Cargando…
One domain fits all: Using disordered regions to sequester misfolded proteins
Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to...
Autores principales: | Boczek, Edgar E., Alberti, Simon |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5881514/ https://www.ncbi.nlm.nih.gov/pubmed/29523584 http://dx.doi.org/10.1083/jcb.201803015 |
Ejemplares similares
-
ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
por: Cortés Sanchón, Adrián, et al.
Publicado: (2021) -
An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function
por: Mateju, Daniel, et al.
Publicado: (2017) -
Rapamycin – “One size does not fit all”
por: Kallijärvi, Jukka, et al.
Publicado: (2019) -
Glycemic control in the critically ill - 3 domains and diabetic status means one size does not fit all!
por: Krinsley, James S
Publicado: (2013) -
Obesity and Inflammation: One Size Never Fits All
por: Elks, Carrie M.
Publicado: (2018)