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

Appears in Networks 4

In-Edges 10

a(MESH:Lysosomes) increases bp(MESH:Proteolysis) View Subject | View Object

. Proteins can be degraded either individually or en masse by proteasomes (20) or lysosomes (21), respectively. PubMed:25784053

bp(HBP:Proteostasis) association bp(MESH:Proteolysis) 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(MESH:Proteolysis) 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(MESH:Proteolysis) 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:Proteasome) increases bp(MESH:Proteolysis) View Subject | View Object

. Proteins can be degraded either individually or en masse by proteasomes (20) or lysosomes (21), respectively. PubMed:25784053

path(MESH:"Alzheimer Disease") decreases bp(MESH:Proteolysis) View Subject | View Object

All three proteolytic activities have been reported to be decreased in AD brains (Keller et al., 2000). PubMed:23528736

p(MGI:Tfeb) increases bp(MESH:Proteolysis) View Subject | View Object

Flow cytometry analysis of primary astrocytes incubated with DQ-BSA revealed an ∼60% increase in median fluorescence for TFEB-transduced astro- cytes, indicating that TFEB enhances uptake and proteolysis of DQ-BSA PubMed:30108137

a(MESH:"Molecular Chaperones") association bp(MESH:Proteolysis) 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(MESH:Proteolysis) 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(MESH:Proteolysis) 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

Out-Edges 2

bp(MESH:Proteolysis) 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(MESH:Proteolysis) 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.