Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (278K) Freely available
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 arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by McGuffin, L. J.
Right arrow Articles by Jones, D. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McGuffin, L. J.
Right arrow Articles by Jones, D. T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2004, Vol. 32, Database issue D196-D199
© 2004 Oxford University Press

The Genomic Threading Database: a comprehensive resource for structural annotations of the genomes from key organisms

Liam J. McGuffin, Stefano A. Street, Kevin Bryson, Søren-Aksel Sørensen and David T. Jones*

Department of Computer Science, University College London, Gower Street, London WC1E 6BT, UK

*To whom correspondence should be addressed. Tel: +44 20 7679 7982; Fax: +44 20 7387 1397; Email: dtj{at}cs.ucl.ac.uk

Currently, the Genomic Threading Database (GTD) contains structural assignments for the proteins encoded within the genomes of nine eukaryotes and 101 prokaryotes. Structural annotations are carried out using a modified version of GenTHREADER, a reliable fold recognition method. The Gen THREADER annotation jobs are distributed across multiple clusters of processors using grid technology and the predictions are deposited in a relational database accessible via a web interface at http://bioinf.cs.ucl.ac.uk/GTD. Using this system, up to 84% of proteins encoded within a genome can be confidently assigned to known folds with 72% of the residues aligned. On average in the GTD, 64% of proteins encoded within a genome are confidently assigned to known folds and 58% of the residues are aligned to structures.


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
 J R Soc InterfaceHome page
G. A Reeves, D. Talavera, and J. M Thornton
Genome and proteome annotation: organization, interpretation and integration
J R Soc Interface, February 6, 2009; 6(31): 129 - 147.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
L. J. McGuffin
Intrinsic disorder prediction from the analysis of multiple protein fold recognition models
Bioinformatics, August 15, 2008; 24(16): 1798 - 1804.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
L. J. McGuffin
The ModFOLD server for the quality assessment of protein structural models
Bioinformatics, February 15, 2008; 24(4): 586 - 587.
[Abstract] [Full Text] [PDF]

Home page
 Phil Trans R Soc BHome page
K. Fleming, L. A Kelley, S. A Islam, R. M MacCallum, A. Muller, F. Pazos, and M. J.E Sternberg
The proteome: structure, function and evolution
Phil Trans R Soc B, March 29, 2006; 361(1467): 441 - 451.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
S. Han, B.-c. Lee, S. T. Yu, C.-s. Jeong, S. Lee, and D. Kim
Fold recognition by combining profile-profile alignment and support vector machine
Bioinformatics, June 1, 2005; 21(11): 2667 - 2673.
[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.