 Unfolded Protein Response
"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) |
G02.111.087.675.871.790.600.962 G02.111.087.693.600.850 G02.149.115.675.871.790.600.850 G02.149.115.693.600.925 G03.495.770.871.790.600.850 G05.355.315.670.600.850
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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".
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
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 UAMS Profiles by year, and whether "Unfolded Protein Response" 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 |
|---|
| 2023 | 1 | 1 | 2 | | 2020 | 0 | 1 | 1 | | 2019 | 0 | 1 | 1 | | 2018 | 0 | 2 | 2 | | 2017 | 0 | 1 | 1 | | 2016 | 0 | 1 | 1 | | 2015 | 0 | 1 | 1 | | 2014 | 1 | 1 | 2 | | 2013 | 1 | 2 | 3 | | 2012 | 0 | 1 | 1 | | 2011 | 2 | 2 | 4 | | 2010 | 0 | 2 | 2 |
To return to the timeline, click here.
Below are the most recent publications written about "Unfolded Protein Response" by people in Profiles over the past ten years.
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Iyer S, Adams DJ. Bone and the Unfolded Protein Response: In Sickness and in Health. Calcif Tissue Int. 2023 Jul; 113(1):96-109.
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Leal EC, Emanuelli T, Santos D, Moura J, Catarina Rg Fonseca A, Burgeiro A, Carvalho E. Dysregulation of endoplasmic reticulum stress response in skin wounds in a streptozotocin-induced diabetes mouse model. J Mol Endocrinol. 2023 04 01; 70(3).
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Plotkin M, O'Brien CA, Goellner J, Williams J, Carter W, Sharma S, Stone A. A Uromodulin Mutation Drives Autoimmunity and Kidney Mononuclear Phagocyte Endoplasmic Reticulum Stress. Am J Pathol. 2020 12; 190(12):2436-2452.
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Correll RN, Grimes KM, Prasad V, Lynch JM, Khalil H, Molkentin JD. Overlapping and differential functions of ATF6a versus ATF6? in the mouse heart. Sci Rep. 2019 02 14; 9(1):2059.
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Burgeiro A, Fonseca AC, Espinoza D, Carvalho L, Louren?o N, Antunes M, Carvalho E. Proteostasis in epicardial versus subcutaneous adipose tissue in heart failure subjects with and without diabetes. Biochim Biophys Acta Mol Basis Dis. 2018 06; 1864(6 Pt A):2183-2198.
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Bright MD, Clarke PA, Workman P, Davies FE. Oncogenic RAC1 and NRAS drive resistance to endoplasmic reticulum stress through MEK/ERK signalling. Cell Signal. 2018 04; 44:127-137.
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Li N, Johnson DC, Weinhold N, Kimber S, Dobbins SE, Mitchell JS, Kinnersley B, Sud A, Law PJ, Orlando G, Scales M, Wardell CP, F?rsti A, Hoang PH, Went M, Holroyd A, Hariri F, Pastinen T, Meissner T, Goldschmidt H, Hemminki K, Morgan GJ, Kaiser M, Houlston RS. Genetic Predisposition to Multiple Myeloma at 5q15 Is Mediated by an ELL2 Enhancer Polymorphism. Cell Rep. 2017 Sep 12; 20(11):2556-2564.
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Joo JH, Wang B, Frankel E, Ge L, Xu L, Iyengar R, Li-Harms X, Wright C, Shaw TI, Lindsten T, Green DR, Peng J, Hendershot LM, Kilic F, Sze JY, Audhya A, Kundu M. The Noncanonical Role of ULK/ATG1 in ER-to-Golgi Trafficking Is Essential for Cellular Homeostasis. Mol Cell. 2016 05 19; 62(4):491-506.
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Chandrika BB, Yang C, Ou Y, Feng X, Muhoza D, Holmes AF, Theus S, Deshmukh S, Haun RS, Kaushal GP. Endoplasmic Reticulum Stress-Induced Autophagy Provides Cytoprotection from Chemical Hypoxia and Oxidant Injury and Ameliorates Renal Ischemia-Reperfusion Injury. PLoS One. 2015; 10(10):e0140025.
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Cooley CB, Ryno LM, Plate L, Morgan GJ, Hulleman JD, Kelly JW, Wiseman RL. Unfolded protein response activation reduces secretion and extracellular aggregation of amyloidogenic immunoglobulin light chain. Proc Natl Acad Sci U S A. 2014 Sep 09; 111(36):13046-51.
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Cragle FK, Baldini G. Mild lipid stress induces profound loss of MC4R protein abundance and function. Mol Endocrinol. 2014 Mar; 28(3):357-67.
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