Results 61 to 70 of about 6,074 (204)

A primate specific extra domain in the molecular chaperone Hsp90. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Hsp90 S-nitrosylation at Cys521, as a conformational switch, modulates cycling of Hsp90-AHA1-CDC37 chaperone machine to aggravate atherosclerosis

open access: yesRedox 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
doaj   +1 more source

Regulation of CDK4 [PDF]

open access: yes, 2006
Cyclin-dependent kinase (CDK)4 is a master integrator that couples mitogenic and antimitogenic extracellular signals with the cell cycle. It is also crucial for many oncogenic transformation processes.
Laurence Bockstaele   +4 more
core   +2 more sources

Cdc37 Promotes the Stability of Protein Kinases Cdc28 and Cak1 [PDF]

open access: yesMolecular and Cellular Biology, 2000
In the budding yeast Saccharomyces cerevisiae, Cdc37 is required for the productive formation of Cdc28-cyclin complexes. The cdc37-1 mutant arrests at Start with low levels of Cdc28 protein, which is predominantly unphosphorylated at Thr169, fails to bind cyclin, and has little protein kinase activity.
A, Farrell, D O, Morgan
openaire   +2 more sources

Mechanisms of resistance to Hsp90 inhibitor drugs: a complex mosaic emerges [PDF]

open access: yes, 2011
The molecular chaperone Hsp90 holds great promise as a cancer drug target, despite some of the initial clinical trials of Hsp90 inhibitor drugs having not lived up to expectation.
Akerfelt   +116 more
core   +2 more sources

Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B

open access: yesScientific Reports, 2022
The HSP90/CDC37 chaperone system not only assists the maturation of many protein kinases but also maintains their structural integrity after folding.
Marco Papenfuss   +6 more
doaj   +1 more source

Down-regulation of the Lamin A/C in neuroblastoma triggers the expansion of tumor initiating cells [PDF]

open access: yes, 2015
Tumor-initiating cells constitute a population within a tumor mass that shares properties with normal stem cells and is considered responsible for therapy failure in many cancers.
AMENDOLA, Donatella   +20 more
core   +4 more sources

Identification of co-chaperone Cdc37 in Penaeus monodon: coordination with Hsp90 can reduce cadmium stress-induced lipid peroxidation

open access: yesEcotoxicology and Environmental Safety, 2021
Cell division cycle 37 (Cdc37) is an important cytoplasmic phosphoprotein, which usually functions as a complex with heat shock protein 90 (Hsp90), to effectively reduce the damage caused by heavy metals, such as cadmium (Cd), in aquatic animals.
Chao Zhao   +5 more
doaj   +1 more source

Mutation of the Ser18 phosphorylation site on the sole Saccharomyces cerevisiae UCS protein, She4, can compromise high-temperature survival. [PDF]

open access: yes, 2016
Folding of the myosin head often requires the joint actions of Hsp90 and a dedicated UNC45, Cro1, She4 (UCS) domain-containing cochaperone protein. Relatively weak sequence conservation exists between the single UCS protein of simple eukaryotes (She4 in ...
Gomez-Escalante, S.   +2 more
core   +1 more source

Screening the Active Phytochemicals From Eclipta prostrata and Unraveling Their Molecular Insight Into Human Malignancies

open access: yesCancer Innovation, Volume 4, Issue 6, December 2025.
This review comprehensively analyses the phytochemicals from Eclipta prostrata, identifying 25 active compounds with chemotherapeutic potential against 15 different human malignancies. These compounds modulate diverse and complex mechanisms, including targeting critical signaling pathways (e.g., PI3K/AKT/mTOR), inducing regulated cell death (e.g., FAS,
Md. Sakhawat Hossain   +13 more
wiley   +1 more source

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