Cargando…
p53-mediated suppression of BiP triggers BIK-induced apoptosis during prolonged endoplasmic reticulum stress
Physiological and pathological conditions that affect the folding capacity of the endoplasmic reticulum (ER) provoke ER stress and trigger the unfolded protein response (UPR). The UPR aims to either restore the balance between newly synthesized and misfolded proteins or if the damage is severe, to t...
Autores principales: | López, Ignacio, Tournillon, Anne-Sophie, Prado Martins, Rodrigo, Karakostis, Konstantinos, Malbert-Colas, Laurence, Nylander, Karin, Fåhraeus, Robin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5596431/ https://www.ncbi.nlm.nih.gov/pubmed/28622297 http://dx.doi.org/10.1038/cdd.2017.96 |
Ejemplares similares
-
p53-mediated control of gene expression via mRNA translation during Endoplasmic Reticulum stress
por: López, Ignacio, et al.
Publicado: (2015) -
BiP Clustering Facilitates Protein Folding in the Endoplasmic Reticulum
por: Griesemer, Marc, et al.
Publicado: (2014) -
Inadequate BiP availability defines endoplasmic reticulum stress
por: Vitale, Milena, et al.
Publicado: (2019) -
MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP
por: Yan, Yahui, et al.
Publicado: (2019) -
Stress-induced protein disaggregation in the endoplasmic reticulum catalysed by BiP
por: Melo, Eduardo Pinho, et al.
Publicado: (2022)