Intrinsically disordered proteins in human diseases: introducing the D2 concept.

By Vladimir N Uversky, Christopher J. Oldfield, A. Keith Dunker. 2008

1,356 citations recorded by the source corpus.

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In Molecular Biology

Citations in the corpus

SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “Advantaged by their disordered ﬂexibility [4], IDPs play essential roles in signaling, assembling, and regulatory functions [5], and are implicated in numerous human diseases, such as cancer, amyloidoses, cardiovascular disease, neurodegenerative diseases, and various genetic diseases [6].”
DisProt 7.0: a major update of the database of disordered proteins (2016, neutral): “Because of that, IDPs / IDRs are often implicated in diseases (6) and represent important drug targets (7).”
The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins. (2015, background): “Detailed experimental characterization of structure and disorder in proteins remains a difficult and costly task, which is associated with the risk of obtaining inconclusive results especially when not employing a broad range of different techniques [7–12,14].”
Mapping Residual Structure in Intrinsically Disordered Proteins at Residue Resolution Using Millisecond Hydrogen/Deuterium Exchange and Residue Averaging (2015, background): “Intrinsically disordered proteins contain regions that lack well-defined structure under in vivo or native in vitro conditions [1–3].”
p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept (2016, background): “On the contrary, IDPs are characterized by a relative flat but rough energy landscape with multiple local energy minima separated by small barriers [14,33,76,82].”
Comprehensive comparative assessment of in-silico predictors of disordered regions. (2012, background): “Their prevalence was implicated in various human diseases [[6],[7]] and they were suggested as”
Prediction of Protein Binding Regions in Disordered Proteins (2009, background): “Furthermore, disordered proteins are often associated with various diseases [35].”
The Protein Structure Initiative: achievements and visions for the future (2012, background): “Genomes encode large numbers of natively disordered proteins or protein regions that are functionally important for protein-protein interactions, modulating binding affinities, and regulating signaling pathways [51-55].”
Improving protein disorder prediction by deep bidirectional long short‐term memory recurrent neural networks (2016, background): “IDPs have been implicated in many human diseases, including cancer, cardiovascular and neurodegenerative diseases and genetic diseases (Raychaudhuri et al. , 2009; Uversky et al. , 2005, 2008).”
Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell (2019, background): “This observation better specifies the quite established D2 concept 339 [32].”