 HSP40 Heat-Shock Proteins
"HSP40 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 family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.
| Descriptor ID |
D050956
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| MeSH Number(s) |
D12.776.580.216.292
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| Concept/Terms |
HSP40 Heat-Shock Proteins- HSP40 Heat-Shock Proteins
- HSP40 Heat Shock Proteins
- Heat-Shock Proteins, HSP40
- Proteins, HSP40 Heat-Shock
- Heat Shock Protein 40 Family
- Heat-Shock Proteins 40
- Heat Shock Proteins 40
- DnaJ Proteins
- Heat-Shock Protein 40
- Heat Shock Protein 40
- HSP40 Protein Family
- HSP40 Proteins
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Below are MeSH descriptors whose meaning is more general than "HSP40 Heat-Shock Proteins".
Below are MeSH descriptors whose meaning is more specific than "HSP40 Heat-Shock Proteins".
This graph shows the total number of publications written about "HSP40 Heat-Shock Proteins" by people in this website by year, and whether "HSP40 Heat-Shock Proteins" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1998 | 0 | 1 | 1 | | 2005 | 0 | 1 | 1 | | 2007 | 0 | 1 | 1 | | 2010 | 0 | 1 | 1 | | 2011 | 1 | 0 | 1 | | 2012 | 1 | 1 | 2 | | 2015 | 2 | 1 | 3 | | 2016 | 1 | 1 | 2 | | 2021 | 1 | 0 | 1 | | 2022 | 1 | 0 | 1 |
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Below are the most recent publications written about "HSP40 Heat-Shock Proteins" by people in Profiles.
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Yoo H, Bard JAM, Pilipenko EV, Drummond DA. Chaperones directly and efficiently disperse stress-triggered biomolecular condensates. Mol Cell. 2022 02 17; 82(4):741-755.e11.
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Feder ZA, Ali A, Singh A, Krakowiak J, Zheng X, Bindokas VP, Wolfgeher D, Kron SJ, Pincus D. Subcellular localization of the J-protein Sis1 regulates the heat shock response. J Cell Biol. 2021 01 04; 220(1).
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Yang L, Lee MS, Lu H, Oh DY, Kim YJ, Park D, Park G, Ren X, Bristow CA, Haseley PS, Lee S, Pantazi A, Kucherlapati R, Park WY, Scott KL, Choi YL, Park PJ. Analyzing Somatic Genome Rearrangements in Human Cancers by Using Whole-Exome Sequencing. Am J Hum Genet. 2016 05 05; 98(5):843-856.
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Batra J, Tripathi S, Kumar A, Katz JM, Cox NJ, Lal RB, Sambhara S, Lal SK. Human Heat shock protein 40 (Hsp40/DnaJB1) promotes influenza A virus replication by assisting nuclear import of viral ribonucleoproteins. Sci Rep. 2016 Jan 11; 6:19063.
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Henderson MX, Wirak GS, Zhang YQ, Dai F, Ginsberg SD, Dolzhanskaya N, Staropoli JF, Nijssen PC, Lam TT, Roth AF, Davis NG, Dawson G, Velinov M, Chandra SS. Neuronal ceroid lipofuscinosis with DNAJC5/CSPa mutation has PPT1 pathology and exhibit aberrant protein palmitoylation. Acta Neuropathol. 2016 Apr; 131(4):621-37.
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Brouillette AM, Öz G, Gomez CM. Cerebrospinal Fluid Biomarkers in Spinocerebellar Ataxia: A Pilot Study. Dis Markers. 2015; 2015:413098.
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Tsou WL, Hosking RR, Burr AA, Sutton JR, Ouyang M, Du X, Gomez CM, Todi SV. DnaJ-1 and karyopherin a3 suppress degeneration in a new Drosophila model of Spinocerebellar Ataxia Type 6. Hum Mol Genet. 2015 Aug 01; 24(15):4385-96.
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Birukova AA, Singleton PA, Gawlak G, Tian X, Mirzapoiazova T, Mambetsariev B, Dubrovskyi O, Oskolkova OV, Bochkov VN, Birukov KG. GRP78 is a novel receptor initiating a vascular barrier protective response to oxidized phospholipids. Mol Biol Cell. 2014 Jul 01; 25(13):2006-16.
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Gajewski TF, Salama AK, Niedzwiecki D, Johnson J, Linette G, Bucher C, Blaskovich MA, Sebti SM, Haluska F. Phase II study of the farnesyltransferase inhibitor R115777 in advanced melanoma (CALGB 500104). J Transl Med. 2012 Dec 10; 10:246.
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Jo S, Kalló I, Bardóczi Z, Arrojo e Drigo R, Zeöld A, Liposits Z, Oliva A, Lemmon VP, Bixby JL, Gereben B, Bianco AC. Neuronal hypoxia induces Hsp40-mediated nuclear import of type 3 deiodinase as an adaptive mechanism to reduce cellular metabolism. J Neurosci. 2012 Jun 20; 32(25):8491-500.
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