HSP90 Heat-Shock Proteins
"HSP90 Heat-Shock Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.
| Descriptor ID |
D018841
|
| MeSH Number(s) |
D12.776.580.216.380
|
| Concept/Terms |
HSP90 Heat-Shock Proteins- HSP90 Heat-Shock Proteins
- HSP90 Heat Shock Proteins
- Heat-Shock Proteins, HSP90
- Heat-Shock Proteins 90
- Heat Shock Proteins 90
|
Below are MeSH descriptors whose meaning is more general than "HSP90 Heat-Shock Proteins".
Below are MeSH descriptors whose meaning is more specific than "HSP90 Heat-Shock Proteins".
This graph shows the total number of publications written about "HSP90 Heat-Shock Proteins" by people in this website by year, and whether "HSP90 Heat-Shock Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2007 | 1 | 0 | 1 |
| 2008 | 1 | 0 | 1 |
| 2011 | 1 | 1 | 2 |
| 2016 | 1 | 0 | 1 |
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Below are the most recent publications written about "HSP90 Heat-Shock Proteins" by people in Profiles.
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NMNAT2:HSP90 Complex Mediates Proteostasis in Proteinopathies. PLoS Biol. 2016 06; 14(6):e1002472.
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A multicenter phase II study of ganetespib monotherapy in patients with genotypically defined advanced non-small cell lung cancer. Clin Cancer Res. 2013 Jun 01; 19(11):3068-77.
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Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell. 2011 Mar 18; 41(6):672-81.
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Anticancer activity of Celastrol in combination with ErbB2-targeted therapeutics for treatment of ErbB2-overexpressing breast cancers. Cancer Biol Ther. 2011 Jan 15; 11(2):263-76.
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Geldanamycin promotes premature mitotic entry and micronucleation in irradiated p53/p21 deficient colon carcinoma cells. Oncogene. 2008 Sep 18; 27(42):5567-77.
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MDM2 binding induces a conformational change in p53 that is opposed by heat-shock protein 90 and precedes p53 proteasomal degradation. J Biol Chem. 2007 May 11; 282(19):14626-34.