Results 21 to 30 of about 3,736 (194)
The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically
Biological Chemistry, 2002 Cdc37 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.
T. Abbas-Terki +7 more
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Utilizing Multi-omics analysis to elucidate the role of mitochondrial gene defects in Gastric cancer progression. [PDF]
PLoS ONEBackgroundGastric cancer is a leading cause of cancer-related mortality worldwide, with poor survival outcomes despite advances in diagnostic and therapeutic methods.
Jie Chu +6 more
doaj +2 more sources
Hematology, 2023 Objective Cell division cycle 37 (CDC37) modulates disease progression and bortezomib resistance in multiple myeloma by regulating X-box binding protein 1, nuclear factor-kappa-B, etc.
Wuqiang Lin +3 more
doaj +1 more source
Biomolecules, 2022 The kinome specific co-chaperone, CDC37 (cell division cycle 37), is responsible for delivering BRAF (B-Rapidly Accelerated Fibrosarcoma) to the Hsp90 (heat shock protein 90) complex, where it is then translocated to the RAS (protooncogene product p21 ...
Dennis M. Bjorklund +5 more
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A client‐binding site of Cdc37 [PDF]
The FEBS Journal, 2005 The molecular chaperone Hsp90 is distinct from Hsp70 and chaperonin in that client proteins are apparently restricted to a subset of proteins categorized as cellular signaling molecules. Among these, many specific protein kinases require the assistance of Hsp90 and its co‐chaperone Cdc37/p50 for their biogenesis.
Kazuya, Terasawa, Yasufumi, Minami
openaire +4 more sources
Hsp90 provides a platform for kinase dephosphorylation by PP5
Nature Communications, 2023 The Hsp90 molecular chaperone collaborates with the phosphorylated Cdc37 cochaperone for the folding and activation of its many client kinases. As with many kinases, the Hsp90 client kinase CRaf is activated by phosphorylation at specific regulatory ...
Maru Jaime-Garza +5 more
doaj +1 more source
Organization of the Chick CDC37 Gene [PDF]
Journal of Biological Chemistry, 1998 CDC37 and the chaperone protein, Hsp90, form a complex that binds to several kinases, resulting in stabilization and promotion of their activity. CDC37 also binds DNA and glycosaminoglycans in a sequence-specific manner. In this study, we further characterize chick CDC37 and examine the organization of the CDC37 gene.
L, Huang, N, Grammatikakis, B P, Toole
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Structural insight into guanylyl cyclase receptor hijacking of the kinase–Hsp90 regulatory mechanism
eLife, 2023 Membrane receptor guanylyl cyclases play a role in many important facets of human physiology, from regulating blood pressure to intestinal fluid secretion.
Nathanael A Caveney +2 more
doaj +1 more source
The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy
, 2021 The cell division cycle protein 37 (Cdc37) and the 90-kDa heat shock protein (Hsp90) are molecular chaperones, which are crucial elements in the protein signaling pathway. The largest class of client proteins for Cdc37 and Hsp90 are protein kinases.
Schwalbe, Harald +5 more
core +2 more sources
Journal of Pharmaceutical Analysis, 2023 Ginsenoside Rg5 is a rare ginsenoside showing promising tumor-suppressive effects. This study aimed to explore its radio-sensitizing effects and the underlying mechanisms. Human lung adenocarcinoma cell lines A549 and Calu-3 were used for in vitro and in
Hansong Bai +8 more
doaj +1 more source