Intrinsic disorder and functional proteomics.

By Predrag Radivojac, Lilia M. Iakoucheva, Christopher J. Oldfield, Zoran Obradovic, Vladimir N Uversky, A. Keith Dunker. Biophysical Journal, 2007

690 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/ccc06153a8d5a2475d5084481427ca65cbef3cef

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Citations in the corpus

Linking Folding and Binding (2009, background): “Prediction of disordered regions through bioinformatic searches has reached a high degree of sophistication and numerous web servers are available for prediction of disordered regions of protein sequences (reviewed in [9]).”
A decade and a half of protein intrinsic disorder: Biology still waits for physics (2013, background): “Identification of IDPs as unique entities belonging to a new protein tribe is directly related to the recognition that their amino acid sequences are dramatically different from those of ordered proteins.10,12,13,30–32 For example, it has been pointed out that the low content of hydrophobic residues”
Sixty-five years of the long march in protein secondary structure prediction: the final stretch? (2016, background): “As a result, the accuracy of protein secondary structure prediction directly impacts the accuracy of protein structure prediction (template-based or template-free) [15–18], prediction of solvent exposure of amino acid residues [19–21] and discrimination of structured from unstructured, intrinsically”
Standardized evaluation of protein stability. (2010, methodology): “Sequences of unfolded polypeptides It is now well accepted that some proteins do not exist as a unique 3D conformation and that part of the information encoding for their disorder is in sequences [11].”
Protein tandem repeats: the more perfect the less structured (2010, background): “On the other hand, IDPs ⁄ IDRs were shown to be substantially enriched in so-called disorder-promoting residues: Ala, Arg, Gly, Gln, Ser, Pro, Glu, and Lys [32–36].”
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. (2012, neutral): “Unexpectedly, tyrosine (Y) is also enriched in these segments (especially in proteins containing classical RBDs), although the ‘‘orderpromoting’’ aromatic residues are depleted in disordered regions of the human proteome (Figure S6A) (Radivojac et al., 2007).”
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008, result): “Both predictors give good agreement with the experimental determination of intrinsic disorder [83,91-109], and in the case of p53 both of their predictions agree well with experimental characterization.”
Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life (2012, background): “Often, intrinsically disordered regions in proteins are involved in protein–protein interactions and molecular recognitions (Dunker et al., 2001, 2002, 2005; Radivojac et al., 2007; Tompa, 2002; Uversky, Oldfield, & Dunker, 2005).”