"Protein Folding" 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.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Descriptor ID |
D017510
|
MeSH Number(s) |
G01.154.651 G02.111.688
|
Concept/Terms |
Protein Folding- Protein Folding
- Folding, Protein
- Foldings, Protein
- Protein Foldings
Protein Folding, Globular- Protein Folding, Globular
- Folding, Globular Protein
- Foldings, Globular Protein
- Globular Protein Folding
- Globular Protein Foldings
- Protein Foldings, Globular
|
Below are MeSH descriptors whose meaning is more general than "Protein Folding".
Below are MeSH descriptors whose meaning is more specific than "Protein Folding".
This graph shows the total number of publications written about "Protein Folding" by people in this website by year, and whether "Protein Folding" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2010 | 0 | 2 | 2 |
2012 | 1 | 1 | 2 |
2013 | 0 | 2 | 2 |
2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Folding" by people in Profiles.
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Pontocerebellar hypoplasia due to bi-allelic variants in MINPP1. Eur J Hum Genet. 2021 03; 29(3):411-421.
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Integration of two ancestral chaperone systems into one: the evolution of eukaryotic molecular chaperones in light of eukaryogenesis. Mol Biol Evol. 2014 Feb; 31(2):410-8.
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Overexpression of synphilin-1 promotes clearance of soluble and misfolded alpha-synuclein without restoring the motor phenotype in aged A30P transgenic mice. Hum Mol Genet. 2014 Feb 01; 23(3):767-81.
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Cumulative impact of chaperone-mediated folding on genome evolution. Biochemistry. 2012 Dec 18; 51(50):9941-53.
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Chaperones divide yeast proteins into classes of expression level and evolutionary rate. Genome Biol Evol. 2012; 4(5):618-25.
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Chaperonin-dependent accelerated substitution rates in prokaryotes. Genome Biol Evol. 2010; 2:602-8.
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A new amyloidosis caused by fibrillar aggregates of mutated corneodesmosin. FASEB J. 2010 Sep; 24(9):3416-26.