Results 91 to 100 of about 17,129 (242)

Receptor-Interacting Protein Kinase 3 Deficiency Delays Cutaneous Wound Healing. [PDF]

PLoS ONE, 2015
Wound healing consists of a complex, dynamic and overlapping process involving inflammation, proliferation and tissue remodeling. A better understanding of wound healing process at the molecular level is needed for the development of novel therapeutic ...
Andrew Godwin, Archna Sharma, Weng-Lang Yang, Zhimin Wang, Jeffrey Nicastro, Gene F Coppa, Ping Wang   +6 more
doaj   +1 more source

Poly-ubiquitination in TNFR1-mediated necroptosis [PDF]

, 2016
Tumor necrosis factor (TNF) is a master pro-inflammatory cytokine, and inappropriate TNF signaling is implicated in the pathology of many inflammatory diseases.
Henning Walczak, Mathieu J. M. Bertrand, Maurice Darding, Yves Dondelinger   +3 more
core   +3 more sources

Targeting necroptosis protects against astrocyte death and hippocampal sclerosis in experimental temporal lobe epilepsy

The Journal of Physiology, EarlyView.
Abstract figure legend Experimentally induced status epilepticus induces microglial TNFα release, which binds to astrocytic TNFR1 and triggers activation of RIPK1/RIPK3/MLKL signalling, initiating necroptotic astrocytic death that contributes to the development of hippocampal sclerosis. Created with Biorender.com.
Zhou Wu, Lukas Henning, Christian Steinhäuser, Peter Bedner   +3 more
wiley   +1 more source

RIPK1 and RIPK3 regulate TNFα-induced β-cell death in concert with caspase activity

Molecular Metabolism, 2022
Objective: Type 1 diabetes (T1D) is characterized by autoimmune-associated β-cell loss, insulin insufficiency, and hyperglycemia. Although TNFα signaling is associated with β-cell loss and hyperglycemia in non-obese diabetic mice and human T1D, the ...
Christopher J. Contreras, Noyonika Mukherjee, Renato C.S. Branco, Li Lin, Meghan F. Hogan, Erica P. Cai, Andrew A. Oberst, Steven E. Kahn, Andrew T. Templin   +8 more
doaj   +1 more source

Molecular mechanisms of cell death:recommendations of the Nomenclature Committee on Cell Death 2018 [PDF]

, 2018
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.
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 J. M., 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, Galluzzi, Lorenzo, Garcia-Saez, 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., Heiden, Matthew G. Vander, Hengartner, Michael O., Hetz, Claudio, Ichijo, Hidenori, Jaattela, 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., Kroemer, Guido, Kumar, Sharad, Lee, Sam W., Lemasters, John J., Levine, Beth, Linkermann, Andreas, Lipton, Stuart A., Lockshin, Richard A., Lopez-Otin, Carlos, Lowe, Scott W., Luedde, Tom, Lugli, Enrico, MacFarlane, Marion, Madeo, Frank, Malewicz, Michal, Malorni, Walter, Manic, Gwenola, Marine, Jean-Christophe, Martin, Seamus J., Martinou, Jean-Claude, Medema, Jan Paul, Mehlen, Patrick, Meier, Pascal, Melino, Gerry, Melino, Sonia, Miao, Edward A., Molkentin, Jeffery D., Moll, Ute M., Munoz-Pinedo, Cristina, Nagata, Shigekazu, Nunez, Gabriel, Oberst, Andrew, Oren, Moshe, Overholtzer, Michael, Pagano, Michele, Panaretakis, Theocharis, Pasparakis, Manolis, Penninger, Josef M., Pereira, David M., Pervaiz, Shazib, Peter, Marcus E., Piacentini, Mauro, Pinton, Paolo, Prehn, Jochen H. M., Puthalakath, Hamsa, Rabinovich, Gabriel A., Rehm, Markus, Rizzuto, Rosario, Rodrigues, Cecilia M. P., Rubinsztein, David C., Rudel, Thomas, Ryan, Kevin M., Sayan, Emre, Scorrano, Luca, Shao, Feng, Shi, Yufang, Silke, John, Simon, Hans-Uwe, Sistigu, Antonella, Stockwell, Brent R., Strasser, Andreas, Szabadkai, Gyorgy, Tait, Stephen W. G., Tang, Daolin, Tavernarakis, Nektarios, Thorburn, Andrew, Tsujimoto, Yoshihide, Turk, Boris, Vanden Berghe, Tom, Vandenabeele, Peter, Villunger, Andreas, Virgin, Herbert W., Vitale, Ilio, Vousden, Karen H., Vucic, Domagoj, Wagner, Erwin F., Walczak, Henning, Wallach, David, Wang, Ying, Wells, James A., Wood, Will, Yuan, Junying, Zakeri, Zahra, Zhivotovsky, Boris, Zitvogel, Laurence   +168 more
core   +25 more sources

The mitochondrial‐targeted antioxidant SkQ1 prevents skeletal muscle mitochondrial‐apoptotic but not necroptotic signalling during ovarian cancer

The Journal of Physiology, EarlyView.
Abstract figure legend An evaluation of the degree to which mitochondrial hydrogen peroxide emission (mH2O2)‐mediated apoptotic and necroptotic signalling contributes to skeletal muscle atrophy in an orthotopic epithelial ovarian cancer (EOC) model. To determine whether attenuating mH2O2 could prevent regulated cell death signalling and mitigate muscle
Shahrzad Khajehzadehshoushtar, Luca J. Delfinis, Fasih A. Rahman, Madison C. Garibotti, Shivam Gandhi, Aditya N. Brahmbhatt, Brooke A. Morris, Bianca Garlisi, Sylvia Lauks, Caroline Aitken, Leslie Ogilvie, Zhu‐Xu Zhang, Jeremy A. Simpson, Joe Quadrilatero, Jim Petrik, Christopher G. R. Perry   +15 more
wiley   +1 more source

Distinct Kinase-Independent Role of RIPK3 in CD11c+ Mononuclear Phagocytes in Cytokine-Induced Tissue Repair

Cell Reports, 2017
Receptor interacting protein kinase 3 (RIPK3) induces necroptosis, a type of regulated necrosis, through its kinase domain and receptor interacting protein (RIP) homotypic interaction motif (RHIM).
Kenta Moriwaki, Sakthi Balaji, John Bertin, Peter J. Gough, Francis Ka-Ming Chan   +4 more
doaj   +1 more source

Procyanidin Capsules Combat ALF by Restoring Mitochondrial Homeostasis and Inhibiting Necroptosis via the PGAM5/DRP1/PINK1 Pathway

Advanced Science, Volume 13, Issue 7, 3 February 2026.
A biomimetic self‐assembly strategy, Procyanidin Capsules (PC‐Ca), has been developed, which has great stability, bioavailability, and liver‐targeting efficacy and modulates the KEAP1‐NRF2 axis to inhibit ROS formation and necroptosis, regulate mitochondrial homeostasis through the PGAM5/DRP1/PINK1 signaling pathway in thioacetamide (TAA)‐induced ALF ...
Qing Shi, Minmin Wu, Jinwei Zhong, Chao Chen, Zhuang Huang, Jingxuan Peng, Dong Yang, Xingjie Zan, Zhengfei Wang   +8 more
wiley   +1 more source

RIPK3 Facilitates Host Resistance to Oral Toxoplasma gondii Infection

Infection and Immunity, 2021
Toxoplasma gondiiinfection activates pattern recognition receptor (PRR) pathways that drive innate inflammatory responses to control infection. Necroptosis is a proinflammatory cell death pathway apart from the innate immune response that has evolved to control pathogenic infection.
Patrick W. Cervantes, Bruno Martorelli Di Genova, Billy Joel Erazo Flores, Laura J. Knoll   +3 more
openaire   +3 more sources

Kinase-independent function of RIP1, critical for mature T-cell survival and proliferation. [PDF]

, 2016
The death receptor, Fas, triggers apoptotic death and is essential for maintaining homeostasis in the peripheral lymphoid organs. RIP1 was originally cloned when searching for Fas-binding proteins and was later shown to associate also with the signaling ...
Bertin, John, Cai, Yubo, Dowling, John P., Gough, Peter J., Zhang, Jianke   +4 more
core   +2 more sources