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Emmanuel Courcelle

dblp:77/5105 · DBLP profile ↗
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4ranked-venue papers
0as first author
0since 2021 · last 2002
—ORCID · none

Domains — the database's venue-derived domains; a paper can count in several

Applied, interdisciplinary, general and emerging computing · 4

Expertise — from the expertise taxonomy: the topics of the expert's papers under the CCF categories. A weight counts papers with recency: 1 for a paper about the topic, 0.3 when the topic is its context, halved every five years.

Interdisciplinary, comprehensive, and emerging computing
2 papers
Bioinformatics and computational biology · 100%

Topics — the 4 heaviest of 4, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › structural bioinformatics › protein structure representation
protein structure visualization
0.012002
ENDscript: a workflow to display sequence and structure information · Bioinform. 2002
Bioinformatics and computational biology
multiple sequence alignment
0.022002
ESPript: analysis of multiple sequence alignments in PostScript · Bioinform. 1999
ENDscript: a workflow to display sequence and structure information · Bioinform. 2002
Bioinformatics and computational biology › multiple sequence alignment
alignment visualization
0.011999
ESPript: analysis of multiple sequence alignments in PostScript · Bioinform. 1999
Bioinformatics and computational biology › structural bioinformatics › protein structure
protein secondary structure
0.011999
ESPript: analysis of multiple sequence alignments in PostScript · Bioinform. 1999

Methods — techniques the papers use, named apart from their topics

multalin · 0.0DSSP · 0.0BLAST · 0.0homology scoring · 0.0
YearPublicationVenuePosition
2002 InterPro: An Integrated Documentation Resource for Protein Families, Domains and Functional Sites
abstract
The exponential increase in the submission of nucleotide sequences to the nucleotide sequence database by genome sequencing centres has resulted in a need for rapid, automatic methods for classification of the resulting protein sequences. There are several signature and sequence cluster-based methods for protein classification, each resource having distinct areas of optimum application owing to the differences in the underlying analysis methods. In recognition of this, InterPro was developed as an integrated documentation resource for protein families, domains and functional sites, to rationalise the complementary efforts of the individual protein signature database projects. The member databases - PRINTS, PROSITE, Pfam, ProDom, SMART and TIGRFAMs - form the InterPro core. Related signatures from each member database are unified into single InterPro entries. Each InterPro entry includes a unique accession number, functional descriptions and literature references, and links are made back to the relevant member database(s). Release 4.0 of InterPro (November 2001) contains 4,691 entries, representing 3,532 families, 1,068 domains, 74 repeats and 15 sites of post-translational modification (PTMs) encoded by different regular expressions, profiles, fingerprints and hidden Markov models (HMMs). Each InterPro entry lists all the matches against SWISS-PROT and TrEMBL (2,141,621 InterPro hits from 586,124 SWISS-PROT and TrEMBL protein sequences). The database is freely accessible for text- and sequence-based searches.
Nicola J. Mulder, Rolf Apweiler, Terri K. Attwood, Amos Bairoch, Alex Bateman, David Binns, Margaret Biswas, Paul Bradley, Peer Bork, Philipp Bucher, Richard R. Copley, Emmanuel Courcelle, Richard Durbin, Laurent Falquet, Wolfgang Fleischmann, Jérôme Gouzy, Sam Griffiths-Jones, Daniel H. Haft, Henning Hermjakob, Nicolas Hulo, Daniel Kahn, Alexander Kanapin, Maria Krestyaninova, Rodrigo Lopez, Ivica Letunic, Sue Orchard, Marco Pagni, David Peyruc, Chris P. Ponting, Florence Servant, Christian J. A. Sigrist
Briefings Bioinform.12
2002 ProDom: Automated Clustering of Homologous Domains
abstract
The ProDom database is a comprehensive set of protein domain families automatically generated from the SWISS-PROT and TrEMBL sequence databases. An associated database, ProDom-CG, has been derived as a restriction of ProDom to completely sequenced genomes. The ProDom construction method is based on iterative PSI-BLAST searches and multiple alignments are generated for each domain family. The ProDom web server provides the user with a set of tools to visualise multiple alignments, phylogenetic trees and domain architectures of proteins, as well as a BLAST-based server to analyse new sequences for homologous domains. The comprehensive nature of ProDom makes it particularly useful to help sustain the growth of InterPro.
Florence Servant, Catherine Bru, Sébastien Carrère, Emmanuel Courcelle, Jérôme Gouzy, David Peyruc, Daniel Kahn
Briefings Bioinform.4
2002 ENDscript: a workflow to display sequence and structure information
abstract
UNLABELLED: ENDscript is a web server grouping popular programs such as BLAST, Multalin and DSSP. It uses as query the co-ordinates file of a protein in Protein Data Bank format and generates PostScript and png figures showing: residues conserved after a multiple alignment against homologous sequences, secondary structure elements, accessibility, hydropathy and intermolecular contacts. Thus, the user can relate quickly 1D, 2D and 3D information of a protein of known structure. AVAILABILITY: http://genopole.toulouse.inra.fr/ENDscript
Patrice Gouet, Emmanuel Courcelle
Bioinform.2
1999 ESPript: analysis of multiple sequence alignments in PostScript
abstract
MOTIVATION: The program ESPript (Easy Sequencing in PostScript) allows the rapid visualization, via PostScript output, of sequences aligned with popular programs such as CLUSTAL-W or GCG PILEUP. It can read secondary structure files (such as that created by the program DSSP) to produce a synthesis of both sequence and structural information. RESULTS: ESPript can be run via a command file or a friendly html-based user interface. The program calculates an homology score by columns of residues and can sort this calculation by groups of sequences. It offers a palette of markers to highlight important regions in the alignment. ESPript can also paste information on residue conservation into coordinate files, for subsequent visualization with a graphics program. AVAILABILITY: ESPript can be accessed on its Web site at http://www.ipbs.fr/ESPript. Sources and helpfiles can be downloaded via anonymous ftp from ftp.ipbs.fr. A tar file is held in the directory pub/ESPript.
Patrice Gouet, Emmanuel Courcelle, D. I. Stuart, F. Metoz
Bioinform.2