Equivalencies: 0 | Classes: 0 | Children: 6 | Explore

Entity

Name
Molecular Chaperones
Namespace
MeSH
Namespace Version
20181007
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/01c9daa61012b37dd0a1bc962521ba51a15b38f1/external/mesh-names.belns

Appears in Networks 7

In-Edges 14

bp(GO:"response to unfolded protein") increases a(MESH:"Molecular Chaperones") View Subject | View Object

The UPR is a mechanism that involves a stress response in the ER, including increased biosynthesis of ER chaperones, in response to accumulation of misfolded/denatured/mutated proteins in this organelle (for a recent review on UPR, see Kaufman, 2002). PubMed:14556719

act(p(HGNC:HSF1), ma(tscript)) increases a(MESH:"Molecular Chaperones") View Subject | View Object

Upon increased levels of nonnative proteins, HSF1 is released from its repressive complex, acquires DNA-binding activity through homotrimerization, and rapidly translocates to the nucleus to induce expression of genes encoding molecular chaperones (7, 35). PubMed:25784053

bp(GO:"protein folding") association a(MESH:"Molecular Chaperones") View Subject | View Object

All of these chaperones assist in various ways to help fold, refold and degrade misfolded proteins. PubMed:29311797

bp(MESH:Proteolysis) association a(MESH:"Molecular Chaperones") View Subject | View Object

All of these chaperones assist in various ways to help fold, refold and degrade misfolded proteins. PubMed:29311797

p(HGNC:HSF1) increases a(MESH:"Molecular Chaperones") View Subject | View Object

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257

Out-Edges 6

a(MESH:"Molecular Chaperones") decreases path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

As discussed above, one approach is to employ specialized molecular chaperone machines to release misfolded proteins from aggregates and direct them to the proteasome for degradation (19). PubMed:25784053

a(MESH:"Molecular Chaperones") association bp(GO:"protein folding") View Subject | View Object

All of these chaperones assist in various ways to help fold, refold and degrade misfolded proteins. PubMed:29311797

a(MESH:"Molecular Chaperones") association bp(MESH:Proteolysis) View Subject | View Object

All of these chaperones assist in various ways to help fold, refold and degrade misfolded proteins. PubMed:29311797

a(MESH:"Molecular Chaperones") decreases path(HBP:proteotoxicity) View Subject | View Object

Genetic approaches using these disease models demonstrate that the chaperome plays a crucial role in protecting cells from proteotoxicity. PubMed:27491084

a(MESH:"Molecular Chaperones") decreases a(MESH:"Protein Aggregates") View Subject | View Object

A key role of molecular chaperones is preventing pro- tein aggregation, especially under conditions of cellular stress. PubMed:23746257

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.