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p(HGNC:HSPA1A)

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

Entity

Name
HSPA1A
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 5

The Biology of Proteostasis in Aging and Disease v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease v1.0.0

Tau oligomers and tau toxicity in neurodegenerative disease by Ward et al., 2012

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

Molecular chaperones and proteostasis regulation during redox imbalance v1.0.0

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 6

path(MESH:"Protein Aggregation, Pathological") negativeCorrelation p(HGNC:HSPA1A) View Subject | View Object

Studies of chaperone levels in tissue culture and mouse models of polyQ disease showed that the levels of HSP70 (HSPA1A/B) and DNAJ/HSP40 (DNAJB1), as well as some cochaperones, decline with protein aggregation (64, 65). PubMed:25784053

Appears in Networks:

complex(a(HBP:"Tau oligomers"), p(HGNC:HSPA1A)) hasComponent p(HGNC:HSPA1A) View Subject | View Object

Appears in Networks:

composite(p(HGNC:HSPA1A), p(HGNC:MAPT, frag("2_18"))) hasComponent p(HGNC:HSPA1A) View Subject | View Object

Appears in Networks:

complex(a(CHEBI:ATP), p(HGNC:HSPA1A)) hasComponent p(HGNC:HSPA1A) View Subject | View Object

Appears in Networks:

bp(GO:"cellular response to heat") increases p(HGNC:HSPA1A, loc(MESH:"Extracellular Space")) View Subject | View Object

Moreover, it was shown that the concentration of the extracellular heat shock protein 72 (eHSP72) increases during exercise-heat stress [65]. PubMed:24563850

Appears in Networks:

a(CHEBI:heme) increases p(HGNC:HSPA1A) View Subject | View Object

However, in the presence of 40 μM heme, the toxic response was characterized by the strong induction of heat shock proteins, namely HSP70 (HSPA1B, HSPA4, HSPA5, DNAJB1), HSP72 (HSPA1A), HSP105 (HSPH1), and HSP10 (HSPE1), as well as the proteasome adaptor protein sequestosome. PubMed:26794659

Appears in Networks:
Annotations
Cell Ontology (CL)
epithelial cell
MeSH
Kidney
Text Location
Results

Out-Edges 3

p(HGNC:HSPA1A) negativeCorrelation path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

Studies of chaperone levels in tissue culture and mouse models of polyQ disease showed that the levels of HSP70 (HSPA1A/B) and DNAJ/HSP40 (DNAJB1), as well as some cochaperones, decline with protein aggregation (64, 65). PubMed:25784053

Appears in Networks:

p(HGNC:HSPA1A) decreases a(HBP:"Tau aggregates") View Subject | View Object

Previous findings indicate that Hsp70 prevents tau toxicity by preserving tau in its soluble form and preventing it from aggregating by binding to exposed hydrophobic residues [33] PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

p(HGNC:HSPA1A) increases deg(a(HBP:"Tau aggregates")) View Subject | View Object

It has also been demonstrated that Hsp70 can facilitate the degradation of pre-formed aggregates [33] PubMed:22817713

Appears in Networks:
Annotations
Confidence
High
MeSH
Intracellular Space

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.