Results 41 to 50 of about 3,509 (196)
Role of p50/CDC37 in Hepadnavirus Assembly and Replication [PDF]
Journal of Biological Chemistry, 2002 The cellular chaperone Hsp90 has been shown to associate with the reverse transcriptase (RT) of the duck hepatitis B virus and is required for RT functions. However, the molecular basis for the specific interaction between the RT and Hsp90 remains unknown.
Xingtai, Wang +2 more
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Assembly mechanism of early Hsp90-Cdc37-kinase complexes
Science Advances, 2022 Molecular chaperones have an essential role for the maintenance of a balanced protein homeostasis. Here, we investigate how protein kinases are recruited and loaded to the Hsp90-Cdc37 complex, the first step during Hsp90-mediated chaperoning that leads to enhanced client kinase stability and activation.
Dimitra Keramisanou +4 more
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Gene-expression changes in cerium chloride-induced injury of mouse hippocampus. [PDF]
PLoS ONE, 2013 Cerium is widely used in many aspects of modern society, including agriculture, industry and medicine. It has been demonstrated to enter the ecological environment, is then transferred to humans through food chains, and causes toxic actions in several ...
Zhe Cheng +15 more
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Cdc37 as a Co-chaperone to Hsp90 [PDF]
, 2014 The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. The Hsp90/Cdc37complex controls the folding of a large proportion of protein kinases and thus stands at the hub of a multitude of intracellular signaling networks.
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The Human Cdc37·Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy
, 2009 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.
Sreeramulu, S. +11 more
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Bio-Protocol, 2017 Interactions between Hsp90, its co-chaperone Cdc37 and kinases have been biochemically studied for over three decades and have been shown to be functionally important in organisms from yeast to humans.
Kliment Verba, David Agard
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A primate specific extra domain in the molecular chaperone Hsp90. [PDF]
PLoS 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
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Redox 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
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Cdc37 Promotes the Stability of Protein Kinases Cdc28 and Cak1 [PDF]
Molecular 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
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, 2018 The sup. Excel file for the comprehensive analysis of Hsp90-Cdc37’s client proteins. Comprehensive Analysis of Hsp90-Cdc37’s client proteins by using FunRich tool.
Ting Li (117885) +3 more
core +1 more source