Results 41 to 50 of about 3,736 (194)
HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
Scientific Reports, 2021 Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation.
Siyuan Sima +7 more
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Characterization of Celastrol to Inhibit Hsp90 and Cdc37 Interaction [PDF]
Journal of Biological Chemistry, 2009 The molecular chaperone heat shock protein 90 (Hsp90) is required for the stabilization and conformational maturation of various oncogenic proteins in cancer. The loading of protein kinases to Hsp90 is actively mediated by the cochaperone Cdc37. The crucial role of the Hsp90-Cdc37 complex has made it an exciting target for cancer treatment.
Tao, Zhang +5 more
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Cdc37 as a Co-chaperone to Hsp90 [PDF]
, 2014 The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. The Hsp90/Cdc37complex controls the folding of a large proportion of protein kinases and thus stands at the hub of a multitude of intracellular signaling networks.
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Interaction between Cdc37 and Cdk4 in human cells [PDF]
Oncogene, 1997 Using the yeast two-hybrid system we have identified novel potential Cdk4 interacting proteins. Here we described the interaction of Cdk4 with a human homologue of the yeast Drosophila CDC37 gene products. Cdc37 protein specifically interacts with Cdk4 and Cdk6, but not with Cdc2, Cdk2, Cdk3, Cdk5 and any of a number of cyclins tested.
L, Lamphere +7 more
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Role of p50/CDC37 in Hepadnavirus Assembly and Replication [PDF]
Journal of Biological Chemistry, 2002 The cellular chaperone Hsp90 has been shown to associate with the reverse transcriptase (RT) of the duck hepatitis B virus and is required for RT functions. However, the molecular basis for the specific interaction between the RT and Hsp90 remains unknown.
Xingtai, Wang +2 more
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Cdc37 and protein kinase folding
RSC Advances, 2007 Cdc37 is a molecular chaperone that collaborates with Hsp90 to fold protein kinases and other clients including transcription factors. Cdc37 function in protein kinase folding is dependent on direct interaction between the chaperone and the N-lobe of the kinase catalytic domain.
Robert Matts, Avrom J. Caplan
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Gene-expression changes in cerium chloride-induced injury of mouse hippocampus. [PDF]
PLoS ONE, 2013 Cerium is widely used in many aspects of modern society, including agriculture, industry and medicine. It has been demonstrated to enter the ecological environment, is then transferred to humans through food chains, and causes toxic actions in several ...
Zhe Cheng +15 more
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Bio-Protocol, 2017 Interactions between Hsp90, its co-chaperone Cdc37 and kinases have been biochemically studied for over three decades and have been shown to be functionally important in organisms from yeast to humans.
Kliment Verba, David Agard
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A primate specific extra domain in the molecular chaperone Hsp90. [PDF]
PLoS ONE, 2013 Hsp90 (heat shock protein 90) is an essential molecular chaperone that mediates folding and quality control of client proteins. Many of them such as protein kinases, steroid receptors and transcription factors are involved in cellular signaling processes.
Vishwadeepak Tripathi +1 more
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Redox Biology, 2022 Endothelial dysfunction is the initial process of atherosclerosis. Heat shock protein 90 (Hsp90), as a molecular chaperone, plays a crucial role in various cardiovascular diseases. Hsp90 function is regulated by S-nitrosylation (SNO).
Shuang Zhao +20 more
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