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Domain-Mediated Dimerization of the Hsp90 Cochaperones Harc and Cdc37
Biochemistry, 2005Hsp90 is a highly conserved molecular chaperone that acts in concert with Hsp70 and a cohort of cochaperones to mediate the folding of client proteins into functional conformations. The novel Hsp90 cochaperone Harc was identified previously on the basis of its amino acid sequence similarity to Cdc37.
John, Roiniotis +3 more
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Interaction of Rat Cdc37-Related Protein with Retinoblastoma Gene Product
DNA and Cell Biology, 1996By using in vitro binding assays and the yeast two-hybrid system, we have found that a full-length rat Cdc37-related protein (RCdc37) could associate specifically with the retinoblastoma susceptibility gene product (pRB). A series of GST-RCdc37 deletion mutants was constructed to define the amino acid sequence required for the interaction with pRB.
T, Ozaki, S, Sakiyama
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The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically
Biological Chemistry, 2002Cdc37 associates with the heat-shock protein 90 (Hsp90) molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. Cdc37 has been proposed to be a specificity factor for Hsp90, directing it notably towards kinases.
Abbas-Terki, Toufik +3 more
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Role of Cdc37 in Protein Kinase Folding
2007As nascent chains emerge from the ribosome, they interact with molecular chaperone proteins that prevent aggregation and promote protein folding. Chaperones such as Hsp70 and Hsp40 function together to protect nascent chains while still ribosome bound, and function with little if any specificity for the unfolded polypeptide.
Atin K. Mandal +2 more
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A role for Cdc37 in EGFRvIII biogenesis
2013The mutant epidermal growth factor receptor, EGFRvIII, is associated with tumour aggressiveness and drug resistance in glioblastoma. Our lab has shown that the molecular chaperone Hsp90 interacts with nascent EGFRvIII, and that EGFRvIII expression and function is dependent upon Hsp90 activity.
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Allosteric CDC37 Inhibitor Disrupts Chaperone Complex to Block CDK4/6 Maturation
Angewandte Chemie International EditionAbstractCell division cycle 37 (CDC37) is a member of the molecular chaperone family and acts as a cochaperone of heat shock protein 90 (HSP90), which is overexpressed in many cancer types as a regulator of protein kinase maturation. In this process, CDC37 selectively recognizes and stabilizes protein kinases by forming a HSP90‐CDC37‐kinase chaperone ...
Lixiao Zhang +14 more
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