Cargando…
Multivalent protein–protein interactions are pivotal regulators of eukaryotic Hsp70 complexes
Heat shock protein 70 (Hsp70) is a molecular chaperone and central regulator of protein homeostasis (proteostasis). Paramount to this role is Hsp70’s binding to client proteins and co-chaperones to produce distinct complexes, such that understanding the protein–protein interactions (PPIs) of Hsp70 i...
Autores principales: | Johnson, Oleta T., Gestwicki, Jason E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9346034/ https://www.ncbi.nlm.nih.gov/pubmed/35670950 http://dx.doi.org/10.1007/s12192-022-01281-1 |
Ejemplares similares
-
Analogs of the Heat Shock Protein 70 Inhibitor MKT-077 Suppress Medullary Thyroid Carcinoma Cells
por: Hong, Seung-Keun, et al.
Publicado: (2022) -
Two distinct classes of cochaperones compete for the EEVD motif in heat shock protein 70 to tune its chaperone activities
por: Johnson, Oleta T., et al.
Publicado: (2022) -
An Unbiased Screen Identified the Hsp70-BAG3 Complex as a Regulator of Myosin-Binding Protein C3
por: Thompson, Andrea D., et al.
Publicado: (2023) -
Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
por: Ben-Khoud, Yassin, et al.
Publicado: (2023) -
Allosteric inhibition of HSP70 in collaboration with STUB1 augments enzalutamide efficacy in antiandrogen resistant prostate tumor and patient-derived models
por: Xu, Pengfei, et al.
Publicado: (2023)