Cargando…
Misfolded proteins bind and activate death receptor 5 to trigger apoptosis during unresolved endoplasmic reticulum stress
Disruption of protein folding in the endoplasmic reticulum (ER) activates the unfolded protein response (UPR)—a signaling network that ultimately determines cell fate. Initially, UPR signaling aims at cytoprotection and restoration of ER homeostasis; that failing, it drives apoptotic cell death. ER...
Autores principales: | Lam, Mable, Marsters, Scot A, Ashkenazi, Avi, Walter, Peter |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7041945/ https://www.ncbi.nlm.nih.gov/pubmed/31904339 http://dx.doi.org/10.7554/eLife.52291 |
Ejemplares similares
-
Confirming a critical role for death receptor 5 and caspase-8 in apoptosis induction by endoplasmic reticulum stress
por: Lam, Mable, et al.
Publicado: (2018) -
MET Suppresses Epithelial VEGFR2 via Intracrine VEGF-induced Endoplasmic Reticulum-associated Degradation
por: Chen, Tom T., et al.
Publicado: (2015) -
Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes
por: Preissler, Steffen, et al.
Publicado: (2020) -
Pharmacologic ATF6 activating compounds are metabolically activated to selectively modify endoplasmic reticulum proteins
por: Paxman, Ryan, et al.
Publicado: (2018) -
Caspase-mediated cleavage of IRE1 controls apoptotic cell commitment during endoplasmic reticulum stress
por: Shemorry, Anna, et al.
Publicado: (2019)