 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 |
|---|
| 2013 | 1 | 1 | 2 | | 2014 | 0 | 1 | 1 | | 2015 | 1 | 0 | 1 | | 2016 | 1 | 1 | 2 | | 2017 | 1 | 2 | 3 | | 2018 | 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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Protter DSW, Rao BS, Van Treeck B, Lin Y, Mizoue L, Rosen MK, Parker R. Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly. Cell Rep. 2018 02 06; 22(6):1401-1412.
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Amore A, Knott BC, Supekar NT, Shajahan A, Azadi P, Zhao P, Wells L, Linger JG, Hobdey SE, Vander Wall TA, Shollenberger T, Yarbrough JM, Tan Z, Crowley MF, Himmel ME, Decker SR, Beckham GT, Taylor LE. Distinct roles of N- and O-glycans in cellulase activity and stability. Proc Natl Acad Sci U S A. 2017 12 26; 114(52):13667-13672.
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Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. Biochem J. 2017 10 25; 474(21):3689-3704.
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Ozdilek BA, Thompson VF, Ahmed NS, White CI, Batey RT, Schwartz JC. Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding. Nucleic Acids Res. 2017 Jul 27; 45(13):7984-7996.
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Wheeler JR, Matheny T, Jain S, Abrisch R, Parker R. Distinct stages in stress granule assembly and disassembly. Elife. 2016 09 07; 5.
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Protter DSW, Parker R. Principles and Properties of Stress Granules. Trends Cell Biol. 2016 09; 26(9):668-679.
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Lin Y, Protter DS, Rosen MK, Parker R. Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins. Mol Cell. 2015 Oct 15; 60(2):208-19.
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Xue R, Zakharov MN, Xia Y, Bhasin S, Costello JC, Jasuja R. Research resource: EPSLiM: ensemble predictor for short linear motifs in nuclear hormone receptors. Mol Endocrinol. 2014 May; 28(5):768-77.
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Geist L, Henen MA, Haiderer S, Schwarz TC, Kurzbach D, Zawadzka-Kazimierczuk A, Saxena S, Zerko S, Kozminski W, Hinderberger D, Konrat R. Protonation-dependent conformational variability of intrinsically disordered proteins. Protein Sci. 2013 Sep; 22(9):1196-205.
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Kurzbach D, Platzer G, Schwarz TC, Henen MA, Konrat R, Hinderberger D. Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin. Biochemistry. 2013 Aug 06; 52(31):5167-75.
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