1. Catalog
  2. Nodes
  3. bp(GO:"protein quality control for misfolded or incompletely synthesized proteins")

bp(GO:"protein quality control for misfolded or incompletely synthesized proteins")

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

Entity

Name
protein quality control for misfolded or incompletely synthesized proteins
Namespace
go
Namespace Version
20190207
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/a5b84013a08880975ca84f40999e4404b14a97e2/external/go-names.belns

Appears in Networks 2

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

In-Edges 5

p(HGNC:LTN1) association bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") View Subject | View Object

BAG1 interacted with the E3 ubiquitin ligase Listerin (LTN1), which is involved in ribosomal quality control (RQC) of stalled polypeptides (Bengtson and Joazeiro, 2010). PubMed:25036637

Appears in Networks:

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

Appears in Networks:

p(HGNC:HSPB1) increases bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") View Subject | View Object

During protein quality control, Hsp70, Hsp90 and Hsp27 (and their co-chaperones) often work in concert. If prolonged misfolding is detected, the chaperones shuttle the protein to a degradation endpoint, such as the proteasome or autophagy PubMed:21882945

Appears in Networks:

p(FPLX:HSP90) increases bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") View Subject | View Object

During protein quality control, Hsp70, Hsp90 and Hsp27 (and their co-chaperones) often work in concert. If prolonged misfolding is detected, the chaperones shuttle the protein to a degradation endpoint, such as the proteasome or autophagy PubMed:21882945

Appears in Networks:

p(INTERPRO:"Heat shock protein 70 family") increases bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") View Subject | View Object

During protein quality control, Hsp70, Hsp90 and Hsp27 (and their co-chaperones) often work in concert. If prolonged misfolding is detected, the chaperones shuttle the protein to a degradation endpoint, such as the proteasome or autophagy PubMed:21882945

Appears in Networks:

Out-Edges 2

bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") association p(HGNC:LTN1) View Subject | View Object

BAG1 interacted with the E3 ubiquitin ligase Listerin (LTN1), which is involved in ribosomal quality control (RQC) of stalled polypeptides (Bengtson and Joazeiro, 2010). PubMed:25036637

Appears in Networks:

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

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.