Protein Aggregation, Pathological
"Protein Aggregation, Pathological" 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 biochemical phenomenon in which misfolded proteins aggregate either intra- or extracellularly. Triggered by factors such as MUTATION, POST-TRANSLATIONAL MODIFICATIONS, and environmental stress, it is generally associated with ALZHEIMER DISEASE; PARKINSON DISEASE; HUNTINGTON DISEASE; and TYPE 2 DIABETES MELLITUS.
| Descriptor ID |
D066263
|
| MeSH Number(s) |
C23.550.770 G02.111.675
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Protein Aggregation, Pathological".
Below are MeSH descriptors whose meaning is more specific than "Protein Aggregation, Pathological".
This graph shows the total number of publications written about "Protein Aggregation, Pathological" by people in this website by year, and whether "Protein Aggregation, Pathological" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2015 | 1 | 0 | 1 |
| 2016 | 0 | 1 | 1 |
| 2017 | 1 | 2 | 3 |
| 2018 | 3 | 1 | 4 |
| 2019 | 1 | 0 | 1 |
| 2020 | 1 | 0 | 1 |
| 2021 | 1 | 0 | 1 |
| 2024 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Aggregation, Pathological" by people in Profiles.
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TYK2 regulates tau levels, phosphorylation and aggregation in a tauopathy mouse model. Nat Neurosci. 2024 Dec; 27(12):2417-2429.
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Disulfide bond formation in microtubule-associated tau protein promotes tau accumulation and toxicity in vivo. Hum Mol Genet. 2021 10 13; 30(21):1955-1967.
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Deletion of ubiquitin ligase Nedd4l exacerbates ischemic brain damage. J Cereb Blood Flow Metab. 2021 05; 41(5):1058-1066.
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Acute zoster plasma contains elevated amyloid, correlating with A?42 and amylin levels, and is amyloidogenic. J Neurovirol. 2020 06; 26(3):422-428.
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Traumatic Brain Injury Induces Tau Aggregation and Spreading. J Neurotrauma. 2020 01 01; 37(1):80-92.
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Single-Molecule FRET Detection of Early-Stage Conformations in a-Synuclein Aggregation. Methods Mol Biol. 2019; 1948:221-233.
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A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation. Biochemistry. 2018 12 18; 57(50):6822-6826.
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Acetylation Disfavors Tau Phase Separation. Int J Mol Sci. 2018 May 04; 19(5).
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Mapping interactions with the chaperone network reveals factors that protect against tau aggregation. Nat Struct Mol Biol. 2018 05; 25(5):384-393.
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Phosphorylated TDP-43 (pTDP-43) aggregates in the axial skeletal muscle of patients with sporadic and familial amyotrophic lateral sclerosis. Acta Neuropathol Commun. 2018 04 13; 6(1):28.