Cargando…
Proteome-wide identification of HSP70/HSC70 chaperone clients in human cells
The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protection from stress-induced misfolding and aggregation of polypeptides in most organisms and are responsible for promoting the stability, folding, and degradation of clients to maintain cellular protein homeostasis....
Autores principales: | Ryu, Seung W., Stewart, Rose, Pectol, D. Chase, Ender, Nicolette A., Wimalarathne, Oshadi, Lee, Ji-Hoon, Zanini, Carlos P., Harvey, Antony, Huibregtse, Jon M., Mueller, Peter, Paull, Tanya T. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7392334/ https://www.ncbi.nlm.nih.gov/pubmed/32687490 http://dx.doi.org/10.1371/journal.pbio.3000606 |
Ejemplares similares
-
Hsp110 Chaperones Control Client Fate Determination in the Hsp70–Hsp90 Chaperone System
por: Mandal, Atin K., et al.
Publicado: (2010) -
Quantitative analysis of the interplay between hsc70 and its co-chaperone HspBP1
por: Mahboubi, Hicham, et al.
Publicado: (2015) -
Hsp70 Architecture: The Formation of Novel Polymeric Structures of Hsp70.1 and Hsc70 after Proteotoxic Stress
por: Steel, Rohan, et al.
Publicado: (2012) -
Exploration of the cysteine reactivity of human inducible Hsp70 and cognate Hsc70
por: Hong, Zhouping, et al.
Publicado: (2022) -
Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications
por: Nitika,, et al.
Publicado: (2022)