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a(MESH:"Molecular Chaperones")

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

The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0

The Biology of Proteostasis in Aging and Disease v1.0.0

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways v1.0.0

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0

Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

In-Edges 14

p(HGNC:HSPD1) isA a(MESH:"Molecular Chaperones") View Subject | View Object

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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

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Annotations
MeSH
Endoplasmic Reticulum

complex(a(MESH:"Molecular Chaperones"), a(MESH:Proteins)) hasComponent a(MESH:"Molecular Chaperones") View Subject | View Object

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complex(a(MESH:"Molecular Chaperones"), p(HGNC:HSF1)) hasComponent a(MESH:"Molecular Chaperones") View Subject | View Object

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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

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p(FPLX:HSPA) isA a(MESH:"Molecular Chaperones") View Subject | View Object

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p(FPLX:HSP90) isA a(MESH:"Molecular Chaperones") View Subject | View Object

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p(FPLX:HSPB) isA a(MESH:"Molecular Chaperones") View Subject | View Object

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p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") isA a(MESH:"Molecular Chaperones") View Subject | View Object

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p(HGNC:PDCL) isA a(MESH:"Molecular Chaperones") View Subject | View Object

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bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") association a(MESH:"Molecular Chaperones") View Subject | View Object

Molecular chaperones are abundant and highly conserved proteins that assume an important role in protein quality control PubMed:21882945

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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

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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

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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

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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

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a(MESH:"Molecular Chaperones") association bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") View Subject | View Object

Molecular chaperones are abundant and highly conserved proteins that assume an important role in protein quality control PubMed:21882945

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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

Appears in Networks:

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

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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

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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

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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.