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• W2117936420 abstract "Phosphorylation is the most common protein post-translational modification. Phosphorylated residues (serine, threonine and tyrosine) play critical roles in the regulation of many cellular processes. Since the amount of data produced by screening assays is growing continuously, the development of computational tools for collecting and analysing experimental data has become a pivotal task for unravelling the complex network of interactions regulating eukaryotic cell life. Here we present Phospho3D, Author Webpage, a database of 3D structures of phosphorylation sites, which stores information retrieved from the phospho.ELM database and is enriched with structural information and annotations at the residue level. The database also collects the results of a large-scale structural comparison procedure providing clues for the identification of new putative phosphorylation sites." @default.
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• W2117936420 date "2007-01-03" @default.
• W2117936420 modified "2023-10-03" @default.
• W2117936420 title "Phospho3D: a database of three-dimensional structures of protein phosphorylation sites" @default.
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• W2117936420 doi "https://doi.org/10.1093/nar/gkl922" @default.
• W2117936420 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1669737" @default.
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