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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Molecular Chaperones [D12.776.580]
Heat-Shock Proteins [D12.776.580.216]
HSP70 Heat-Shock Proteins [D12.776.580.216.375]

Below are MeSH descriptors whose meaning is related to "HSP70 Heat-Shock Proteins".

Below are MeSH descriptors whose meaning is more specific than "HSP70 Heat-Shock Proteins".

publications

Timeline | Most Recent

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.

Bar chart showing 43 publications over 19 distinct years, with a maximum of 6 publications in 2003

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
2000	1	0	1
2001	1	1	2
2002	2	2	4
2003	2	4	6
2004	1	1	2
2005	0	1	1
2006	1	1	2
2007	1	0	1
2009	2	1	3
2010	0	1	1
2011	1	1	2
2012	1	1	2
2013	0	1	1
2014	1	3	4
2015	3	1	4
2018	0	3	3
2021	0	1	1
2023	0	2	2
2024	1	0	1

Below are the most recent publications written about "HSP70 Heat-Shock Proteins" by people in Profiles.

Benedetti F, Silvestri G, Denaro F, Finesso G, Contreras-Galindo R, Munawwar A, Williams S, Davis H, Bryant J, Wang Y, Radaelli E, Rathinam CV, Gallo RC, Zella D. Mycoplasma DnaK expression increases cancer development in vivo upon DNA damage. Proc Natl Acad Sci U S A. 2024 Mar 05; 121(10):e2320859121.

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Alimardan Z, Abbasi M, Hasanzadeh F, Aghaei M, Khodarahmi G, Kashfi K. Heat shock proteins and cancer: The FoxM1 connection. Biochem Pharmacol. 2023 05; 211:115505.

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van Oosten-Hawle P, Backe SJ, Ben-Zvi A, Bourboulia D, Brancaccio M, Brodsky J, Clark M, Colombo G, Cox MB, De Los Rios P, Echtenkamp F, Edkins A, Freeman B, Goloubinoff P, Houry W, Johnson J, LaPointe P, Li W, Mezger V, Neckers L, Nillegoda NB, Prahlad V, Reitzel A, Scherz-Shouval R, Sistonen L, Tsai FTF, Woodford MR, Mollapour M, Truman AW. Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8-9, 2022. Cell Stress Chaperones. 2023 01; 28(1):1-9.

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Peng Z, Bedi S, Mann V, Sundaresan A, Homma K, Gaskey G, Kowada M, Umar S, Kulkarni AD, Eltzschig HK, Doursout MF. Neuroprotective Effects of Asparagus officinalis Stem Extract in Transgenic Mice Overexpressing Amyloid Precursor Protein. J Immunol Res. 2021; 2021:8121407.

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Zella D, Curreli S, Benedetti F, Krishnan S, Cocchi F, Latinovic OS, Denaro F, Romerio F, Djavani M, Charurat ME, Bryant JL, Tettelin H, Gallo RC. Mycoplasma promotes malignant transformation in vivo, and its DnaK, a bacterial chaperone protein, has broad oncogenic properties. Proc Natl Acad Sci U S A. 2018 12 18; 115(51):E12005-E12014.

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Oyagbemi AA, Omobowale TO, Ola-Davies OE, Asenuga ER, Ajibade TO, Adejumobi OA, Arojojoye OA, Afolabi JM, Ogunpolu BS, Falayi OO, Hassan FO, Ochigbo GO, Saba AB, Adedapo AA, Yakubu MA. Quercetin attenuates hypertension induced by sodium fluoride via reduction in oxidative stress and modulation of HSP 70/ERK/PPAR? signaling pathways. Biofactors. 2018 Sep; 44(5):465-479.

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Xiong L, Yan W, Zubia E, Zhou Y, Zhang Y, Duan Q, Narayan M, Xu G. Quantitative proteomics and biochemical analyses reveal the role of endoplasmin in the regulation of the expression and secretion of A Disintegrin And Metalloproteinase 12. J Proteomics. 2018 06 30; 182:34-44.

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Sane S, Abdullah A, Nelson ME, Wang H, Chauhan SC, Newton SS, Rezvani K. Structural studies of UBXN2A and mortalin interaction and the putative role of silenced UBXN2A in preventing response to chemotherapy. Cell Stress Chaperones. 2016 Mar; 21(2):313-26.

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Patra M, Roy SS, Dasgupta R, Basu T. GroEL to DnaK chaperone network behind the stability modulation of s(32) at physiological temperature in Escherichia coli. FEBS Lett. 2015 Dec 21; 589(24 Pt B):4047-52.

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Singha UK, Hamilton V, Chaudhuri M. Tim62, a Novel Mitochondrial Protein in Trypanosoma brucei, Is Essential for Assembly and Stability of the TbTim17 Protein Complex. J Biol Chem. 2015 Sep 18; 290(38):23226-39.

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