 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
|
| MeSH Number(s) |
D12.776.580.216.292
|
| 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 Protein 40
- Heat Shock Protein 40
- HSP40 Proteins
- DnaJ Proteins
- HSP40 Protein Family
- Heat-Shock Proteins 40
- Heat Shock Proteins 40
|
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 |
|---|
| 1997 | 0 | 1 | 1 | | 2002 | 0 | 1 | 1 | | 2005 | 0 | 1 | 1 | | 2006 | 0 | 3 | 3 | | 2007 | 0 | 1 | 1 | | 2008 | 1 | 0 | 1 | | 2010 | 1 | 0 | 1 | | 2015 | 1 | 0 | 1 | | 2017 | 1 | 0 | 1 | | 2018 | 2 | 0 | 2 | | 2019 | 0 | 1 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "HSP40 Heat-Shock Proteins" by people in Profiles.
-
Barbier-Torres L, Fortner KA, Iruzubieta P, Delgado TC, Giddings E, Chen Y, Champagne D, Fernández-Ramos D, Mestre D, Gomez-Santos B, Varela-Rey M, de Juan VG, Fernández-Tussy P, Zubiete-Franco I, García-Monzón C, González-Rodríguez Á, Oza D, Valença-Pereira F, Fang Q, Crespo J, Aspichueta P, Tremblay F, Christensen BC, Anguita J, Martínez-Chantar ML, Rincón M. Silencing hepatic MCJ attenuates non-alcoholic fatty liver disease (NAFLD) by increasing mitochondrial fatty acid oxidation. Nat Commun. 2020 07 03; 11(1):3360.
-
Moreno DF, Parisi E, Yahya G, Vaggi F, Csikász-Nagy A, Aldea M. Competition in the chaperone-client network subordinates cell-cycle entry to growth and stress. Life Sci Alliance. 2019 04; 2(2).
-
Kim JS, Liu L, Fitzsimmons LF, Wang Y, Crawford MA, Mastrogiovanni M, Trujillo M, Till JKA, Radi R, Dai S, Vázquez-Torres A. DksA-DnaJ redox interactions provide a signal for the activation of bacterial RNA polymerase. Proc Natl Acad Sci U S A. 2018 12 11; 115(50):E11780-E11789.
-
Cornec-Le Gall E, Olson RJ, Besse W, Heyer CM, Gainullin VG, Smith JM, Audrézet MP, Hopp K, Porath B, Shi B, Baheti S, Senum SR, Arroyo J, Madsen CD, Férec C, Joly D, Jouret F, Fikri-Benbrahim O, Charasse C, Coulibaly JM, Yu AS, Khalili K, Pei Y, Somlo S, Le Meur Y, Torres VE, Harris PC. Monoallelic Mutations to DNAJB11 Cause Atypical Autosomal-Dominant Polycystic Kidney Disease. Am J Hum Genet. 2018 05 03; 102(5):832-844.
-
Saarikangas J, Caudron F, Prasad R, Moreno DF, Bolognesi A, Aldea M, Barral Y. Compartmentalization of ER-Bound Chaperone Confines Protein Deposit Formation to the Aging Yeast Cell. Curr Biol. 2017 Mar 20; 27(6):773-783.
-
Johnson CR, Weems AD, Brewer JM, Thorner J, McMurray MA. Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast. Mol Biol Cell. 2015 Apr 01; 26(7):1323-44.
-
Majtan T, Liu L, Carpenter JF, Kraus JP. Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes. J Biol Chem. 2010 May 21; 285(21):15866-73.
-
Dong M, Bridges JP, Apsley K, Xu Y, Weaver TE. ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol Biol Cell. 2008 Jun; 19(6):2620-30.
-
Chow LQ, Eckhardt SG, O'Bryant CL, Schultz MK, Morrow M, Grolnic S, Basche M, Gore L. A phase I safety, pharmacological, and biological study of the farnesyl protein transferase inhibitor, lonafarnib (SCH 663366), in combination with cisplatin and gemcitabine in patients with advanced solid tumors. Cancer Chemother Pharmacol. 2008 Sep; 62(4):631-46.
-
Gore L, Holden SN, Cohen RB, Morrow M, Pierson AS, O'Bryant CL, Persky M, Gustafson D, Mikule C, Zhang S, Palmer PA, Eckhardt SG. A phase I safety, pharmacological and biological study of the farnesyl protein transferase inhibitor, tipifarnib and capecitabine in advanced solid tumors. Ann Oncol. 2006 Nov; 17(11):1709-17.
|
People  People who have written about this concept. _
Similar Concepts
People who have written about this concept.
_
Top Journals
Top journals in which articles about this concept have been published.
|