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bp(GO:"protein folding")

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Entity

Name
protein folding
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 6

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

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

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

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

Molecular chaperones and proteostasis regulation during redox imbalance v1.0.0

In-Edges 13

complex(p(HGNC:HSPA5), p(HGNC:PRNP)) increases bp(GO:"protein folding") View Subject | View Object

The Prion protein normally interacts with the chaperone BiP and undergoes assisted folding (Jin et al., 2000). PubMed:14556719

Appears in Networks:

p(FPLX:HSP90) increases bp(GO:"protein folding") View Subject | View Object

Knockdown of daf-21 (HSP90) or hsp-1 (HSC70) led to increased paralysis in 45% and 44% of day 6 animals, respectively, and knockdown of TPR co-chaper- ones tpr-1 and dnj-12 resulted in 70% impairment (Figure S4D). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:DNAJA1) increases bp(GO:"protein folding") View Subject | View Object

Knockdown of daf-21 (HSP90) or hsp-1 (HSC70) led to increased paralysis in 45% and 44% of day 6 animals, respectively, and knockdown of TPR co-chaper- ones tpr-1 and dnj-12 resulted in 70% impairment (Figure S4D). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:HSPA8) increases bp(GO:"protein folding") View Subject | View Object

Knockdown of daf-21 (HSP90) or hsp-1 (HSC70) led to increased paralysis in 45% and 44% of day 6 animals, respectively, and knockdown of TPR co-chaper- ones tpr-1 and dnj-12 resulted in 70% impairment (Figure S4D). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:TTC1) increases bp(GO:"protein folding") View Subject | View Object

Knockdown of daf-21 (HSP90) or hsp-1 (HSC70) led to increased paralysis in 45% and 44% of day 6 animals, respectively, and knockdown of TPR co-chaper- ones tpr-1 and dnj-12 resulted in 70% impairment (Figure S4D). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

bp(HBP:Proteostasis) association bp(GO:"protein folding") View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

p(FPLX:HSPA) regulates bp(GO:"protein folding") View Subject | View Object

As such, HSP70 and HSP90 are central to the process of triaging proteins for refolding or elimination. PubMed:25784053

Appears in Networks:

p(FPLX:HSP90) regulates bp(GO:"protein folding") View Subject | View Object

As such, HSP70 and HSP90 are central to the process of triaging proteins for refolding or elimination. PubMed:25784053

Appears in Networks:

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:

bp(MESH:Aging) decreases bp(GO:"protein folding") View Subject | View Object

Not only does aging lead to an increased likelihood of protein misfolding and aggregation, it is compounded by a decrease in the efficiency of the protein degradation machinery. PubMed:29311797

Appears in Networks:

act(p(FPLX:HSP90)) increases bp(GO:"protein folding") View Subject | View Object

Hsp90 requires ATP to perform these functions including protein degradation, protein folding, prevention of protein aggregation, and protein modification (Echeverría et al., 2011). PubMed:29311797

Appears in Networks:

act(p(FPLX:HSP90)) increases bp(GO:"protein folding") View Subject | View Object

After hydrolysis the Hsp90 N termini separate, releasing the client protein in an active state (Figure 7b). PubMed:23746257

Appears in Networks:

p(FPLX:HSPA) increases bp(GO:"protein folding") View Subject | View Object

HSP70 chaperones have a diverse array of cellular functions but their major role is to ensure correct folding of newly synthesized proteins and to perform the refolding of proteins that are misfolded and/or aggregated. PubMed:24563850

Appears in Networks:

Out-Edges 2

bp(GO:"protein folding") association bp(HBP:Proteostasis) View Subject | View Object

Proteome fidelity is maintained by the protein homeostasis (proteostasis) network (PN), a multi-compartmental system that coordinatesprotein synthesis, folding, disaggregation, and degradation (1). PubMed:25784053

Appears in Networks:

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

Appears in Networks:

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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.