Results 21 to 30 of about 6,022 (190)
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
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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
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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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
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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
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Computational and Structural Biotechnology Journal, 2023 Heat shock protein 90 (Hsp90) and cell division cycle 37 (Cdc37) work together as a molecular chaperone complex to regulate the activity of a multitude of client protein kinases.
Surya Sukumaran +7 more
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Protein kinase CK2 is widely expressed in follicular, Burkitt and diffuse large B-cell lymphomas and propels malignant B-cell growth. [PDF]
, 2015 Serine-threonine kinase CK2 is highly expressed and pivotal for survival and proliferation in multiple myeloma, chronic lymphocytic leukemia and mantle cell lymphoma.
Agostinelli, C +9 more
core +1 more source
HECTD3 mediates an HSP90-dependent degradation pathway for protein kinase clients [PDF]
, 2017 Inhibition of the ATPase cycle of the HSP90 chaperone promotes ubiquitylation and proteasomal degradation of its client proteins, which include many oncogenic protein kinases.
Li, Zhaobo +4 more
core +6 more sources
Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System
Cell Reports, 2017 Summary: Selective recruitment of protein kinases to the Hsp90 system is mediated by the adaptor co-chaperone Cdc37. We show that assembly of CDK4 and CDK6 into protein complexes is differentially regulated by the Cdc37-Hsp90 system.
Stephen T. Hallett +10 more
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