Results 31 to 40 of about 3,509 (196)
Journal of Extracellular Vesicles, 2020 Evidence has been accumulating to indicate that extracellular vesicles (EVs), including exosomes, released by cancer cells can foster tumour progression.
Kisho Ono +16 more
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Elaiophylin Is a Potent Hsp90/ Cdc37 Protein Interface Inhibitor with K-Ras Nanocluster Selectivity
Biomolecules, 2021 The natural product elaiophylin is a macrodiolide with a broad range of biological activities. However, no direct target of elaiophylin in eukaryotes has been described so far, which hinders a systematic explanation of its astonishing activity range.
Farid A. Siddiqui +3 more
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Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Journal of Hematology & Oncology, 2018 Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins.
Ting Li +3 more
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Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains. [PDF]
PLoS ONE, 2017 A fundamental role of the Hsp90 and Cdc37 chaperones in mediating conformational development and activation of diverse protein kinase clients is essential in signal transduction. There has been increasing evidence that the Hsp90-Cdc37 system executes its
Josh Czemeres +2 more
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Pharmaceuticals, 2013 A fundamental role of the Hsp90-Cdc37 chaperone system in mediating maturation of protein kinase clients and supporting kinase functional activity is essential for the integrity and viability of signaling pathways involved in cell cycle control and ...
Gennady Verkhivker +3 more
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Cells, 2020 Tumor cells exhibit therapeutic stress resistance-associated secretory phenotype involving extracellular vesicles (EVs) such as oncosomes and heat shock proteins (HSPs). Such a secretory phenotype occurs in response to cell stress and cancer therapeutics.
Takanori Eguchi +8 more
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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 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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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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