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Entity

Name
cellular protein catabolic process
Namespace
go
Namespace Version
20190207
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/a5b84013a08880975ca84f40999e4404b14a97e2/external/go-names.belns

Appears in Networks 5

In-Edges 12

p(HGNC:STUB1) regulates bp(GO:"cellular protein catabolic process") View Subject | View Object

CHIP binds Hsp90 and Hsp70 with similar affinities and can regulate the degradation of chaperone clients (Kundrat and Regan, 2010). PubMed:25036637

p(HGNC:DCP1A) association bp(GO:"cellular protein catabolic process") View Subject | View Object

These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007) PubMed:25036637

p(HGNC:DDX6) association bp(GO:"cellular protein catabolic process") View Subject | View Object

These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007) PubMed:25036637

p(HGNC:EDC3) association bp(GO:"cellular protein catabolic process") View Subject | View Object

These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007) PubMed:25036637

composite(a(HP:"Argyrophilic inclusion bodies"), p(MGI:Mapt)) negativeCorrelation bp(GO:"cellular protein catabolic process") View Subject | View Object

Surprisingly, the axonal grains of Tau appear to resist protein degradation because they are negative for markers of degradation (vimentin, ubiquitin, Lamp1, Sqstm1/P62, Hsc70, and Tia-1) (Fig. S5) PubMed:27671637

bp(GO:"proteasome-mediated ubiquitin-dependent protein catabolic process") increases bp(GO:"cellular protein catabolic process") View Subject | View Object

UPS-mediated catabolism is also essential to mainten amino acid pools in acute starvation and contributes significantly to the degradation of defective proteins [1,2,7]. PubMed:18930136

bp(GO:autophagy) increases bp(GO:"cellular protein catabolic process") View Subject | View Object

Autophagy, by contrast, is primarily responsible for degrading long-lived proteins and maintaining amino acid pools in the setting of chronic starvation, although its contribution to the degradation of defective proteins may equal that of the UPS. PubMed:18930136

path(HBP:Neurodegeneration) negativeCorrelation bp(GO:"cellular protein catabolic process") View Subject | View Object

Considering the importance of protein catabolism in maintaining cell homeostasis, it is not surprising that dysregulation of protein turnover is associated with myriad disease states such as cancer and neurodegeneration [5]. PubMed:18930136

path(MESH:Neoplasms) negativeCorrelation bp(GO:"cellular protein catabolic process") View Subject | View Object

Considering the importance of protein catabolism in maintaining cell homeostasis, it is not surprising that dysregulation of protein turnover is associated with myriad disease states such as cancer and neurodegeneration [5]. PubMed:18930136

a(CHEBI:"advanced glycation end-product") increases bp(GO:"cellular protein catabolic process") View Subject | View Object

AGEs induce tau hyperphosphorylation, memory deterioration, decline of synaptic proteins, and impairment of long-term potentiation in rats [10]. PubMed:27288790

Out-Edges 7

bp(GO:"cellular protein catabolic process") association p(HGNC:DCP1A) View Subject | View Object

These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007) PubMed:25036637

bp(GO:"cellular protein catabolic process") association p(HGNC:EDC3) View Subject | View Object

These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007) PubMed:25036637

bp(GO:"cellular protein catabolic process") association p(HGNC:DDX6) View Subject | View Object

These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007) PubMed:25036637

bp(GO:"cellular protein catabolic process") negativeCorrelation composite(a(HP:"Argyrophilic inclusion bodies"), p(MGI:Mapt)) View Subject | View Object

Surprisingly, the axonal grains of Tau appear to resist protein degradation because they are negative for markers of degradation (vimentin, ubiquitin, Lamp1, Sqstm1/P62, Hsc70, and Tia-1) (Fig. S5) PubMed:27671637

bp(GO:"cellular protein catabolic process") regulates bp(GO:"cellular homeostasis") View Subject | View Object

Considering the importance of protein catabolism in maintaining cell homeostasis, it is not surprising that dysregulation of protein turnover is associated with myriad disease states such as cancer and neurodegeneration [5]. PubMed:18930136

bp(GO:"cellular protein catabolic process") negativeCorrelation path(MESH:Neoplasms) View Subject | View Object

Considering the importance of protein catabolism in maintaining cell homeostasis, it is not surprising that dysregulation of protein turnover is associated with myriad disease states such as cancer and neurodegeneration [5]. PubMed:18930136

bp(GO:"cellular protein catabolic process") negativeCorrelation path(HBP:Neurodegeneration) View Subject | View Object

Considering the importance of protein catabolism in maintaining cell homeostasis, it is not surprising that dysregulation of protein turnover is associated with myriad disease states such as cancer and neurodegeneration [5]. PubMed:18930136

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.