Cargando…
Structural Basis for the Inhibition of HSP70 and DnaK Chaperones by Small-Molecule Targeting of a C-Terminal Allosteric Pocket
[Image: see text] The stress-inducible mammalian heat shock protein 70 (HSP70) and its bacterial orthologue DnaK are highly conserved nucleotide binding molecular chaperones. They represent critical regulators of cellular proteostasis, especially during conditions of enhanced stress. Cancer cells re...
Autores principales: | Leu, Julia I-Ju, Zhang, Pingfeng, Murphy, Maureen E., Marmorstein, Ronen, George, Donna L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4241170/ https://www.ncbi.nlm.nih.gov/pubmed/25148104 http://dx.doi.org/10.1021/cb500236y |
Ejemplares similares
-
Crystal Structure of the Stress-Inducible Human Heat Shock Protein 70 Substrate-Binding Domain in Complex with Peptide Substrate
por: Zhang, Pingfeng, et al.
Publicado: (2014) -
Pathways of allosteric regulation in Hsp70 chaperones
por: Kityk, Roman, et al.
Publicado: (2015) -
Development of Fluorescence Polarization Assays for the Molecular Chaperone Hsp70 Family Members: Hsp72 and DnaK
por: Ricci, Laura, et al.
Publicado: (2008) -
Theory of Allosteric Regulation in Hsp70 Molecular Chaperones
por: Hendrickson, Wayne A.
Publicado: (2020) -
Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism
por: Anglès, Fréderic, et al.
Publicado: (2017)