"Unfolded Protein Response" 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 cellular response to environmental insults that cause disruptions in PROTEIN FOLDING and/or accumulation of defectively folded protein in the ENDOPLASMIC RETICULUM. It consists of a group of regulatory cascades that are triggered as a response to altered levels of calcium and/or the redox state of the endoplasmic reticulum. Persistent activation of the unfolded protein response leads to the induction of APOPTOSIS.
Descriptor ID |
D056811
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MeSH Number(s) |
G02.111.660.871.790.600.962 G02.111.691.600.850 G03.734.871.790.600.850 G05.308.670.600.850
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Concept/Terms |
Unfolded Protein Response- Unfolded Protein Response
- Protein Response, Unfolded
- Protein Responses, Unfolded
- Response, Unfolded Protein
- Responses, Unfolded Protein
- Unfolded Protein Responses
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Below are MeSH descriptors whose meaning is more general than "Unfolded Protein Response".
Below are MeSH descriptors whose meaning is more specific than "Unfolded Protein Response".
This graph shows the total number of publications written about "Unfolded Protein Response" by people in this website by year, and whether "Unfolded Protein Response" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2017 | 0 | 1 | 1 |
2021 | 1 | 1 | 2 |
2023 | 1 | 0 | 1 |
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Below are the most recent publications written about "Unfolded Protein Response" by people in Profiles.
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Analysis of Electric Field Stimulation in Blue Light Stressed 661W Cells. Int J Mol Sci. 2023 Feb 08; 24(4).
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Creld2 function during unfolded protein response is essential for liver metabolism homeostasis. FASEB J. 2021 10; 35(10):e21939.
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Molecular and Functional Effects of Loss of Cytochrome c Oxidase Subunit 8A. Biochemistry (Mosc). 2021 Jan; 86(1):33-43.
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Orientia tsutsugamushi Ank9 is a multifunctional effector that utilizes a novel GRIP-like Golgi localization domain for Golgi-to-endoplasmic reticulum trafficking and interacts with host COPB2. Cell Microbiol. 2017 07; 19(7).