Coupling of folding and binding for unstructured proteins.

By H. J. Dyson, Peter E. Wright. 2002

1,258 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

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Citations in the corpus

The determinants for the native activities of the bovine papillomavirus type 1 E2 protein are separable (2004, methodology): “Later this hypothesis was verified at least for some TAD-s (for a review (Dyson and Wright, 2002)).”
Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008, background): “NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).”
The importance of intrinsic disorder for protein phosphorylation. (2004, background): “The phosphorylation sites [ST]-x-[RK] and [ST]-x(2)-[DE] for protein kinase C and casein kinase II, respectively, are also identical to the sites observed here (Fig.”
Intrinsic disorder in cell-signaling and cancer-associated proteins. (2002, positive): “Second, intrinsic disorder promotes binding diversity by enabling proteins to interact with numerous partners.(7,9) Thus, hubs and nodes in signaling networks are likely to include proteins with extended disordered regions.”
Linking Folding and Binding (2009, background): “folding and binding events involve relatively short amphipathic motifs contained within longer disordered sequences [1,21].”
Otolith Biochemistry—A Review (2019, background): “An intrinsically disordered protein (IDP) is one which lacks a specific tertiary structure, but that upon binding to a ligand, often folds into a globular or other specified shape (Dyson and Wright, 2002; Fink, 2005; Kaplon et al., 2008; Kaplon et al., 2009; Uversky and Dunker, 2010).”
Intrinsic disorder in transcription factors. (2006, background): “Reported evidence demonstrated that high abundance of intrinsic disorder in eukaryotic genomes in comparison to bacteria and archaea may reflect the greater need for disorder-associated signaling and regulation in nucleated cells [Dyson & Wright, 2002; Iakoucheva et al., 2002; Ward et al., 2004].”
Flexible nets (2005, background): “…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 in [48]; see…”
Casein Proteins: Structural and Functional Aspects (2016, background): “This property can therefore also help these proteins to interact with multiple proteins or target molecules at one time [59].”
Disorder Prediction Methods, Their Applicability to Different Protein Targets and Their Usefulness for Guiding Experimental Studies (2015, background): “Proteins containing disorder are now understood to be involved in various regulatory roles; intrinsic disorder is believed to allow for binding to multiple targets and also to increase efficiency of binding [13,14].”
Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes (2006, background): “Many ID proteins have been shown to mediate interactions through a disorder-to-order transition upon binding to their biological targets [14,15].”
ANCHOR: web server for predicting protein binding regions in disordered proteins (2009, positive): “Disordered binding regions play a critical role in various biological processes, involving regulation and signaling (Dyson and Wright, 2002).”