 Endoplasmic Reticulum-Associated Degradation
"Endoplasmic Reticulum-Associated Degradation" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A degradation process whereby incorrectly folded proteins are selectively transported out of the ENDOPLASMIC RETICULUM and into the CYTOSOL. The misfolded proteins are subsequently ubiquitinated and degraded by the PROTEASOME.
| Descriptor ID |
D060746
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| MeSH Number(s) |
G02.111.087.675.871.790.600.962.500 G02.111.087.693.600.850.500 G02.149.115.675.871.790.600.850.500 G02.149.115.693.600.925.500 G03.495.770.871.790.600.850.500 G05.355.315.670.600.850.500
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| Concept/Terms |
Endoplasmic Reticulum-Associated Degradation- Endoplasmic Reticulum-Associated Degradation
- Degradation, Endoplasmic Reticulum-Associated
- Endoplasmic Reticulum Associated Degradation
- Reticulum-Associated Degradation, Endoplasmic
- ERAD Pathway
- ERAD Pathways
- Pathway, ERAD
- Pathways, ERAD
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Below are MeSH descriptors whose meaning is more general than "Endoplasmic Reticulum-Associated Degradation".
- Biological Sciences [G]
- Chemical Phenomena [G02]
- Biochemical Phenomena [G02.111]
- Biochemical Processes [G02.111.087]
- Peptide Biosynthesis [G02.111.087.675]
- Protein Biosynthesis [G02.111.087.675.871]
- Protein Modification, Translational [G02.111.087.675.871.790]
- Protein Processing, Post-Translational [G02.111.087.675.871.790.600]
- Unfolded Protein Response [G02.111.087.675.871.790.600.962]
- Endoplasmic Reticulum-Associated Degradation [G02.111.087.675.871.790.600.962.500]
- Protein Modification, Translational [G02.111.087.693]
- Protein Processing, Post-Translational [G02.111.087.693.600]
- Unfolded Protein Response [G02.111.087.693.600.850]
- Endoplasmic Reticulum-Associated Degradation [G02.111.087.693.600.850.500]
- Chemical Processes [G02.149]
- Biochemical Processes [G02.149.115]
- Peptide Biosynthesis [G02.149.115.675]
- Protein Biosynthesis [G02.149.115.675.871]
- Protein Modification, Translational [G02.149.115.675.871.790]
- Protein Processing, Post-Translational [G02.149.115.675.871.790.600]
- Unfolded Protein Response [G02.149.115.675.871.790.600.850]
- Endoplasmic Reticulum-Associated Degradation [G02.149.115.675.871.790.600.850.500]
- Protein Modification, Translational [G02.149.115.693]
- Protein Processing, Post-Translational [G02.149.115.693.600]
- Unfolded Protein Response [G02.149.115.693.600.925]
- Endoplasmic Reticulum-Associated Degradation [G02.149.115.693.600.925.500]
- Metabolic Phenomena [G03]
- Metabolism [G03.495]
- Peptide Biosynthesis [G03.495.770]
- Protein Biosynthesis [G03.495.770.871]
- Protein Modification, Translational [G03.495.770.871.790]
- Protein Processing, Post-Translational [G03.495.770.871.790.600]
- Unfolded Protein Response [G03.495.770.871.790.600.850]
- Endoplasmic Reticulum-Associated Degradation [G03.495.770.871.790.600.850.500]
- Genetic Phenomena [G05]
- Genetic Processes [G05.355]
- Gene Expression Regulation [G05.355.315]
- Protein Modification, Translational [G05.355.315.670]
- Protein Processing, Post-Translational [G05.355.315.670.600]
- Unfolded Protein Response [G05.355.315.670.600.850]
- Endoplasmic Reticulum-Associated Degradation [G05.355.315.670.600.850.500]
Below are MeSH descriptors whose meaning is more specific than "Endoplasmic Reticulum-Associated Degradation".
This graph shows the total number of publications written about "Endoplasmic Reticulum-Associated Degradation" by people in this website by year, and whether "Endoplasmic Reticulum-Associated Degradation" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2013 | 0 | 1 | 1 | | 2017 | 1 | 0 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "Endoplasmic Reticulum-Associated Degradation" by people in Profiles.
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Ren G, Tardi NJ, Matsuda F, Koh KH, Ruiz P, Wei C, Altintas MM, Ploegh H, Reiser J. Podocytes exhibit a specialized protein quality control employing derlin-2 in kidney disease. Am J Physiol Renal Physiol. 2018 03 01; 314(3):F471-F482.
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Arrojo E Drigo R, Egri P, Jo S, Gereben B, Bianco AC. The type II deiodinase is retrotranslocated to the cytoplasm and proteasomes via p97/Atx3 complex. Mol Endocrinol. 2013 Dec; 27(12):2105-15.
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