Cargando…
The Hsp70–Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration
The Hsp70 and Hsp90 molecular chaperone systems are critical regulators of protein homeostasis (proteostasis) in eukaryotes under normal and stressed conditions. The Hsp70 and Hsp90 systems physically and functionally interact to ensure cellular proteostasis. Co-chaperones interact with Hsp70 and Hs...
Autores principales: | Bhattacharya, Kaushik, Picard, Didier |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8629791/ https://www.ncbi.nlm.nih.gov/pubmed/34677645 http://dx.doi.org/10.1007/s00018-021-03962-z |
Ejemplares similares
-
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
por: Bhattacharya, Kaushik, et al.
Publicado: (2020) -
Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules
por: Röhl, Alina, et al.
Publicado: (2015) -
Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)
por: Gitau, Grace W., et al.
Publicado: (2011) -
Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes
por: Bhattacharya, Kaushik, et al.
Publicado: (2018) -
Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer
por: Ruckova, Eva, et al.
Publicado: (2012)