Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins

By Zsuzsanna Dosztányi, Bálint Mészáros, István Simon. 2010

131 citations recorded by the source corpus.

Subfields: Biomedical Engineering, Materials Chemistry, Molecular Biology

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Citations in the corpus

CABS-flex 2.0: a web server for fast simulations of flexibility of protein structures (2018, background): “In comparison to sequence-based predictors (10), CABS-flex is better adapted to detecting non-obvious dynamic fluctuations, for example within the well-defined secondary structural elements that could be biologically relevant.”
Evaluation of disorder predictions in CASP9 (2011, background): “23–25 In a recent review, He et al. 24 provide a historical perspective of progress in this field, pointing out the important role that the CASP experiments have played in these advancements.”
Prediction of protein disorder based on IUPred (2018, background): “Since then, more than 50 different disorder prediction methods has been developed by various research groups.(20,21) One class of methods relies on simple amino acid propensity scales, such as various types of hydrophobicity scales, the propensity to participate in regular secondary structure elemen”
Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions (2017, methodology): “We searched for the disorder predictors using a variety of sources including prior reviews [30,34,32,33,3537,31], studies that assess and compare predictive performance of these methods [38-40,27], and manual search of PubMed with query “(((disorder[Title]) OR unstructured[Title]) AND prediction[Tit”
Genome‐scale prediction of proteins with long intrinsically disordered regions (2014, background): “7,15–17 This suggests that disorder is predictable from the protein sequence and enables development of computational approaches for the sequence-derived prediction of disorder.”
Comprehensive comparative assessment of in-silico predictors of disordered regions. (2012, methodology): “The disorder is frequently observed in regions with low sequence complexity and with low content of hydrophobic amino acids and high net charge, which would often form a core of a folded globular protein, and is often associated with lack of secondary structure and unique evolutionary profiles [[9]-”