ArticleNucleic acids research2007
Phospho3D: a database of three-dimensional structures of protein phosphorylation sites.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Phosphopeptide Neoantigens as Emerging Targets in Cancer Immunotherapy.Journal of cancer immunology · 2024Article
- A Review of Machine Learning and Algorithmic Methods for Protein Phosphorylation Site Prediction.Genomics, proteomics & bioinformatics · 2023Review
- Current status of PTMs structural databases: applications, limitations and prospects.Amino acids · 2022Review
- The carboxy-terminus, a key regulator of protein function.Critical reviews in biochemistry and molecular biology · 2019Review
- Investigation and identification of functional post-translational modification sites associated with drug binding and protein-protein interactions.BMC systems biology · 2017Article
- Recent Advances in Substrate Identification of Protein Kinases in Plants and Their Role in Stress Management.Current genomics · 2017Review
- Selection on meiosis genes in diploid and tetraploid Arabidopsis arenosa.Molecular biology and evolution · 2015Article
- AMASS: a database for investigating protein structures.Bioinformatics (Oxford, England) · 2014Article
- Incorporating substrate sequence motifs and spatial amino acid composition to identify kinase-specific phosphorylation sites on protein three-dimensional structures.BMC bioinformatics · 2013Article
- Human Protein Reference Database and Human Proteinpedia as resources for phosphoproteome analysis.Molecular bioSystems · 2012Review
- Incorporating distant sequence features and radial basis function networks to identify ubiquitin conjugation sites.PloS one · 2011Article
- Phospho.ELM: a database of phosphorylation sites--update 2011.Nucleic acids research · 2011Article
- Phospho3D 2.0: an enhanced database of three-dimensional structures of phosphorylation sites.Nucleic acids research · 2011Article
- Visualization of macromolecular structures.Nature methods · 2010Review
- A structure filter for the Eukaryotic Linear Motif Resource.BMC bioinformatics · 2009Article
- A comprehensive resource for integrating and displaying protein post-translational modifications.BMC research notes · 2009Article
- Article
- SiteSeek: post-translational modification analysis using adaptive locality-effective kernel methods and new profiles.BMC bioinformatics · 2008Article
- Charge environments around phosphorylation sites in proteins.BMC structural biology · 2008Article
- Phospho.ELM: a database of phosphorylation sites--update 2008.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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.
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Registered trials
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