"Amyloid" 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 fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.
| Descriptor ID |
D000682
|
| MeSH Number(s) |
D05.500.049 D12.776.049
|
| Concept/Terms |
Amyloid- Amyloid
- Amyloid Substance
- Substance, Amyloid
|
Below are MeSH descriptors whose meaning is more general than "Amyloid".
Below are MeSH descriptors whose meaning is more specific than "Amyloid".
This graph shows the total number of publications written about "Amyloid" by people in this website by year, and whether "Amyloid" 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 |
|---|
| 1995 | 1 | 0 | 1 |
| 1998 | 1 | 0 | 1 |
| 2000 | 1 | 2 | 3 |
| 2003 | 1 | 0 | 1 |
| 2004 | 0 | 1 | 1 |
| 2006 | 0 | 1 | 1 |
| 2009 | 0 | 1 | 1 |
| 2010 | 1 | 1 | 2 |
| 2012 | 0 | 1 | 1 |
| 2013 | 1 | 0 | 1 |
| 2014 | 0 | 1 | 1 |
| 2016 | 2 | 0 | 2 |
| 2017 | 3 | 0 | 3 |
| 2018 | 1 | 0 | 1 |
| 2019 | 2 | 2 | 4 |
| 2020 | 4 | 2 | 6 |
| 2021 | 0 | 2 | 2 |
| 2022 | 1 | 2 | 3 |
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Below are the most recent publications written about "Amyloid" by people in Profiles.
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Modulating Nanodroplet Formation En Route to Fibrillization of Amyloid Peptides with Designed Flanking Sequences. Biomacromolecules. 2022 10 10; 23(10):4179-4191.
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Substoichiometric Inhibition of Insulin against IAPP Aggregation Is Attenuated by the Incompletely Processed N-Terminus of proIAPP. ACS Chem Neurosci. 2022 07 06; 13(13):2006-2016.
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Hydrophobic/Hydrophilic Ratio of Amphiphilic Helix Mimetics Determines the Effects on Islet Amyloid Polypeptide Aggregation. J Chem Inf Model. 2022 04 11; 62(7):1760-1770.
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A buried glutamate in the cross-? core renders ?-endorphin fibrils reversible. Nanoscale. 2021 Dec 02; 13(46):19593-19603.
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Direct Observation of ?-Barrel Intermediates in the Self-Assembly of Toxic SOD128-38 and Absence in Nontoxic Glycine Mutants. J Chem Inf Model. 2021 02 22; 61(2):966-975.
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Amyloid Aggregation under the Lens of Liquid-Liquid Phase Separation. J Phys Chem Lett. 2021 Jan 14; 12(1):368-378.
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aB-Crystallin Chaperone Inhibits A? Aggregation by Capping the ?-Sheet-Rich Oligomers and Fibrils. J Phys Chem B. 2020 11 12; 124(45):10138-10146.
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Phosphorylated cofilin-2 is more prone to oxidative modifications on Cys39 and favors amyloid fibril formation. Redox Biol. 2020 10; 37:101691.
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Elevated amyloidoses of human IAPP and amyloid beta by lipopolysaccharide and their mitigation by carbon quantum dots. Nanoscale. 2020 Jun 18; 12(23):12317-12328.
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Interfacial charge transfer with exfoliated graphene inhibits fibril formation in lysozyme amyloid. Biointerphases. 2020 06 03; 15(3):031010.