Hsp90/Cdc37 Chaperone/co-chaperone complex, a novel junction anticancer target elucidated by the mode of action of herbal drug Withaferin A [PDF]
Background HSPs (Heat shock proteins) are highly conserved ubiquitous proteins among species which are involved in maintaining appropriate folding and conformation of other proteins and are thus referred to as molecular chaperones.
Bisaria Virendra S +6 more
doaj +2 more sources
Design of Disruptors of the Hsp90–Cdc37 Interface [PDF]
The molecular chaperone Hsp90 is a ubiquitous ATPase-directed protein responsible for the activation and structural stabilization of a large clientele of proteins.
Ilda D’Annessa +10 more
doaj +5 more sources
Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome [PDF]
Hsp90 is an abundant and essential molecular chaperone that is required for the folding and/or activity of up to 15%-20% of all yeast proteins. Hsp90 and its cochaperone Cdc37 are of interest due to their cooperative role in chaperoning oncogenic protein
Erick I. Rios, Jill L. Johnson
doaj +2 more sources
Tumor‐Derived CDC37 Inhibits Antigen Cross‐Presentation in Dendritic Cells and Impairs Anti‐Tumor Immunity in Breast Cancer [PDF]
Tumor mutational burden (TMB), usually representing high immunogenicity, cannot always predict treatment response of immune checkpoint blockade (ICB).
Ruxin Wang +10 more
doaj +2 more sources
Targeting the oncogene and kinome chaperone CDC37 [PDF]
CDC37 is a molecular chaperone that physically stabilizes the catalytic domains found in protein kinases and is therefore a wide-spectrum regulator of protein phosphorylation. It is also an overexpressed oncoprotein that mediates carcinogenesis by stabilizing the compromised structures of mutant and/or overexpressed oncogenic kinases. Recent work shows
Thomas Prince +2 more
exaly +3 more sources
The oncolytic avian reovirus p17 protein triggers chaperone-mediated autophagy by modulating Hsp90 and the T-complex protein-1 ring complex chaperones and co-chaperones to activate the IKK/NF-κB signaling [PDF]
This study is the first to reveal that oncolytic avian reovirus (ARV) modulates the IKK/NF-κB signaling through the Hsp90-Cdc37, T-complex protein-1 ring complex (TRiC)/Hsc70, and TRiC-phosducin-like protein 1 (PhLP1) chaperone complexes, thereby ...
Wei‐Ru Huang +5 more
doaj +2 more sources
Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System
Summary: Selective recruitment of protein kinases to the Hsp90 system is mediated by the adaptor co-chaperone Cdc37. We show that assembly of CDK4 and CDK6 into protein complexes is differentially regulated by the Cdc37-Hsp90 system.
Martyna W Pastok +2 more
exaly +3 more sources
ERK5 and cell proliferation: nuclear localization is what matters [PDF]
ERK5, the last MAP kinase family member discovered, is activated by the upstream kinase MEK5 in response to growth factors and stress stimulation. MEK5-ERK5 pathway has been associated to different cellular processes, playing a crucial role in cell ...
Nestor Gomez +2 more
doaj +4 more sources
Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia [PDF]
The Cdc37 gene encodes a 50 kDa protein which targets intrinsically unstable oncoprotein kinases such as Cdk4, Raf-1, and src to the molecular chaperone Hsp90. This activity is thought to play an important role in the establishment of signaling pathways controlling cell proliferation.
Thomas M Wheeler +2 more
exaly +3 more sources
Koumine exerts its anti-colorectal cancer effects by disrupting the interaction between HSP90 and CDC37, thereby downregulating downstream signaling pathways [PDF]
BackgroundKoumine, a principal bioactive alkaloid derived from the traditional Chinese herb Gelsemium elegans, has demonstrated broad cytotoxic activity against various cancer cell lines. However, its specific anti-tumor efficacy and underlying molecular
HaiLing Lin +6 more
doaj +2 more sources

