Skip Navigation


Nucleic Acids Research Advance Access originally published online on November 16, 2006
Nucleic Acids Research 2007 35(Database issue):D229-D231; doi:10.1093/nar/gkl922
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (1236K) Freely available
Right arrow Screen PDF (245K) Freely available
Right arrowOA All Versions of this Article:
35/suppl_1/D229    most recent
gkl922v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Zanzoni, A.
Right arrow Articles by Helmer-Citterich, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zanzoni, A.
Right arrow Articles by Helmer-Citterich, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2007, Vol. 35, Database issue D229-D231
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.


Articles

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

Andreas Zanzoni*, Gabriele Ausiello, Allegra Via, Pier Federico Gherardini and Manuela Helmer-Citterich

Centre for Molecular Bioinformatics, Department of Biology University of Rome ‘Tor Vergata’, Rome 00133, Italy

*To whom correspondence should be addressed. Tel: +39 067 259 4314; Fax: +39 062 023 500; Email: andreas{at}cbm.bio.uniroma2.it

Received August 11, 2006. Revised October 13, 2006. Accepted October 17, 2006.

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.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
BioinformaticsHome page
C.-Y. Yang, C.-H. Chang, Y.-L. Yu, T.-C. E. Lin, S.-A. Lee, C.-C. Yen, J.-M. Yang, J.-M. Lai, Y.-R. Hong, T.-L. Tseng, et al.
PhosphoPOINT: a comprehensive human kinase interactome and phospho-protein database
Bioinformatics, August 15, 2008; 24(16): i14 - i20.
[Abstract] [PDF]


Home page
Nucleic Acids ResHome page
F. Diella, C. M. Gould, C. Chica, A. Via, and T. J. Gibson
Phospho.ELM: a database of phosphorylation sites update 2008
Nucleic Acids Res., January 11, 2008; 36(suppl_1): D240 - D244.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.