A comparative proteomics resource: proteins of Arabidopsis thaliana
Open Access
- 28 July 2003
- journal article
- research article
- Published by Springer Nature in Genome Biology
- Vol. 4 (8) , R51
- https://doi.org/10.1186/gb-2003-4-8-r51
Abstract
Using an integrative genome annotation pipeline (iGAP) for proteome-wide protein structure and functional domain assignment, we analyzed all the proteins of Arabidopsis thaliana. Three-dimensional structures at the level of the domain are assigned by fold recognition and threading based on a novel fold library that extends common domain classifications. iGAP is being applied to proteins from all available proteomes as part of a comparative proteomics resource. The database is accessible from the web.Keywords
This publication has 35 references indexed in Scilit:
- PDP: protein domain parserBioinformatics, 2003
- Gene3D: Structural Assignment for Whole Genes and Genomes Using the CATH Domain Structure DatabaseGenome Research, 2002
- Apoptotic Molecular Machinery: Vastly Increased Complexity in Vertebrates Revealed by Genome ComparisonsScience, 2001
- Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. ThorntonJournal of Molecular Biology, 2000
- The GeneQuiz Web server: protein functional analysis through the WebTrends in Biochemical Sciences, 2000
- Alignment algorithm for homology modeling and threadingProtein Science, 1998
- Profile hidden Markov models.Bioinformatics, 1998
- Gapped BLAST and PSI-BLAST: a new generation of protein database search programsNucleic Acids Research, 1997
- A putative modular domain present in diverse signaling proteinsCell, 1993
- Predicting Coiled Coils from Protein SequencesScience, 1991