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p(HGNC:HSPD1)

Equivalencies: 0 | Classes: 1 | Children: 0 | Explore

Entity

Name
HSPD1
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 4

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. v1.0.0

The Biology of Proteostasis in Aging and Disease 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 7

a(CHEBI:ATP) association act(p(HGNC:HSPD1)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

bp(MESH:Aging) decreases p(HGNC:HSPD1) View Subject | View Object

Ranked by decreasing median aging correlation, the induction of sHSPs and TPR genes consistently ranked high and the HSP60s, HSP40s, and HSP70s were consistently repressed. PubMed:25437566

Appears in Networks:

bp(MESH:"Energy Metabolism") association p(HGNC:HSPD1) View Subject | View Object

HSP60 is essential for maturation and maintenance of the mitochondrial proteome and is therefore intimately linked to energy production. PubMed:25784053

Appears in Networks:
Annotations
MeSH
Mitochondria

bp(HBP:Proteostasis) association p(HGNC:HSPD1) View Subject | View Object

Many studies based on model systems support a role for candidates from each of the major chaperome families; HSP100, HSP90, HSP70, HSP60, HSP40, sHSPs, and TPR-domain-containing proteins in proteostasis. PubMed:27491084

Appears in Networks:

bp(MESH:Aging) decreases p(HGNC:HSPD1) View Subject | View Object

The HSP40, HSP60 and HSP70 families were amongst the most repressed chaperones, with HSP70s being the most repressed group overall. However, in contrast with the broad spectrum of repressed chaperone families, sHSPs and the TPR co-chaperone proteins were the only families that were significantly induced. PubMed:27491084

Appears in Networks:

complex(a(CHEBI:ATP), p(HGNC:HSPD1)) hasComponent p(HGNC:HSPD1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:HSPD1), p(HGNC:HSPE1)) hasComponent p(HGNC:HSPD1) View Subject | View Object

Appears in Networks:

Out-Edges 6

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

Appears in Networks:

act(p(HGNC:HSPD1)) association a(CHEBI:ATP) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

p(HGNC:HSPD1) increases bp(HBP:Proteostasis) View Subject | View Object

HSP60 is essential for maturation and maintenance of the mitochondrial proteome and is therefore intimately linked to energy production. PubMed:25784053

Appears in Networks:
Annotations
MeSH
Mitochondria

p(HGNC:HSPD1) association bp(MESH:"Energy Metabolism") View Subject | View Object

HSP60 is essential for maturation and maintenance of the mitochondrial proteome and is therefore intimately linked to energy production. PubMed:25784053

Appears in Networks:
Annotations
MeSH
Mitochondria

p(HGNC:HSPD1) association bp(HBP:Proteostasis) View Subject | View Object

Many studies based on model systems support a role for candidates from each of the major chaperome families; HSP100, HSP90, HSP70, HSP60, HSP40, sHSPs, and TPR-domain-containing proteins in proteostasis. PubMed:27491084

Appears in Networks:

p(HGNC:HSPD1) decreases a(MESH:"Protein Aggregates") View Subject | View Object

Binding to GroEL prevents aggregation of these flexible folding intermediates, and subsequent folding depends critically on the global encapsulation of the substrate in the chaperonin cavity by the cochaperone GroES (7, 132–135). PubMed:23746257

Appears in Networks:

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.