Intrinsically Disordered Proteins
"Intrinsically Disordered Proteins" 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.
Functional proteins that do not have unique, stable, folded, three-dimensional native structures or that possess non-ordered regions under physiological conditions. They are characterized by extraordinary structural flexibility and plasticity, which enable them to adopt different conformations in response to different stimuli or different interactions.
| Descriptor ID |
D064267
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| MeSH Number(s) |
D12.776.481
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Intrinsically Disordered Proteins".
Below are MeSH descriptors whose meaning is more specific than "Intrinsically Disordered Proteins".
This graph shows the total number of publications written about "Intrinsically Disordered Proteins" by people in this website by year, and whether "Intrinsically Disordered Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2019 | 1 | 0 | 1 |
| 2020 | 1 | 0 | 1 |
| 2022 | 1 | 0 | 1 |
| 2023 | 1 | 0 | 1 |
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Below are the most recent publications written about "Intrinsically Disordered Proteins" by people in Profiles.
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A call to order: Examining structured domains in biomolecular condensates. J Magn Reson. 2023 01; 346:107318.
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IGF-dependent dynamic modulation of a protease cleavage site in the intrinsically disordered linker domain of human IGFBP2. Proteins. 2022 09; 90(9):1732-1743.
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Intrinsically Disordered Regions of the DNA-Binding Domain of Human FoxP1 Facilitate Domain Swapping. J Mol Biol. 2020 09 04; 432(19):5411-5429.
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Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins. Biomolecules. 2019 03 22; 9(3).