Research
Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data
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* Corresponding author: Michal Linial michall@cc.huji.ac.il
1 School of Computer Science and Engineering, Hebrew University of Jerusalem, 91904, Israel
2 Department of Biological Chemistry, Institute of Life Sciences, Sudarsky Center for Computational Biology, Hebrew University of Jerusalem, 91904, Israel
Biology Direct 2010, 5:6 doi:10.1186/1745-6150-5-6
Published: 26 January 2010Additional files
Additional file 1:
Supplementary data S1. List of exceptionally cluster-rich proteins and their functional assignments. Source data for Figure 4.
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Additional file 2:
Supplementary data S2. Distribution of the number of possible protein kinases. Supportive information for Table 3.
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Additional file 3:
Supplementary data S3. The distribution of the distance to the nearest phosphosite, for real phosphosites and random phosphosites; where the random distribution was calculated taking into consideration the actual number of sites on the protein (see Materials and Methods, and also Reviewers' Comments).
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Additional file 4:
Supplementary data S4. The distribution of the distance to the nearest phosphosite, for real phosphosites and random phosphosites; where the random distribution was calculated taking into consideration the actual number of sites on the protein, and also the number of residues in 'ordered' and 'disordered' regions (see Materials and Methods, and also Reviewers' Comments).
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Additional file 5:
Supplementary data S5. Extension of Figure 2A (see Reviewers' Comments).
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