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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click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 1 | 1 | 2 |
| 1997 | 2 | 0 | 2 |
| 1998 | 1 | 0 | 1 |
| 1999 | 2 | 0 | 2 |
| 2000 | 2 | 1 | 3 |
| 2001 | 3 | 0 | 3 |
| 2002 | 1 | 0 | 1 |
| 2003 | 2 | 0 | 2 |
| 2004 | 2 | 0 | 2 |
| 2005 | 5 | 1 | 6 |
| 2006 | 1 | 0 | 1 |
| 2007 | 2 | 0 | 2 |
| 2008 | 1 | 0 | 1 |
| 2009 | 5 | 0 | 5 |
| 2010 | 4 | 0 | 4 |
| 2011 | 5 | 0 | 5 |
| 2012 | 2 | 2 | 4 |
| 2013 | 2 | 2 | 4 |
| 2014 | 1 | 1 | 2 |
| 2018 | 3 | 1 | 4 |
| 2019 | 0 | 1 | 1 |
| 2021 | 1 | 0 | 1 |
| 2022 | 1 | 1 | 2 |
| 2024 | 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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Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity. PLoS Genet. 2024 Dec; 20(12):e1011338.
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Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications. PLoS Biol. 2022 10; 20(10):e3001839.
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Crystal structure of the middle and C-terminal domains of Hsp90a labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target. Acta Crystallogr D Struct Biol. 2022 May 01; 78(Pt 5):571-585.
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Selective Inhibition of the Hsp90a Isoform. Angew Chem Int Ed Engl. 2021 05 03; 60(19):10547-10551.
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ß-hCG-induced mutant BRCA1 ignites drug resistance in susceptible breast tissue. Carcinogenesis. 2019 Nov 25; 40(11):1415-1426.
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Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding. J Med Chem. 2018 04 12; 61(7):2793-2805.
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Structure-guided design of an Hsp90ß N-terminal isoform-selective inhibitor. Nat Commun. 2018 01 30; 9(1):425.
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A High-Throughput Screen for Inhibitors of the Hsp90-Chaperone Machine. Methods Mol Biol. 2018; 1709:87-96.
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Proteomic Profiling of Hsp90 Inhibitors. Methods Mol Biol. 2018; 1709:139-162.
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Thioredoxin-1 redox signaling regulates cell survival in response to hyperoxia. Free Radic Biol Med. 2014 Oct; 75:167-77.