Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life

By Zhenling Peng, Jing Yan, Xiao Fan, Marcin J. Mizianty, Bin Xue, Kui Wang, Gang Hu, Vladimir N Uversky, Lukasz Kurgan. 2014

345 citations recorded by the source corpus.

Subfields: Molecular Biology

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In Molecular Biology

Citations in the corpus

Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “According to various computational analyses, the presumed portion of sequences with predicted long IDPRs (≥30 residues) is roughly the same in bacteria and archaea, but is drastically higher in eukaryota [2, 6, 8, 17, 25].”
Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell (2019, background): “304 Many studies aiming at a general classification of functional roles of protein intrinsic disorder were 305 based on the required presence of long disordered regions in the sequence [18-20, 42-45], thus 306 considering IDPRs and IDPs as a single entity [see, for example, 18-20, 42-45].”
How Common Is Disorder? Occurrence of Disordered Residues in Four Domains of Life (2015, background): “If to use the definition of the fraction of disordered residues as the number of disordered residues divided by the total number of residues [22,28], then both proteins are ordered proteins.”
Disorder Prediction Methods, Their Applicability to Different Protein Targets and Their Usefulness for Guiding Experimental Studies (2015, background): “Intrinsic disorder is a highly conserved phenomenon and the more “complex” an organism, the greater the levels of disorder that are found within the proteome [3,6,7].”
Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions (2017, methodology): “According to estimates between 3 and 17% of eukaryotic proteins are fully disordered, depending on an organism [4], and about 30-50% of eukaryotic proteins have at least one long (≥ 30 consecutive residues) IDR [5,4,6,3].”
OpenCell: proteome-scale endogenous tagging enables the cartography of human cellular organization (2022, background): “This adds to the growing appreciation that intrinsic disorder, which is much more prevalent in eukaryotic than in prokaryotic proteomes ( 84 , 85 ), plays a key role in the functional sub-compartmentalization of the eukaryotic nucleo-and cytoplasm in the context of biomolecular condensation ( 86 ).”
DFLpred: High-throughput prediction of disordered flexible linker regions in protein sequences (2016, neutral): “…signaling, regulation, control, storage of small molecules, sites for posttranslational modifications (PTMs), transcription, translation and assembly of multi-protein complexes (Dunker et al., 2008; Dyson and Wright, 2005; Peng et al., 2014; Tompa, 2005; Wright and Dyson, 1999; Xie et al., 2007).”