, Lewandowski, E. Douglas, McClung, Joseph M., Mochly-Rosen, Daria, O’Brien, Kevin D., O’Rourke, Brian, Park, Joon-Young, Ping, Peipei, Sack, Michael N., Sheu, Shey-Shing, Shi, Yang, Shiva, Sruti, Wallace, Douglas C., Weiss, Robert G., Vernon, Hilary J., Wong, Renee, Longacre, Lisa Schwartz, and Shi, Scarlet

Published
2019
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23. Apoptotic cell death in disease—Current understanding of the NCCD 2023

Author

Associazione Italiana per la Ricerca sul Cancro, Italian Institute for Genomic Medicine, Compagnia di San Paolo, Vitale, Ilio [0000-0002-5918-1841], Pietrocola, Federico [0000-0002-2930-234X], Guilbaud, Emma [0000-0001-5261-1944], Aaronson, Stuart A. [0000-0002-4643-0474], Dieter, Adam [0000-0002-5668-5032], Agostini, Massimiliano [0000-0003-3124-2072], Agostinis, Patrizia [0000-0003-1314-2115], Alnemri, Emad S. [0000-0002-7295-3383], Altucci, Lucia [0000-0002-7312-5387], Amelio, Ivano [0000-0002-9126-5391], Andrews, David W. [0000-0002-9266-7157], Aqeilan, Rami I. [0000-0002-6034-023X], Arama, Eli [0000-0001-5953-0629], Balachandran, Siddharth [0000-0003-2084-1803], Bano, Daniele [0000-0002-9617-5504], Bartek, Jiri [0000-0003-2013-7525], Bazan, Nicolas G. [0000-0002-9243-5444], Bernassola, Francesca [0000-0002-8883-8654], Bertrand, Mathieu J. M. [0000-0001-9000-0626], Bianchi, Marco Emilio [0000-0002-5329-6445], Blander, J. Magarian [0000-0001-9207-1700], Blandino, Giovanni [0000-0002-6970-2241], Blomgren, Klas [0000-0002-0476-7271], Bortner, Carl D. [0000-0002-5444-6628], Bove, Pierluigi [0000-0002-4788-2982], Boya, Patricia [0000-0003-3045-951X], Broz, Petr [0000-0002-2334-7790], Damgaard, Rune Busk [0000-0002-1709-6534], Calin, George A. [0000-0002-7427-0578], Campanella, Michelangelo [0000-0002-6948-4184], Candi, Eleonora [0000-0001-8332-4825], Carbone, Michele [0000-0001-8928-8474], Carmona-Gutierrez, Didac [0000-0001-7548-7771], Cecconi, Francesco [0000-0002-5614-4359], Chen, Guo‑Qiang [0000-0002-7226-1782], Cheng, Emily H. [0000-0002-3595-2648], Chipuk, Jerry E. [0000-0002-1337-842X], Cidlowski, John A. [0000-0003-1420-0516], Ciechanover, Aaron [0000-0001-9184-8944], Ciliberto, Gennaro [0000-0003-2851-8605], Conrad, Marcus [0000-0003-1140-5612], Czabotar, Peter E. [0000-0002-2594-496X], D’Angiolella, Vincenzo [0000-0001-8365-9094], Daugaard, Mads [0000-0001-8383-055X], Dawson, Valina L. [0000-0002-2915-3970], De Maria, Ruggero [0000-0003-2255-0583], Debatin, Klaus-Michael [0000-0002-8397-1886], Deberardinis, Ralph J. [0000-0002-2705-7432], Degterev, Alexei [0000-0002-8240-7132], Del Sal, Giannino [0000-0003-2185-6003], Deshmukh, Mohanish [0000-0002-2597-5862], Di Virgilio, Francesco [0000-0003-3566-1362], Diederich, Marc [0000-0003-0115-4725], Dixon, Scott J. [0000-0001-6230-8199], El-Deiry, Wafik S. [0000-0002-9577-8266], Elrod, John W. [0000-0003-3925-2224], Engeland, Kurt [0000-0003-3525-0440], Fimia, Gian María [0000-0003-4438-3325], Ganini, Carlo [0000-0002-5839-3965], García-Sáez, Ana J. [0000-0002-3894-5945], Garg, Abhishek D. [0000-0002-9976-9922], Garrido, Carmen [0000-0003-1368-1493], Gavathiotis, Evripidis [0000-0001-6319-8331], Ghosh, Sourav [0000-0001-5990-8708], Green, Douglas R. [0000-0002-7332-1417], Gronemeyer, Hinrich [0000-0001-9454-2449}, Häcker, Georg [0000-0003-1058-5746], Hajnóczky, György [0000-0003-3813-2570], Hardwick, J. Marie [0000-0002-4847-2045], Haupt, Ygal [0000-0001-5925-0096], He, Sudan [0000-0002-0846-1210], Heery, David M. [0000-0002-5035-2392], Hengartner, Michael O. [0000-0002-7584-596X], Hetz, Claudio [0000-0003-1120-7966], Hildeman, David A. [0000-0002-0421-8483], Ichijo, Hidenori [0000-0002-5005-6438], Jäättelä, Marja [0000-0001-5950-7111], Janic, Ana [0000-0002-4200-2560], Joseph, Bertrand [0000-0001-5655-9979], Jost, Philipp J. [0000-0003-2454-0362], Kanneganti, Thirumala-Devi [0000-0002-6395-6443], Karin, Michael [0000-0002-2758-6473], Kashkar, Hamid [0000-0003-2796-1429], Kaufmann, Thomas [0000-0001-9906-874X], Kelly, Gemma L. [0000-0002-6533-1201], Kepp, Oliver [0000-0002-6081-9558], Kimchi, Adi [0000-0002-8236-8989], Klionsky, Daniel J. [0000-0002-7828-8118], Kluck, Ruth [0000-0002-7101-1925], Krysko, Dmitri V. [0000-0002-9692-2047], Kulms, Dagmar [0000-0001-6874-0548], Kumar, Sharad [0000-0001-7126-9814], Lavandero, Sergio [0000-0003-4258-1483], Lavrik, Inna N. [0000-0002-9324-309X], Liccardi, Gianmaria [0000-0002-2662-1281], Linkermann, Andreas [0000-0001-6287-9725], Lipton, Stuart A. [0000-0002-3490-1259], Lockshin, Richard A. [0000-0002-4389-4898], López-Otín, Carlos [0000-0001-6964-1904], Luedde, Tom [0000-0002-6288-8821], MacFarlane, Marion [0000-0001-7886-1159], Madeo, Frank [0000-0002-5070-1329], Malorni, Walter [0000-0002-1223-7000], Manic, Gwenola [0000-0003-3759-8029], Marchi, Saverio [0000-0003-2708-1843], Marine, Jean-Christophe [0000-0003-2433-9837], Martin, Seamus J. [0000-0002-8539-3143], Martinou, Jean-Claude [0000-0002-9847-2051], Mastroberardino, Pier G. [0000-0003-2364-4258], Medema, Jan Paul [0000-0003-3045-2924], Mehlen, Patrick [0000-0003-1743-5417], Meier, Pascal [0000-0003-2760-6523], Melino, Gerry [0000-0001-9428-5972], Melino, Sonia [0000-0001-7694-5279], Miao, Edward A. [0000-0001-7295-3490], Moll, Ute M. [0000-0003-1908-7516], Muñoz-Pinedo, Cristina [0000-0002-9120-664X], Murphy, Daniel J. [0000-0002-5538-5468], Niklison-Chirou, Maria Victoria [0000-0002-2147-370X], Novelli, Flavia [0000-0002-3746-7478], Oberst, Andrew [0000-0002-9500-7912], Ofengeim, Dimitry [0000-0003-2348-3642], Opferman, Joseph T. [0000-0002-1147-5621], Oren, Moshe [0000-0003-4311-7172], Pagano, Michele [0000-0003-3210-2442], Panaretakis, Theocharis [0000-0001-5754-6950], Pasparakis, Manolis [0000-0002-9870-0966], Penninger, Josef M. [0000-0002-8194-3777], Pentimalli, Francesca [0000-0003-4740-6801], Pereira, David M. [0000-0003-0384-7592], Pervaiz, Shazib [0000-0002-4738-019X], Peter, Marcus E. [0000-0003-3216-036X], Pinton, Paolo [0000-0001-7108-6508], Porta, Giovanni [0000-0001-5260-2415], Puthalakath, Hamsa [0000-0001-5178-1175], Rabinovich, Gabriel A. [0000-0002-0947-8735], Rajalingam, Krishnaraj [0000-0002-4175-9633], Ravinchandran, Kodi S. [0000-0001-9049-1410], Rehm, Markus [0000-0001-6149-9261], Ricci, Jean-Ehrland [0000-0003-1585-8117], Rizzuto, Rosario [0000-0001-7044-5097], Robinson, Nirmal [0000-0002-7361-9491], Rotblat, Barak [0000-0003-2985-7115], Rothlin, Carla V. [0000-0002-5693-5572], Rubinsztein, David C. [0000-0001-5002-5263], Rufini, Alessandro [0000-0002-5855-655X], Ryan, Kevin M. [0000-0002-1059-9681], Sarosiek, Kristopher A. [0000-0002-4618-5085], Sawa, Akira [0000-0003-1401-3008], Sayan, Emre [0000-0002-5291-1485], Schroder, Kate [0000-0001-9261-3805], Scorrano, Luca [0000-0002-8515-8928], Sesti, Federico [0000-0002-2761-9693], Shi, Yufang [0000-0001-8964-319X], Sica, Giuseppe [0000-0002-7407-0584], Silke, John [0000-0002-7611-5774], Simon, Hans-Uwe [0000-0002-9404-7736], Sistigu, Antonella [0000-0002-2528-1238], Stockwell, Brent R. 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Abstract

Apoptosis is a form of regulated cell death (RCD) that involves proteases of the caspase family. Pharmacological and genetic strategies that experimentally inhibit or delay apoptosis in mammalian systems have elucidated the key contribution of this process not only to (post-)embryonic development and adult tissue homeostasis, but also to the etiology of multiple human disorders. Consistent with this notion, while defects in the molecular machinery for apoptotic cell death impair organismal development and promote oncogenesis, the unwarranted activation of apoptosis promotes cell loss and tissue damage in the context of various neurological, cardiovascular, renal, hepatic, infectious, neoplastic and inflammatory conditions. Here, the Nomenclature Committee on Cell Death (NCCD) gathered to critically summarize an abundant pre-clinical literature mechanistically linking the core apoptotic apparatus to organismal homeostasis in the context of disease.

Published
2023

24. Supplemental Figure.1 from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
Full Text
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25. Supplemental Figure. 5 from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
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26. Supplemental Figure. 3 from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
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27. Supplemental methods from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
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28. Data from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
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29. Supplementary Figure legends from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
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30. Supplemental Figure. 2 from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
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31. Supplemental Figure. 4 from An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis

Author

Suyama, Kimita, primary, Yao, Jiahong, primary, Liang, Huizhi, primary, Benard, Outhiriaradjou, primary, Loudig, Olivier D., primary, Amgalan, Dulguun, primary, McKimpson, Wendy M., primary, Phillips, Greg R., primary, Segall, Jeffrey, primary, Wang, Yihong, primary, Fineberg, Susan, primary, Norton, Larry, primary, Kitsis, Richard N., primary, and Hazan, Rachel B., primary

Published
2023
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40. Correcting mitochondrial fusion by manipulating mitofusin conformations

Author

Franco, Antonietta, Kitsis, Richard N., Fleischer, Julie A., Gavathiotis, Evripidis, Kornfeld, Opher S., Gong, Guohua, Biris, Nikolaos, Benz, Ann, Qvit, Nir, Donnelly, Sara K., Chen, Yun, Mennerick, Steven, Hodgson, Louis, Mochly-Rosen, Daria, and Dorn II, Gerald W.

Subjects
Cellular proteins -- Physiological aspects -- Genetic aspects, Gene mutation -- Research, Cytological research, Mitochondria -- Physiological aspects -- Genetic aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Mitochondria are dynamic organelles that exchange contents and undergo remodelling during cyclic fusion and fission. Genetic mutations in MFN2 (the gene encoding mitofusin 2) interrupt mitochondrial fusion and cause the untreatable neurodegenerative condition Charcot-Marie-Tooth disease type 2A (CMT2A). It has not yet been possible to directly modulate mitochondrial fusion, in part because the structural basis of mitofusin function is not completely understood. Here we show that mitofusins adopt either a fusion-constrained or a fusion-permissive molecular conformation, directed by specific intramolecular binding interactions, and demonstrate that mitofusin-dependent mitochondrial fusion can be regulated in mouse cells by targeting these conformational transitions. On the basis of this model, we engineered a cell-permeant minipeptide to destabilize the fusion-constrained conformation of mitofusin and promote the fusion-permissive conformation, reversing mitochondrial abnormalities in cultured fibroblasts and neurons that harbour CMT2A-associated genetic defects. The relationship between the conformational plasticity of mitofusin 2 and mitochondrial dynamism reveals a central mechanism that regulates mitochondrial fusion, the manipulation of which can correct mitochondrial pathology triggered by defective or imbalanced mitochondrial dynamics., Author(s): Antonietta Franco [1]; Richard N. Kitsis [2]; Julie A. Fleischer [1]; Evripidis Gavathiotis [3]; Opher S. Kornfeld [4]; Guohua Gong [1]; Nikolaos Biris [3]; Ann Benz [5]; Nir Qvit [...]

Published
2016
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43. Bax regulates primary necrosis through mitochondrial dynamics

Author

Whelan, Russell S., Konstantinidis, Klitos, Wei, An-Chi, Chen, Yun, Reyna, Denis E., Jha, Saurabh, Yang, Ying, Calvert, John W., Lindsten, Tullia, Thompson, Craig B., Crow, Michael T., Gavathiotis, Evripidis, Dorn, Gerald W., O'Rourke, Brian, and Kitsis, Richard N.

Published
2012

49. Regulation of p53 Tetramerization and Nuclear Export by ARC

Author

Foo, Roger S.-Y., Nam, Young-Jae, Ostreicher, Marc Jason, Metzl, Mark D., Whelan, Russell S., Peng, Chang-Fu, Ashton, Anthony W., Fu, Weimin, Mani, Kartik, Chin, Suet-Feung, Provenzano, Elena, Ellis, Ian, Figg, Nichola, Pinder, Sarah, Bennett, Martin R., Caldas, Carlos, and Kitsis, Richard N.

Published
2007
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50. IDH2-mediated regulation of the biogenesis of the oxidative phosphorylation system

Author

Murari, Anjaneyulu, primary, Goparaju, Naga S. V., additional, Rhooms, Shauna-Kay, additional, Hossain, Kaniz F. B., additional, Liang, Felix G., additional, Garcia, Christian J., additional, Osei, Cindy, additional, Liu, Tong, additional, Li, Hong, additional, Kitsis, Richard N., additional, Patel, Rajesh, additional, and Owusu-Ansah, Edward, additional

Published
2022
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