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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Annual Review of Biochemistry, 2014Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
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Intrinsically disordered protein regions at membrane contact sites
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2021Membrane contact sites (MCS) are regions of close apposition between membrane-bound organelles. Proteins that occupy MCS display various domain organisation. Among them, lipid transfer proteins (LTPs) frequently contain both structured domains as well as regions of intrinsic disorder.
Denisa, Jamecna, Bruno, Antonny
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Functional roles of transiently and intrinsically disordered regions within proteins
FEBS Journal, 2015 Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well-folded structures.
Vladimir N Uversky
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Presence and utility of intrinsically disordered regions in kinases
Molecular BioSystems, 2014Abstract Since aberrant cell signaling pathways underlie majority of pathophysiological morbidities, kinase inhibitors are routinely used for pharmacotherapy. However, most kinase inhibitors suffer from adverse off-target effects.
Kathiriya, Jaymin J. +5 more
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Computational prediction of functions of intrinsically disordered regions
2019Intrinsically disorder regions (IDRs) are abundant in nature, particularly among Eukaryotes. While they facilitate a wide spectrum of cellular functions including signaling, molecular assembly and recognition, translation, transcription and regulation, only several hundred IDRs are annotated functionally.
Akila, Katuwawala +2 more
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Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER
2020Intrinsically disordered proteins and protein regions are ubiquitous across eukaryotic proteomes where they play a range of functional roles. Unlike folded proteins, IDRs lack a well-defined native state but exist in heterogeneous ensembles of conformations.
Garrett M, Ginell, Alex S, Holehouse
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Coding Regions of Intrinsic Disorder Accommodate Parallel Functions
Trends in Biochemical Sciences, 2016Numerous DNA- and RNA-level functions are embedded in protein-coding regions, which constrains their structure, function, and evolution. Accumulating evidence suggests that such additional, overlapping functions occur preferentially in the coding sequences of intrinsically disordered proteins/regions (IDPs/IDRs), especially in those that are newly ...
Tompa, Peter, PANCSA, Rita
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Protein & Peptide Letters, 2020
Background: Intrinsically disordered proteins lack a well-defined three dimensional structure under physiological conditions while possessing the essential biological functions. They take part in various physiological processes such as signal transduction, transcription and posttranslational modifications and etc.
WeiXia, Xie, Yong E, Feng
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Background: Intrinsically disordered proteins lack a well-defined three dimensional structure under physiological conditions while possessing the essential biological functions. They take part in various physiological processes such as signal transduction, transcription and posttranslational modifications and etc.
WeiXia, Xie, Yong E, Feng
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Acetylation of intrinsically disordered regions regulates phase separation
Nature Chemical Biology, 2018Liquid-liquid phase separation (LLPS) of proteins containing intrinsically disordered regions (IDRs) has been proposed as a mechanism underlying the formation of membrane-less organelles. Tight regulation of IDR behavior is essential to ensure that LLPS only takes place when necessary.
Makoto Saito +7 more
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PREDICTION OF BOUNDARIES BETWEEN INTRINSICALLY ORDERED AND DISORDERED PROTEIN REGIONS [PDF]
Biocomputing 2003, 2002 Using proteins with both disordered and ordered regions collected through literature searches and database scanning, we assembled a set of 24-residue long segments centered on their order/disorder boundaries as well as a larger set of non-boundary segments consisting of either order or disorder.
Predrag Radivojac +3 more
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