Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins
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Title
Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins
Authors
Keywords
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Journal
PROTEIN SCIENCE
Volume -, Issue -, Pages -
Publisher
Wiley
Online
2019-11-14
DOI
10.1002/pro.3789
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Note: Only part of the references are listed.- Comprehensive analysis of kinase-oriented phospho-signalling pathways
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- IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners
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- Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs
- (2012) Xiaowei Zhao et al. PLoS One
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- (2011) Hafumi Nishi et al. STRUCTURE
- Binary classification of protein molecules into intrinsically disordered and ordered segments
- (2011) Satoshi Fukuchi et al. BMC STRUCTURAL BIOLOGY
- Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data
- (2010) Regev Schweiger et al. Biology Direct
- Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis
- (2010) J. V. Olsen et al. Science Signaling
- Selectivity of Docking Sites in MAPK Kinases
- (2009) A. Jane Bardwell et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- In SilicoAnalysis of Phosphoproteome Data Suggests a Rich-get-richer Process of Phosphosite Accumulation over Evolution
- (2009) Nozomu Yachie et al. MOLECULAR & CELLULAR PROTEOMICS
- Identification, analysis, and prediction of protein ubiquitination sites
- (2009) Predrag Radivojac et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder
- (2008) Mark O. Collins et al. MOLECULAR & CELLULAR PROTEOMICS
- Comparative phosphoproteomics reveals evolutionary and functional conservation of phosphorylation across eukaryotes
- (2008) Jos Boekhorst et al. GENOME BIOLOGY
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