Results 21 to 30 of about 6,074 (204)
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
doaj +1 more source
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
openaire +2 more sources
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
Structure of an Hsp90-Cdc37-Cdk4 Complex [PDF]
Molecular Cell, 2006 Activation of many protein kinases depends on their interaction with the Hsp90 molecular chaperone system. Recruitment of protein kinase clients to the Hsp90 chaperone system is mediated by the cochaperone adaptor protein Cdc37, which acts as a scaffold, simultaneously binding protein kinases and Hsp90. We have now expressed and purified an Hsp90-Cdc37-
Vaughan, C +8 more
openaire +4 more sources
Physical Interaction of Mammalian CDC37 with CDK4 [PDF]
Journal of Biological Chemistry, 1996 CDC37 was originally identified as a Start gene in budding yeast and has been shown to be required for association of CDC28 with cyclins. The exact functional mechanism by which CDC37 promotes this association, however, remains unknown. CDK4 is a cyclin D-dependent kinase that controls progression through G1 of the mammalian cell cycle.
K, Dai, R, Kobayashi, D, Beach
openaire +2 more sources
Hsp90 modulates human sperm capacitation via the Erk1/2 and p38 MAPK signaling pathways
Reproductive Biology and Endocrinology, 2021 Background Heat shock protein 90 (Hsp90) is a highly abundant eukaryotic molecular chaperone that plays important roles in client protein maturation, protein folding and degradation, and signal transduction.
Peibei Sun +6 more
doaj +1 more source
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