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, http://cbm.bio.uniroma2.it/phospho3d, 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.

Zanzoni, A., Ausiello, G., Via, A., Gherardini, P., HELMER CITTERICH, M. (2007). Phospho3D: a database of three-dimensional structures of protein phosphorylation sites. NUCLEIC ACIDS RESEARCH, 35(Database issue), D229-D231 [10.1093/nar/gkl922].

Phospho3D: a database of three-dimensional structures of protein phosphorylation sites

AUSIELLO, GABRIELE;Gherardini, PF;HELMER CITTERICH, MANUELA
2007-01-01

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, http://cbm.bio.uniroma2.it/phospho3d, 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.
1-gen-2007
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/11 - BIOLOGIA MOLECOLARE
English
Con Impact Factor ISI
Models, Molecular; Phosphoproteins; User-Computer Interface; Protein Conformation; Phosphorylation; Databases, Protein; Internet
http://nar.oxfordjournals.org/content/35/suppl_1/D229.full
Zanzoni, A., Ausiello, G., Via, A., Gherardini, P., HELMER CITTERICH, M. (2007). Phospho3D: a database of three-dimensional structures of protein phosphorylation sites. NUCLEIC ACIDS RESEARCH, 35(Database issue), D229-D231 [10.1093/nar/gkl922].
Zanzoni, A; Ausiello, G; Via, A; Gherardini, P; HELMER CITTERICH, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/14722
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