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Florence Corpet

dblp:52/3535 · DBLP profile ↗
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4ranked-venue papers
2as first author
0since 2021 · last 2000
—ORCID · none

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

Applied, interdisciplinary, general and emerging computing · 4 · 2 first-author

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
4 papers
Bioinformatics and computational biology · 100%

Topics — the 7 heaviest of 8, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › multiple sequence alignment
multiple sequence alignment visualization
0.011999
Browsing protein families via the 'Rich Family Description' format · Bioinform. 1999
Bioinformatics and computational biology › protein sequence analysis
protein family analysis
0.011999
Browsing protein families via the 'Rich Family Description' format · Bioinform. 1999
Bioinformatics and computational biology › protein structure analysis
protein domain analysis
0.011997
XDOM, a graphical tool to analyse domain arrangements in any set of protein sequences · Comput. Appl. Biosci. 1997
Bioinformatics and computational biology › sequence analysis
RNA sequence analysis
0.011994
RNAlign program: alignment of RNA sequences using both primary and secondary structures · Comput. Appl. Biosci. 1994
Bioinformatics and computational biology
phylogenetics
0.011999
Browsing protein families via the 'Rich Family Description' format · Bioinform. 1999
Bioinformatics and computational biology
protein sequence analysis
0.011997
XDOM, a graphical tool to analyse domain arrangements in any set of protein sequences · Comput. Appl. Biosci. 1997
Bioinformatics and computational biology › RNA biology
ribosomal RNA
0.011994
RNAlign program: alignment of RNA sequences using both primary and secondary structures · Comput. Appl. Biosci. 1994

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

regular expression · 0.0profile · 0.0hidden markov model · 0.0fingerprint · 0.0phylogenetic tree computation · 0.0consensus sequence computation · 0.0sequence comparison · 0.0secondary structure alignment · 0.0dynamic programming · 0.0
YearPublicationVenuePosition
2000 InterPro-an integrated documentation resource for protein families, domains and functional sites
abstract
MOTIVATION: InterPro is a new integrated documentation resource for protein families, domains and functional sites, developed initially as a means of rationalising the complementary efforts of the PROSITE, PRINTS, Pfam and ProDom database projects. RESULTS: Merged annotations from PRINTS, PROSITE and Pfam form the InterPro core. Each combined InterPro entry includes functional descriptions and literature references, and links are made back to the relevant parent database(s), allowing users to see at a glance whether a particular family or domain has associated patterns, profiles, fingerprints, etc. Merged and individual entries (i.e. those that have no counterpart in the companion resources) are assigned unique accession numbers. Release 1.2 of InterPro (June 2000) contains over 3000 entries, representing families, domains, repeats and sites of post-translational modification (PTMs) encoded by 6581 different regular expressions, profiles, fingerprints and Hidden Markov Models (HMMs). Each InterPro entry lists all the matches against SWISS-PROT and TrEMBL (more than 1000000 hits from 264333 different proteins out of 384572 in SWISS-PROT and TrEMBL).
Rolf Apweiler, Terri K. Attwood, Amos Bairoch, Alex Bateman, Ewan Birney, Margaret Biswas, Philipp Bucher, Lorenzo Cerutti, Florence Corpet, Michael D. R. Croning, Richard Durbin, Laurent Falquet, Wolfgang Fleischmann, Jérôme Gouzy, Henning Hermjakob, Nicolas Hulo, Inge Jonassen, Daniel Kahn, Alexander Kanapin, Youla Karavidopoulou, Rodrigo Lopez, Beate Marx, Nicola J. Mulder, Thomas M. Oinn, Marco Pagni, Florence Servant, Christian J. A. Sigrist, Evgeny M. Zdobnov
Bioinform.9
1999 Browsing protein families via the 'Rich Family Description' format
abstract
Abstract Motivation: Multiple alignments of protein sequences are the basis of structural and functional analysis of protein families. It is however difficult even for an expert biologist to comprehend an alignment of more than 50 to 100 homologous sequences. Results: This paper presents a browser for the analysis of multiple alignments of large numbers of protein sequences. Phylogenetic trees and consensus sequences are computed and used to summarise the alignments; these data are stored in a structure called Rich Family Description. Summary alignments and trees are displayed in HTML pages and can be developed or reduced by the user. This browser is used to display the ProDom domain families on the Web. Its zooming facilities allow extracting information from alignments of more than 1000 homologous sequences. Availability: Programs are available free of charge on request from the authors. The ProDom database can be consulted at http://www.toulouse.inra.fr/prodom.html Contact: [email protected]
Florence Corpet, Jérôme Gouzy, Daniel Kahn
Bioinform.1
1997 XDOM, a graphical tool to analyse domain arrangements in any set of protein sequences
abstract
MOTIVATION: To extract the maximum possible information from a set of protein sequences, its modular organization must be known and clearly displayed. This is important both for structural and functional analysis. RESULTS: This paper presents an algorithm and a graphical interface called XDOM which performs a systematic analysis of the modular organization of any set of protein sequences. The algorithm is an automatic method to identify putative domains from sequence comparisons. The graphical tool displays the proteins as a set of linked boxes, corresponding to its domains. The method has been tested on a family of bacterial proteins and on whole genomes. It is currently applied to the complete SWISS-PROT database to build the PRODOM database. AVAILABILITY: XDOM is available free of charge by anonymous ftp:¿¿ftp://ftp.toulouse.inra.fr/pub/xdom¿ ¿. The ProDom database can be consulted at ¿¿http://protein.toulouse.inra.fr/prodom.html¿¿.
Jérôme Gouzy, P. Eugène, Elizabeth A. Greene, Daniel Kahn, Florence Corpet
Comput. Appl. Biosci.5
1994 RNAlign program: alignment of RNA sequences using both primary and secondary structures
abstract
We have developed an algorithm and a computer program for aligning new RNA sequences with a bank of aligned homologous RNA sequences. Given a common folding structure for the bank, the program performs an alignment between the bank and a new sequence, optimal both in terms of primary and secondary structure. This method is useful to align sequences that present a common folding structure despite extensive divergence of their primary structures. It allows these preserved regions to be precisely distinguished from domains with more variable secondary structure. An optimal alignment of a sequence of length N with a bank of homologous sequences of length M is produced in O (M2N3) time and O(M2N2) space. For sequences that are too long for an algorithm of this complexity, a proposed strategy is to use a classical alignment (using only primary structure data) then improve it with the new algorithm in the regions where the bank stems are not aligned with possible stems in the new sequence. The algorithm has been implemented in Turbo Pascal on a PC, and has been used to align RNA sequences of eubacterial large ribosomal subunit.
Florence Corpet, B. Michot
Comput. Appl. Biosci.1