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Endoplasmic Reticulum

Name
Endoplasmic Reticulum
Namespace Keyword
MeSHAnatomy
Namespace
MeSH
Namespace Version
20170511
Namespace URL
https://arty.scai.fraunhofer.de/artifactory/bel/annotation/mesh-anatomy/mesh-anatomy-20170511.belanno

Sample Annotated Edges 5

bp(GO:"response to unfolded protein") increases bp(GO:"response to endoplasmic reticulum stress") View Subject | View Object

The UPR is a mechanism that involves a stress response in the ER, including increased biosynthesis of ER chaperones, in response to accumulation of misfolded/denatured/mutated proteins in this organelle (for a recent review on UPR, see Kaufman, 2002). PubMed:14556719

Appears in Networks:
Annotations
MeSH
Endoplasmic Reticulum

bp(GO:"response to unfolded protein") increases a(MESH:"Molecular Chaperones") View Subject | View Object

The UPR is a mechanism that involves a stress response in the ER, including increased biosynthesis of ER chaperones, in response to accumulation of misfolded/denatured/mutated proteins in this organelle (for a recent review on UPR, see Kaufman, 2002). PubMed:14556719

Appears in Networks:
Annotations
MeSH
Endoplasmic Reticulum

composite(p(HGNC:PRKN), p(HGNC:UBE2G1), p(HGNC:UBE2J1)) increases deg(p(HGNC:GPR37)) View Subject | View Object

Parkin ubiquitinates and promotes the degradation of the insoluble Pael receptor, acting in this reaction along Ubc6 and Ubc7, two E2s located in the ER PubMed:14556719

Appears in Networks:
Annotations
MeSH
Endoplasmic Reticulum

p(MESH:Proteins, pmod(HBP:misfolding)) increases bp(GO:"response to unfolded protein") View Subject | View Object

The UPR is a mechanism that involves a stress response in the ER, including increased biosynthesis of ER chaperones, in response to accumulation of misfolded/denatured/mutated proteins in this organelle (for a recent review on UPR, see Kaufman, 2002). PubMed:14556719

Appears in Networks:
Annotations
MeSH
Endoplasmic Reticulum

p(MESH:Proteins, var("?")) increases bp(GO:"response to unfolded protein") View Subject | View Object

The UPR is a mechanism that involves a stress response in the ER, including increased biosynthesis of ER chaperones, in response to accumulation of misfolded/denatured/mutated proteins in this organelle (for a recent review on UPR, see Kaufman, 2002). PubMed:14556719

Appears in Networks:
Annotations
MeSH
Endoplasmic Reticulum

Showing 5 of 15 edges

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.