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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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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.