Cargando…
Phospho3D: a database of three-dimensional structures of protein phosphorylation sites
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 com...
Autores principales: | Zanzoni, Andreas, Ausiello, Gabriele, Via, Allegra, Gherardini, Pier Federico, Helmer-Citterich, Manuela |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1669737/ https://www.ncbi.nlm.nih.gov/pubmed/17142231 http://dx.doi.org/10.1093/nar/gkl922 |
Ejemplares similares
-
Phospho3D 2.0: an enhanced database of three-dimensional structures of phosphorylation sites
por: Zanzoni, Andreas, et al.
Publicado: (2011) -
pdbFun: mass selection and fast comparison of annotated PDB residues
por: Ausiello, Gabriele, et al.
Publicado: (2005) -
Phosphate binding sites identification in protein structures
por: Parca, Luca, et al.
Publicado: (2011) -
FunClust: a web server for the identification of structural motifs in a set of non-homologous protein structures
por: Ausiello, Gabriele, et al.
Publicado: (2008) -
A Proteome-wide Domain-centric Perspective on Protein Phosphorylation
por: Palmeri, Antonio, et al.
Publicado: (2014)