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bp(GO:"protein catabolic process")

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Entity

Name
protein catabolic process
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 5

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Perilous journey: a tour of the ubiquitin–proteasome system v1.0.0

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection v1.0.0

In-Edges 14

a(MESH:Denervation) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

Appears in Networks:
Annotations
MeSH
Muscle, Skeletal

path(MESH:Acidosis) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

Appears in Networks:
Annotations
MeSH
Muscle, Skeletal

path(MESH:Cachexia) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

Appears in Networks:
Annotations
MeSH
Muscle, Skeletal

path(MESH:Sepsis) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

Appears in Networks:
Annotations
MeSH
Muscle, Skeletal

complex(a(GO:"proteasome complex"), p(HGNC:UCHL5)) increases bp(GO:"protein catabolic process") View Subject | View Object

It was initially believed that the presence of DUBs at the proteasome (such as Uch37/UchL5 and Usp14) would promote the degradation of proteins through facilitating substrate processing (see also the next section) PubMed:24457024

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complex(a(GO:"proteasome complex"), p(HGNC:USP14)) increases bp(GO:"protein catabolic process") View Subject | View Object

It was initially believed that the presence of DUBs at the proteasome (such as Uch37/UchL5 and Usp14) would promote the degradation of proteins through facilitating substrate processing (see also the next section) PubMed:24457024

Appears in Networks:

complex(a(GO:"proteasome complex"), p(HGNC:USP14)) decreases bp(GO:"protein catabolic process") View Subject | View Object

However, recent studies have shown that, by contrast, upon chemical inhibition of the proteasome-bound DUB Usp14, the degradation of aggregation-prone substrates in mammalian tissue culture cells significantly increased [65] PubMed:24457024

Appears in Networks:

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

Alternatively, either Hsp70 or Hsp90 can recruit the ubiquitin E3 ligase, C-terminal Hsp70 interacting protein (CHIP), to degrade the bound substrate [104] PubMed:21882945

Appears in Networks:

p(FPLX:HSP90) increases bp(GO:"protein catabolic process") View Subject | View Object

Although both Hsp70 and Hsp90 can promote degradation of client proteins, it has recently been shown that, functionally, the Hsp70 complex often dominates triage decisions [85,107,109] PubMed:21882945

Appears in Networks:

p(INTERPRO:"Heat shock protein 70 family") increases bp(GO:"protein catabolic process") View Subject | View Object

Although both Hsp70 and Hsp90 can promote degradation of client proteins, it has recently been shown that, functionally, the Hsp70 complex often dominates triage decisions [85,107,109] PubMed:21882945

Appears in Networks:

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

The PN branch of degradation includes the ubiquitin- proteasome system (UPS) and machinery of autophagy (23, 196–200). PubMed:23746257

Appears in Networks:

act(p(FPLX:HSPA)) association bp(GO:"protein catabolic process") View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

p(FPLX:Proteasome) increases bp(GO:"protein catabolic process") View Subject | View Object

The PN branch of degradation includes the ubiquitin- proteasome system (UPS) and machinery of autophagy (23, 196–200). PubMed:23746257

Appears in Networks:

bp(GO:"autophagosome-lysosome fusion") increases bp(GO:"protein catabolic process") View Subject | View Object

Once formed, new autophagosomes move through a stepwise maturation process that culminates with fusion to a lysosome permitting degradation of the lumenal contents. PubMed:18930136

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Out-Edges 2

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

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

Appears in Networks:
Annotations
MeSH
Muscle, Skeletal

bp(GO:"protein catabolic process") association act(p(FPLX:HSPA)) View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

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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.