Cargando…
Heat shock-induced chaperoning by Hsp70 is enabled in-cell
Recent work has shown that weak protein-protein interactions are susceptible to the cellular milieu. One case in point is the binding of heat shock proteins (Hsps) to substrate proteins in cells under stress. Upregulation of the Hsp70 chaperone machinery at elevated temperature was discovered in the...
Autores principales: | Guin, Drishti, Gelman, Hannah, Wang, Yuhan, Gruebele, Martin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6762143/ https://www.ncbi.nlm.nih.gov/pubmed/31557226 http://dx.doi.org/10.1371/journal.pone.0222990 |
Ejemplares similares
-
Heat Shock Protein 70 (HSP70) induces cytotoxicity of T-helper cells
por: Figueiredo, C, et al.
Publicado: (2009) -
Chaperone-Based Therapeutic Target Innovation: Heat Shock Protein 70 (HSP70) for Type 2 Diabetes Mellitus
por: Mulyani, W. Riski Widya, et al.
Publicado: (2020) -
Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins
por: Jores, Tobias, et al.
Publicado: (2018) -
Investigating the Chaperone Properties of a Novel Heat Shock Protein, Hsp70.c, from Trypanosoma brucei
por: Burger, Adélle, et al.
Publicado: (2014) -
Biogenesis of the mitochondrial Hsp70 chaperone
por: Blamowska, Marta, et al.
Publicado: (2012)