Intrinsic disorder and protein function.

By A. Keith Dunker, C. Brown, J. David Lawson, Lilia M. Iakoucheva, Zoran Obradovic. Biochemistry, 2002

808 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/74bedec29314b9ea34b9fdacf3b974196ffb5f4b

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Citations in the corpus

Cryo-EM: Beyond the Microscope (2017, background): “In addition, proteins and protein complexes in aqueous solution are intrinsically flexible to varying extents [18], creating structural heterogeneity that can be even more pronounced in multidomain proteins and multi-protein complexes [19,20].”
The interplay between structure and function in intrinsically unstructured proteins (2005, background): “changes or influence the orientation/localization of attached domains [7].”
The importance of intrinsic disorder for protein phosphorylation. (2004, background): “Relatively few regions of disorder have been structurally characterized, yet a signiﬁcant fraction of them contain phosphorylation sites (4).”
Intrinsic disorder and functional proteomics. (2007, background): “Indeed, it is interesting that catalytic events associated with regulation or signaling often occur in IDPs or ID regions (48) as discussed below.”
Variation Interpretation Predictors: Principles, Types, Performance, and Choice (2016, background): “These intrinsically disordered regions and proteins are involved in several activities [Dunker et al., 2002].”
Casein Proteins: Structural and Functional Aspects (2016, background): “Caseins are structurally classified as natively or intrinsically disordered proteins which is different from random coil conformation found in some globular proteins [76, 77].”
PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites (2007, background): “support for the hypothesis that protein phosphorylation occurs predominantly within regions without regular structure [7,8].”
DisProt 7.0: a major update of the database of disordered proteins (2016, unknown): “Therefore, we have developed a novel classification scheme that merges and expands previous schemes that suggested thirty (36) and six (9) different categories, to provide classified descriptors for their MFs.”
DisProt: a database of protein disorder (2005, methodology): “Despite the fact that intrinsically disordered proteins fail to form fixed three dimensional (3D) structure under physiological conditions, existing instead as ensembles of conformations, they carry out critically important biological functions (Dunker et al., 2002a; Iakoucheva et al., 2002).”
Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008, background): “IDP functions can be grouped into four broad classes: (a) molecular recognition, (b) molecular assembly, (c) protein modification, and (d ) entropic chain activities (36, 37).”
Flexible nets (2005, background): “…biological functions including cell signaling [35], molecular recognition [48], and various other interactions with proteins and nucleic acids [32,34,35,37,39–43,49 Recently, a number of groups have published predictors of protein disorder, several of which are available on the web (reviewed…”
Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life (2012, background): “Often, intrinsically disordered regions in proteins are involved in protein–protein interactions and molecular recognitions (Dunker et al., 2001, 2002, 2005; Radivojac et al., 2007; Tompa, 2002; Uversky, Oldfield, & Dunker, 2005).”
DisProt: the Database of Disordered Proteins (2006, background): “Functional proteins that lack the relatively fixed structure of enzymes and other globular proteins have been called ‘rheomormorphic’ (9), ‘natively unfolded’ (10), ‘intrinsically unstructured’ (11) and ‘natively or intrinsically disordered’ ( 12 ), among other terms.”
Conformational constraints for amyloid fibrillation: the importance of being unfolded. (2004, unknown): “unstructured) proteins [7–15].”