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.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 1 | 2 |
| 1999 | 1 | 0 | 1 |
| 2000 | 2 | 0 | 2 |
| 2001 | 1 | 1 | 2 |
| 2002 | 1 | 1 | 2 |
| 2003 | 1 | 1 | 2 |
| 2004 | 0 | 1 | 1 |
| 2005 | 2 | 0 | 2 |
| 2006 | 2 | 1 | 3 |
| 2007 | 2 | 0 | 2 |
| 2008 | 1 | 1 | 2 |
| 2010 | 3 | 1 | 4 |
| 2011 | 2 | 0 | 2 |
| 2012 | 1 | 0 | 1 |
| 2013 | 0 | 1 | 1 |
| 2014 | 2 | 0 | 2 |
| 2015 | 2 | 2 | 4 |
| 2016 | 0 | 1 | 1 |
| 2017 | 3 | 0 | 3 |
| 2018 | 2 | 1 | 3 |
| 2019 | 1 | 2 | 3 |
| 2021 | 2 | 0 | 2 |
| 2022 | 1 | 1 | 2 |
| 2023 | 1 | 0 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "HSP70 Heat-Shock Proteins" by people in Profiles.
-
Rossi MA, Pozhidaeva AK, Clerico EM, Petridis C, Gierasch LM. New insights into the structure and function of the complex?between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE. J Biol Chem. 2024 Jan; 300(1):105574.
-
Nordquist EB, Clerico EM, Chen J, Gierasch LM. Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future. J Phys Chem B. 2022 09 15; 126(36):6780-6791.
-
Clerico EM, Gierasch LM. There are more Hsp90 chaperone mechanisms in heaven and earth, dear reader, than are dreamt of in your philosophy. Mol Cell. 2022 04 21; 82(8):1403-1404.
-
Nordquist EB, English CA, Clerico EM, Sherman W, Gierasch LM, Chen J. Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones. PLoS Comput Biol. 2021 11; 17(11):e1009567.
-
Clerico EM, Pozhidaeva AK, Jansen RM, ?zden C, Tilitsky JM, Gierasch LM. Selective promiscuity in the binding of E. coli Hsp70 to an unfolded protein. Proc Natl Acad Sci U S A. 2021 10 12; 118(41).
-
Wu Y, Wang Y, Liu Q, Zhu LJ, Gao H, Cui M, Liu J, Zhao P, Liu J, Chen L, Wang J, Zeng W, Woodruff TK, Zeng S. Conserved microRNA mediates heating tolerance in germ cells versus surrounding somatic cells. RNA Biol. 2019 10; 16(10):1494-1503.
-
Cherepanova NA, Venev SV, Leszyk JD, Shaffer SA, Gilmore R. Quantitative glycoproteomics reveals new classes of STT3A- and STT3B-dependent N-glycosylation sites. J Cell Biol. 2019 08 05; 218(8):2782-2796.
-
Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. Biochem J. 2019 06 14; 476(11):1653-1677.
-
Mayer MP, Gierasch LM. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. J Biol Chem. 2019 02 08; 294(6):2085-2097.
-
Meng W, Clerico EM, McArthur N, Gierasch LM. Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proc Natl Acad Sci U S A. 2018 11 20; 115(47):11970-11975.