Correction for Huang et al., "p17-Modulated Hsp90/Cdc37 Complex Governs Oncolytic Avian Reovirus Replication by Chaperoning p17, Which Promotes Viral Protein Synthesis and Accumulation of Viral Proteins σC and σA in Viral Factories". [PDF]
Huang W +5 more
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Regulation of RAF family kinases: new insights from recent structural and biochemical studies. [PDF]
Spencer-Smith R, Morrison DK.
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Predictive value of CDC37 gene expression for targeted therapy in metastatic colorectal cancer. [PDF]
Arai H +31 more
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Prodrug-inspired adenosine triphosphate-activatable celastrol-Fe(III) chelate for cancer therapy. [PDF]
Li H +15 more
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Genetic, Transcriptomic, and Epigenomic Insights into Sjögren's Disease: An Integrative Network Investigation and Immune Diseases Comparison. [PDF]
Enduru N, Manuel AM, Zhao Z.
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Protective effect of CK2 against endoplasmic reticulum stress in pancreatic β cells. [PDF]
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More than Just Protein Folding: The Epichaperome, Mastermind of the Cancer Cell. [PDF]
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Targeting Hsp90-Cdc37 protein-protein interaction (PPI) is becoming an alternative approach for future anti-cancer drug development. We previously reported the discovery of an eleven-residue peptide (Pep-1) with micromolar activity for the disruption of Hsp90-Cdc37 PPI.
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Computational investigation of interactions between Cdc37 and celastrol
Molecular Simulation, 2013Celastrol is a novel inhibitor of the human protein complex Hsp90–Cdc37. It was found that the N-terminal domain of Cdc37 (Cdc37_N) was the molecular target for celastrol binding through covalent bonding. To get insight into the binding mode of celastrol in the active site of Cdc37, herein, the homology models of Cdc37_N and N-terminal/middle domain of
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