Cargando…
BiP Availability Distinguishes States of Homeostasis and Stress in the Endoplasmic Reticulum of Living Cells
Accumulation of misfolded secretory proteins causes cellular stress and induces the endoplasmic reticulum (ER) stress pathway, the unfolded protein response (UPR). Although the UPR has been extensively studied, little is known about the molecular changes that distinguish the homeostatic and stressed...
Autores principales: | Lai, Chun Wei, Aronson, Deborah E., Snapp, Erik Lee |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883936/ https://www.ncbi.nlm.nih.gov/pubmed/20410136 http://dx.doi.org/10.1091/mbc.E09-12-1066 |
Ejemplares similares
-
Inadequate BiP availability defines endoplasmic reticulum stress
por: Vitale, Milena, et al.
Publicado: (2019) -
Stress-induced protein disaggregation in the endoplasmic reticulum catalysed by BiP
por: Melo, Eduardo Pinho, et al.
Publicado: (2022) -
BiP Clustering Facilitates Protein Folding in the Endoplasmic Reticulum
por: Griesemer, Marc, et al.
Publicado: (2014) -
GPNMB Induces BiP Expression by Enhancing Splicing of BiP Pre-mRNA during the Endoplasmic Reticulum Stress Response
por: Noda, Yasuhiro, et al.
Publicado: (2017) -
MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP
por: Yan, Yahui, et al.
Publicado: (2019)