Characterization of molecular recognition features, MoRFs, and their binding partners.

By Vladimir Vacic, Christopher J. Oldfield, Amrita Mohan, Predrag Radivojac, Marc S. Cortese, Vladimir N Uversky, A. Keith Dunker. 2007

473 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Materials Chemistry, Molecular Biology

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Citations in the corpus

IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “Such disordered binding regions or MoRFs (molecular recognition features) commonly occur in modular proteins involved in signaling and regulation (3,4).”
Prediction of Protein Binding Regions in Disordered Proteins (2009, background): “However, recent comparisons of these structures with complexes formed between ordered proteins pointed out several differences [42–44].”
The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins. (2015, background): “These proteins contain disordered segments that undergo disorder-to-order transitions upon binding, which have been referred to as molecular recognition features/molecular recognition elements [46–48] or preformed structural elements and prestructured motifs [44,49].”
Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008, methodology): “In agreement with this model, recent computational studies of such binding showed that the disordered partner might contain a conformational preference for the structure it will take upon binding, and that these so-called preformed elements are helices (53, 94, 98, 145).”
Rosetta FlexPepDock ab-initio: Simultaneous Folding, Docking and Refinement of Peptides onto Their Receptors (2011, background): “These peptides often form a modular binding motif, which can be embedded in intrinsically unstructured protein regions and within flexible loops, in order to confer desired interactions [2,3,4,5].”
Computational Identification of MoRFs in Protein Sequences Using Hierarchical Application of Bayes Rule (2015, methodology): “On the other hand, SVM T relies on a RBF kernel to identify sequence B) Disorder : The residue composition of MoRFs is more similar to structured domains than to their surrounding disordered regions [7, 12, 13, 16].”
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).”
MFSPSSMpred: identifying short disorder-to-order binding regions in disordered proteins based on contextual local evolutionary conservation (2013, background): “A number of studies have analyzed the attributes of MoRFs [1-9].”