Publication: Rhinovirus 3C protease suppresses apoptosis and triggers caspase-independent cell death
Rhinovirus 3C protease suppresses apoptosis and triggers caspase-independent cell death
Date
Date
Date
Citations
Lötzerich, M., Roulin, P. S., Boucke, K., Witte, R., Georgiev, O., & Greber, U. F. (2018). Rhinovirus 3C protease suppresses apoptosis and triggers caspase-independent cell death. Cell Death and Disease, 9, 272. https://doi.org/10.1038/s41419-018-0306-6
Abstract
Abstract
Abstract
Apoptosis and programmed necrosis (necroptosis) determine cell fate, and antagonize infection. Execution of these complementary death pathways involves the formation of receptor-interacting protein kinase 1 (RIPK1) containing complexes. RIPK1 binds to adaptor proteins, such as TRIF (Toll-IL-1 receptor-domain-containing-adaptor-inducing interferon-beta factor), FADD (Fas-associated-protein with death domain), NEMO (NF-κB regulatory subunit IKKγ), SQSTM1 (sequestosome 1/p62), or RIPK3 (receptor-interacting protein kinase 3), which are i
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Creators (Authors)
- Lötzerich, Mark
- Roulin, Pascal S
- Boucke, Karin
- Witte, Robert
- Georgiev, Oleg
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Citations
Lötzerich, M., Roulin, P. S., Boucke, K., Witte, R., Georgiev, O., & Greber, U. F. (2018). Rhinovirus 3C protease suppresses apoptosis and triggers caspase-independent cell death. Cell Death and Disease, 9, 272. https://doi.org/10.1038/s41419-018-0306-6
