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 |
|---|
| 2017 | 1 | 1 | 2 |
| 2019 | 1 | 0 | 1 |
| 2022 | 4 | 0 | 4 |
| 2024 | 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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How hydrophobicity, side chains, and salt affect the dimensions of disordered proteins. Protein Sci. 2024 May; 33(5):e4986.
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Intrinsically disordered BMP4 morphogen and the beak of the finch: Co-option of an ancient axial patterning system. Int J Biol Macromol. 2022 Oct 31; 219:366-373.
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Pan-cancer assessment of mutational landscape in intrinsically disordered hotspots reveals potential driver genes. Nucleic Acids Res. 2022 05 20; 50(9):e49.
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Intrinsically Disordered Proteins: Critical Components of the Wetware. Chem Rev. 2022 03 23; 122(6):6614-6633.
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Co-opting disorder into order: Intrinsically disordered proteins and the early evolution of complex multicellularity. Int J Biol Macromol. 2022 Mar 15; 201:29-36.
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Structural and Dynamical Order of a Disordered Protein: Molecular Insights into Conformational Switching of PAGE4 at the Systems Level. Biomolecules. 2019 02 22; 9(2).
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1H, 15N, and 13C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck. Biomol NMR Assign. 2019 04; 13(1):71-74.
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Allosteric control of a bacterial stress response system by an anti-s factor. Mol Microbiol. 2018 01; 107(2):164-179.
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Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water. Science. 2017 10 13; 358(6360):238-241.
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Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response. Cell. 2017 03 09; 168(6):1028-1040.e19.