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p(MESH:Proteins, pmod(HBP:misfolding))

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

Entity

Name
Proteins
Namespace
MeSH
Namespace Version
20181007
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/01c9daa61012b37dd0a1bc962521ba51a15b38f1/external/mesh-names.belns

Appears in Networks 5

The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0

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

Alzheimer’s disease and the autophagic-lysosomal system v1.0.0

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

Caenorhabditis elegans models of tauopathy v1.0.0

In-Edges 11

p(HGNC:SEC61A1) increases tloc(p(MESH:Proteins, pmod(HBP:misfolding)), fromLoc(GO:"endoplasmic reticulum lumen"), toLoc(GO:cytosol)) View Subject | View Object

It should be noted that CFTR degradation is mediated by Endoplasmic Reticulum Associated Degradation (ERAD—a quality control mechanism that eliminates, via the UPS, misfolded/mutated/abnormal membrane or lumenal ER proteins following their retrotranslocation to the cytosol via the Sec61 translocation channel). PubMed:14556719

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p(MESH:Proteins) hasVariant p(MESH:Proteins, pmod(HBP:misfolding)) View Subject | View Object

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complex(a(GO:"proteasome complex"), p(HGNC:BAG6)) increases deg(p(MESH:Proteins, pmod(HBP:misfolding))) View Subject | View Object

Because Bag6 interacts with both E3 ligases as well as the proteasome [57,58,60], it may promote both the ubiquitination and delivery of misfolded proteins to the proteasome while preventing their aggregation PubMed:24457024

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complex(a(MESH:Ubiquitin), p(MESH:Proteins, pmod(HBP:misfolding))) hasComponent p(MESH:Proteins, pmod(HBP:misfolding)) View Subject | View Object

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complex(a(MESH:Ubiquitin), p(MESH:Proteins, pmod(HBP:misfolding))) increases deg(p(MESH:Proteins, pmod(HBP:misfolding))) View Subject | View Object

Misfolded proteins can aggregate with time, and protein quality-control pathways are tasked with their ubiquitination and subsequent degradation [46,47]. PubMed:24457024

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complex(p(HGNC:BAG6), p(HGNC:UBA3)) increases deg(p(MESH:Proteins, pmod(HBP:misfolding))) View Subject | View Object

Because Bag6 interacts with both E3 ligases as well as the proteasome [57,58,60], it may promote both the ubiquitination and delivery of misfolded proteins to the proteasome while preventing their aggregation PubMed:24457024

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complex(p(HGNC:BAG6), p(MESH:Proteins, pmod(HBP:misfolding))) hasComponent p(MESH:Proteins, pmod(HBP:misfolding)) View Subject | View Object

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bp(GO:autophagy) increases deg(p(MESH:Proteins, pmod(HBP:misfolding))) View Subject | View Object

Although the UPS is accountable for the degradation of up to 80–90% of proteins, misfolded proteins and aggregates are too large to be processed through the proteasome barrel and can impede UPS function by physical occlusion, leaving autophagic-lysosomal breakdown as the only effective pathway to clear these proteins [25,26] PubMed:29758300

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bp(GO:autophagy) regulates deg(p(MESH:Proteins, pmod(HBP:misfolding))) View Subject | View Object

It has now been established that clearance of misfolded proteins from aggresomes is mediated at least in part by autophagy, implicating this pathway as a compensatory mechanism for degrading misfolded proteins when the proteasome is impaired [27,64,71,73]. PubMed:18930136

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path(MESH:"Neurodegenerative Diseases") positiveCorrelation p(MESH:Proteins, pmod(HBP:misfolding)) View Subject | View Object

Many neurodegenerative diseases are characterized by accumulation of misfolded protein deposits in affected brain regions, suggesting a failure in the cell’s degradative capacity [19]. PubMed:18930136

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Annotations
MeSH
Brain

bp(GO:"aggresome assembly") decreases p(MESH:Proteins, pmod(HBP:misfolding)) View Subject | View Object

Indeed, aggresome formation represents one such process employed by a cell to discard misfolded proteins (125) and has been implicated in neurodegenerative diseases (126). PubMed:29191965

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Out-Edges 6

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

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Annotations
MeSH
Endoplasmic Reticulum

p(MESH:Proteins, pmod(HBP:misfolding)) increases bp(HBP:"protein aggregation") View Subject | View Object

Misfolded proteins can aggregate with time, and protein quality-control pathways are tasked with their ubiquitination and subsequent degradation [46,47]. PubMed:24457024

Appears in Networks:

p(MESH:Proteins, pmod(HBP:misfolding)) decreases bp(GO:"neuron cellular homeostasis") View Subject | View Object

Accumulation of misfolded proteins and damaged organelles is highly detrimental for neuronal homeostasis and survival. PubMed:29758300

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p(MESH:Proteins, pmod(HBP:misfolding)) decreases a(MESH:Neurons) View Subject | View Object

Accumulation of misfolded proteins and damaged organelles is highly detrimental for neuronal homeostasis and survival. PubMed:29758300

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p(MESH:Proteins, pmod(HBP:misfolding)) positiveCorrelation path(MESH:"Neurodegenerative Diseases") View Subject | View Object

Many neurodegenerative diseases are characterized by accumulation of misfolded protein deposits in affected brain regions, suggesting a failure in the cell’s degradative capacity [19]. PubMed:18930136

Appears in Networks:
Annotations
MeSH
Brain

p(MESH:Proteins, pmod(HBP:misfolding)) increases p(HGNC:SQSTM1) View Subject | View Object

Cellular stresses such as polyQ expression, proteasome impairment, oxidative stress, and increased misfolded protein burden activate transcription and translation of p62, suggesting that it functions broadly in stress situations [83,84] PubMed:18930136

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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.