HSP70 Heat-Shock Proteins
"HSP70 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 found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.
Descriptor ID |
D018840
|
MeSH Number(s) |
D12.776.580.216.375
|
Concept/Terms |
HSP70 Heat-Shock Proteins- HSP70 Heat-Shock Proteins
- HSP70 Heat Shock Proteins
- Heat-Shock Proteins, HSP70
- Heat-Shock Protein 70
- Heat Shock Protein 70
- Heat-Shock Proteins 70
- Heat Shock Proteins 70
- Heat Shock 70 kDa Protein
|
Below are MeSH descriptors whose meaning is more general than "HSP70 Heat-Shock Proteins".
Below are MeSH descriptors whose meaning is more specific than "HSP70 Heat-Shock Proteins".
This graph shows the total number of publications written about "HSP70 Heat-Shock Proteins" by people in this website by year, and whether "HSP70 Heat-Shock Proteins" was a major or minor topic of these publications.
View timeline visualization
Year | Major Topic | Minor Topic | Total |
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1995 | 8 | 8 | 16 |
1996 | 17 | 6 | 23 |
1997 | 7 | 4 | 11 |
1998 | 9 | 8 | 17 |
1999 | 5 | 4 | 9 |
2000 | 12 | 6 | 18 |
2001 | 7 | 5 | 12 |
2002 | 10 | 7 | 17 |
2003 | 12 | 7 | 19 |
2004 | 17 | 13 | 30 |
2005 | 9 | 10 | 19 |
2006 | 15 | 11 | 26 |
2007 | 10 | 6 | 16 |
2008 | 9 | 3 | 12 |
2009 | 9 | 8 | 17 |
2010 | 14 | 8 | 22 |
2011 | 8 | 9 | 17 |
2012 | 12 | 6 | 18 |
2013 | 11 | 6 | 17 |
2014 | 12 | 6 | 18 |
2015 | 11 | 6 | 17 |
2016 | 15 | 4 | 19 |
2017 | 7 | 1 | 8 |
2018 | 14 | 3 | 17 |
2019 | 6 | 5 | 11 |
2020 | 10 | 2 | 12 |
2021 | 6 | 6 | 12 |
2022 | 4 | 5 | 9 |
2023 | 1 | 5 | 6 |
2024 | 3 | 7 | 10 |
Below are the most recent publications written about "HSP70 Heat-Shock Proteins" by people in Profiles.
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Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70. Nat Commun. 2024 Dec 30; 15(1):10815.
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Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins. Trends Biochem Sci. 2025 Feb; 50(2):121-133.
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Design principles to tailor Hsp104 therapeutics. Cell Rep. 2024 Dec 24; 43(12):115005.
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EGFR-mediated HSP70 phosphorylation facilitates PCNA association with chromatin and DNA replication. Nucleic Acids Res. 2024 Nov 27; 52(21):13057-13072.
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O-GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co-chaperone. Protein Sci. 2024 Oct; 33(10):e5173.
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Proteostasis perturbation of N-Myc leveraging HSP70 mediated protein turnover improves treatment of neuroendocrine prostate cancer. Nat Commun. 2024 Aug 05; 15(1):6626.
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Exploration of the binding determinants of protein phosphatase 5 (PP5) reveals a chaperone-independent activation mechanism. J Biol Chem. 2024 Jul; 300(7):107435.
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Challenges for heat stress: Intestinal culturable bacteria of Lohmann Brown chickens. Res Vet Sci. 2024 Jun; 172:105258.
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Plasmodium falciparum heat shock proteins as antimalarial drug targets: An update. Cell Stress Chaperones. 2024 Apr; 29(2):326-337.
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Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell survival and resistance to drug-induced apoptosis in fibrolamellar carcinoma. Cell Rep. 2024 02 27; 43(2):113678.