The importance of intrinsic disorder for protein phosphorylation.

By Lilia M. Iakoucheva, Predrag Radivojac, C. Brown, Timothy R. O'Connor, Jason G. Sikes, Zoran Obradovic, A. Keith Dunker. Nucleic Acids Research, 2004

1,418 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/a181a8ded173d680510a790978a3d2584d4e6b79

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Citations in the corpus

Intrinsically disordered proteins: regulation and disease. (2011, background): “Consistent with previous observations [6], we reported that disordered proteins are on average targets of twice as many kinases as structured proteins in yeast [28 ] and observed that the targets of several kinases show a significant enrichment to be disordered.”
Identification, Analysis and Prediction of Protein Ubiquitination Sites (2010, background): “20,27,28,100 Moreover, the development of UbPred represents an attempt to identify candidate Ub sites based on the local sequence information.”
Linking Folding and Binding (2009, background): “Analysis of the sequences surrounding known phosphorylation sites reveals a strong propensity towards intrinsic disorder in the neighboring regions of the protein [56].”
PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse (2011, background): “The results (Figure 6) show that 77% of phospho-Ser/ Thr (pS/T) sites occur outside structured domains, a result consistent with previous observations (42,43).”
Intrinsic disorder and functional proteomics. (2007, methodology): “For example, in predicting protein phosphorylation sites, only 136 tyrosine and 141 threonine sites had been retained for the predictor construction after redundancy removal (123).”
Phospho.ELM: a database of phosphorylation sites—update 2011 (2010, background): “Phosphorylation sites are often found in intrinsically disordered regions of proteins (34), which usually cannot be experimentally determined by X-ray crystallography.”
Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. (2014, background): “%) were found in disordered regions, as expected (Iakoucheva et al., 2004).”
The interplay between structure and function in intrinsically unstructured proteins (2005, background): “success of disorder-based prediction of phosphorylation sites [41] and an array of recent observations of the cleavage of non-ubiquitinated, disordered proteins, such as casein [45], tau [46] and p21 [47] by the 20S proteasome and the disorder-targeted ubiquitination of securin and cyclin B in cell ”
Disorder Prediction Methods, Their Applicability to Different Protein Targets and Their Usefulness for Guiding Experimental Studies (2015, background): “have demonstrated that there is a functional element to disorder [1,3,9–12].”
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008, result): “This is consistent with previous observation of a strong bias for post translational modifications toward intrinsically disordered regions [83].”
GPS 2.0, a Tool to Predict Kinase-specific Phosphorylation Sites in Hierarchy *S (2008, methodology): “To predict general phosphorylation sites, several tools have been developed, such as DISPHOS (2), NetPhos (3), NetPhosYeast (4), and GANNPhos (5).”
Length-dependent prediction of protein intrinsic disorder (2006, background): “designing protein structure-function experiments [1,30], understanding the roles of disorder in cell-signalling and cancer-related proteins [31], improving prediction of protein phosphorylation sites [32], and improving the throughput of structural genomics pipelines [25,33].”
Prediction of Protein Binding Regions in Disordered Proteins (2009, background): “Beside their involvement in protein-protein interactions, these proteins are also subjects of various post-translational modifications that control their functions, localization and turnover [33].”