Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

By Peter E. Wright, H. J. Dyson. 1999

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Citations in the corpus

SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “new perspective where protein rigidity is no longer a foregone conclusion [2].”
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “Intrinsically disordered proteins and protein regions (IDPs/IDRs) carry out important biological functions without relying on a single well-defined conformation, defying the traditional structure-function paradigm (1).”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “IDPs A very specific feature of IDPs/IDRs is the fact that these biologically active proteins/regions fail to form specific 3D structures and exist as highly dynamic structural ensembles, either at the secondary or at the tertiary level [7, 27, 32, 40, 56, 85, 86].”
A microscale protein NMR sample screening pipeline (2009, background): “and transport of proteins in the cell (Dunker et al. 2002; Iakoucheva et al. 2002; Liu et al. 2002; Plaxco and Gross 2001; Wright and Dyson 1999).”
Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life (2012, background): “…undergo disorder-to-order transitions upon binding, which is crucial for recognition, regulation and signalling (Dunker et al., 2001; Dyson & Wright, 2002, 2005; Mohan et al., 2006; Oldfield, Cheng, Cortese, Romero, et al., 2005; Uversky et al., 2000; Vacic et al., 2007; Wright & Dyson, 1999).”
Sequence-based determinants and prediction of fuzzy interactions in protein complexes. (2020, background): “Specific interactions of disordered proteins first have been interpreted within the folding upon binding scenario, where protein that are disordered in their free states adopt well-defined structures in their bound forms [2] driven by specific contacts [3].”
Linking Folding and Binding (2009, background): “Coupled folding and binding of IDPs Although it has long been recognized that many intrinsically disordered protein domains fold upon binding to their targets [20], the molecular principles and broad repertoire of interactions are only now becoming understood.”
Conformational constraints for amyloid fibrillation: the importance of being unfolded. (2004, background): “Certain proteins seem to require a high degree of structural disorder in their native states to fulfill their function [7,9,11,13,15,153,154].”
Analyzing Protein Disorder with IUPred2A (2020, background): “At the N-terminus there are multiple overlapping motif sites that correspond to phosphorylation sites, and a phosphodegron motif which regulates the degradation of the protein (Wu et al., 2003).”
Prediction of intrinsic disorder and its use in functional proteomics. (2007, background): “They are also known as partially folded (3), flexible (4), mobile (5), rheomorphic (6), natively denatured (7), natively unfolded (8), intrinsically unstructured (9), ID (10), and natively disordered (11).”