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Featured researches published by Sandra Orchard.


Nucleic Acids Research | 2010

The IntAct molecular interaction database in 2010

Samuel Kerrien; Bruno Aranda; L Breuza; Alan Bridge; Fiona Broackes-Carter; Carol Chen; Margaret Duesbury; Marine Dumousseau; Marc Feuermann; Ursula Hinz; Christine Jandrasits; Rafael C. Jimenez; Jyoti Khadake; Usha Mahadevan; Patrick Masson; Ivo Pedruzzi; Eric Pfeiffenberger; Pablo Porras; Arathi Raghunath; Bernd Roechert; Sandra Orchard; Henning Hermjakob

IntAct is an open-source, open data molecular interaction database populated by data either curated from the literature or from direct data depositions. Two levels of curation are now available within the database, with both IMEx-level annotation and less detailed MIMIx-compatible entries currently supported. As from September 2011, IntAct contains approximately 275 000 curated binary interaction evidences from over 5000 publications. The IntAct website has been improved to enhance the search process and in particular the graphical display of the results. New data download formats are also available, which will facilitate the inclusion of IntActs data in the Semantic Web. IntAct is an active contributor to the IMEx consortium (http://www.imexconsortium.org). IntAct source code and data are freely available at http://www.ebi.ac.uk/intact.


Nucleic Acids Research | 2007

IntAct—open source resource for molecular interaction data

Samuel Kerrien; Yasmin Alam-Faruque; Bruno Aranda; I. Bancarz; Alan Bridge; C. Derow; Emily Dimmer; Marc Feuermann; A. Friedrichsen; Rachael P. Huntley; C. Kohler; Jyoti Khadake; Catherine Leroy; A. Liban; C. Lieftink; Luisa Montecchi-Palazzi; Sandra Orchard; Judith E. Risse; Karine Robbe; Bernd Roechert; David Thorneycroft; Y. Zhang; Rolf Apweiler; Henning Hermjakob

IntAct is an open source database and software suite for modeling, storing and analyzing molecular interaction data. The data available in the database originates entirely from published literature and is manually annotated by expert biologists to a high level of detail, including experimental methods, conditions and interacting domains. The database features over 126 000 binary interactions extracted from over 2100 scientific publications and makes extensive use of controlled vocabularies. The web site provides tools allowing users to search, visualize and download data from the repository. IntAct supports and encourages local installations as well as direct data submission and curation collaborations. IntAct source code and data are freely available from .


Nucleic Acids Research | 2004

IntAct: an open source molecular interaction database

Henning Hermjakob; Luisa Montecchi-Palazzi; Chris Lewington; Sugath Mudali; Samuel Kerrien; Sandra Orchard; Martin Vingron; Bernd Roechert; Peter Roepstorff; Alfonso Valencia; Hanah Margalit; John Armstrong; Amos Marc Bairoch; Gianni Cesareni; David James Sherman; Rolf Apweiler

IntAct provides an open source database and toolkit for the storage, presentation and analysis of protein interactions. The web interface provides both textual and graphical representations of protein interactions, and allows exploring interaction networks in the context of the GO annotations of the interacting proteins. A web service allows direct computational access to retrieve interaction networks in XML format. IntAct currently contains approximately 2200 binary and complex interactions imported from the literature and curated in collaboration with the Swiss-Prot team, making intensive use of controlled vocabularies to ensure data consistency. All IntAct software, data and controlled vocabularies are available at http://www.ebi.ac.uk/intact.


Nucleic Acids Research | 2004

InterPro, progress and status in 2005

Nicola Mulder; Rolf Apweiler; Teresa K. Attwood; Amos Marc Bairoch; Alex Bateman; David Binns; Paul Bradley; Peer Bork; Phillip Bucher; Lorenzo Cerutti; Richard R. Copley; Emmanuel Courcelle; Ujjwal Das; Richard Durbin; Wolfgang Fleischmann; Julian Gough; Daniel H. Haft; Nicola Harte; Nicolas Hulo; Daniel Kahn; Alexander Kanapin; Maria Krestyaninova; David M. Lonsdale; Rodrigo Lopez; Ivica Letunic; John Maslen; Jennifer McDowall; Alex L. Mitchell; Anastasia N. Nikolskaya; Sandra Orchard

InterPro, an integrated documentation resource of protein families, domains and functional sites, was created to integrate the major protein signature databases. Currently, it includes PROSITE, Pfam, PRINTS, ProDom, SMART, TIGRFAMs, PIRSF and SUPERFAMILY. Signatures are manually integrated into InterPro entries that are curated to provide biological and functional information. Annotation is provided in an abstract, Gene Ontology mapping and links to specialized databases. New features of InterPro include extended protein match views, taxonomic range information and protein 3D structure data. One of the new match views is the InterPro Domain Architecture view, which shows the domain composition of protein matches. Two new entry types were introduced to better describe InterPro entries: these are active site and binding site. PIRSF and the structure-based SUPERFAMILY are the latest member databases to join InterPro, and CATH and PANTHER are soon to be integrated. InterPro release 8.0 contains 11 007 entries, representing 2573 domains, 8166 families, 201 repeats, 26 active sites, 21 binding sites and 20 post-translational modification sites. InterPro covers over 78% of all proteins in the Swiss-Prot and TrEMBL components of UniProt. The database is available for text- and sequence-based searches via a webserver (http://www.ebi.ac.uk/interpro), and for download by anonymous FTP (ftp://ftp.ebi.ac.uk/pub/databases/interpro).


Nucleic Acids Research | 2014

The MIntAct project—IntAct as a common curation platform for 11 molecular interaction databases

Sandra Orchard; Mais G. Ammari; Bruno Aranda; L Breuza; Leonardo Briganti; Fiona Broackes-Carter; Nancy H. Campbell; Gayatri Chavali; Carol Chen; Noemi del-Toro; Margaret Duesbury; Marine Dumousseau; Eugenia Galeota; Ursula Hinz; Marta Iannuccelli; Sruthi Jagannathan; Rafael C. Jimenez; Jyoti Khadake; Astrid Lagreid; Luana Licata; Ruth C. Lovering; Birgit Meldal; Anna N. Melidoni; Mila Milagros; Daniele Peluso; Livia Perfetto; Pablo Porras; Arathi Raghunath; Sylvie Ricard-Blum; Bernd Roechert

IntAct (freely available at http://www.ebi.ac.uk/intact) is an open-source, open data molecular interaction database populated by data either curated from the literature or from direct data depositions. IntAct has developed a sophisticated web-based curation tool, capable of supporting both IMEx- and MIMIx-level curation. This tool is now utilized by multiple additional curation teams, all of whom annotate data directly into the IntAct database. Members of the IntAct team supply appropriate levels of training, perform quality control on entries and take responsibility for long-term data maintenance. Recently, the MINT and IntAct databases decided to merge their separate efforts to make optimal use of limited developer resources and maximize the curation output. All data manually curated by the MINT curators have been moved into the IntAct database at EMBL-EBI and are merged with the existing IntAct dataset. Both IntAct and MINT are active contributors to the IMEx consortium (http://www.imexconsortium.org).


Nucleic Acids Research | 2007

New developments in the InterPro database

Nicola Mulder; Rolf Apweiler; Teresa K. Attwood; Amos Marc Bairoch; Alex Bateman; David Binns; Peer Bork; Virginie Buillard; Lorenzo Cerutti; Richard R. Copley; Emmanuel Courcelle; Ujjwal Das; Louise Daugherty; Mark Dibley; Robert D. Finn; Wolfgang Fleischmann; Julian Gough; Daniel H. Haft; Nicolas Hulo; Sarah Hunter; Daniel Kahn; Alexander Kanapin; Anish Kejariwal; Alberto Labarga; Petra S. Langendijk-Genevaux; David M. Lonsdale; Rodrigo Lopez; Ivica Letunic; John Maslen; Craig McAnulla

InterPro is an integrated resource for protein families, domains and functional sites, which integrates the following protein signature databases: PROSITE, PRINTS, ProDom, Pfam, SMART, TIGRFAMs, PIRSF, SUPERFAMILY, Gene3D and PANTHER. The latter two new member databases have been integrated since the last publication in this journal. There have been several new developments in InterPro, including an additional reading field, new database links, extensions to the web interface and additional match XML files. InterPro has always provided matches to UniProtKB proteins on the website and in the match XML file on the FTP site. Additional matches to proteins in UniParc (UniProt archive) are now available for download in the new match XML files only. The latest InterPro release (13.0) contains more than 13 000 entries, covering over 78% of all proteins in UniProtKB. The database is available for text- and sequence-based searches via a webserver (), and for download by anonymous FTP (). The InterProScan search tool is now also available via a web service at .


Nature Biotechnology | 2008

Promoting coherent minimum reporting guidelines for biological and biomedical investigations: the MIBBI project

Chris F. Taylor; Dawn Field; Susanna-Assunta Sansone; Jan Aerts; Rolf Apweiler; Michael Ashburner; Catherine A. Ball; Pierre Alain Binz; Molly Bogue; Tim Booth; Alvis Brazma; Ryan R. Brinkman; Adam Clark; Eric W. Deutsch; Oliver Fiehn; Jennifer Fostel; Peter Ghazal; Frank Gibson; Tanya Gray; Graeme Grimes; John M. Hancock; Nigel Hardy; Henning Hermjakob; Randall K. Julian; Matthew Kane; Carsten Kettner; Christopher R. Kinsinger; Eugene Kolker; Martin Kuiper; Nicolas Le Novère

The Minimum Information for Biological and Biomedical Investigations (MIBBI) project aims to foster the coordinated development of minimum-information checklists and provide a resource for those exploring the range of extant checklists.


Nature Biotechnology | 2007

The minimum information required for reporting a molecular interaction experiment (MIMIx)

Sandra Orchard; Lukasz Salwinski; Samuel Kerrien; Luisa Montecchi-Palazzi; Matthias Oesterheld; Volker Stümpflen; Arnaud Ceol; Andrew Chatr-aryamontri; John Armstrong; Peter Woollard; John J. Salama; Susan Moore; Jérôme Wojcik; Gary D. Bader; Marc Vidal; Michael E. Cusick; Mark Gerstein; Anne-Claude Gavin; Giulio Superti-Furga; Jack Greenblatt; Joel S. Bader; Peter Uetz; Mike Tyers; Pierre Legrain; Stan Fields; Nicola Mulder; Michael K. Gilson; Michael Niepmann; Lyle D Burgoon; Javier De Las Rivas

A wealth of molecular interaction data is available in the literature, ranging from large-scale datasets to a single interaction confirmed by several different techniques. These data are all too often reported either as free text or in tables of variable format, and are often missing key pieces of information essential for a full understanding of the experiment. Here we propose MIMIx, the minimum information required for reporting a molecular interaction experiment. Adherence to these reporting guidelines will result in publications of increased clarity and usefulness to the scientific community and will support the rapid, systematic capture of molecular interaction data in public databases, thereby improving access to valuable interaction data.


Chemico-Biological Interactions | 2009

The SDR (Short-Chain Dehydrogenase/Reductase and Related Enzymes) Nomenclature Initiative

Bengt Persson; Yvonne Kallberg; James E. Bray; Elspeth A. Bruford; Stephen L. Dellaporta; Angelo D. Favia; Roser Gonzalez Duarte; Hans Jörnvall; K.L. Kavanagh; Natalia Y. Kedishvili; Michael Kisiela; Edmund Maser; Rebekka Mindnich; Sandra Orchard; Trevor M. Penning; Janet M. Thornton; Jerzy Adamski; U. Oppermann

Short-chain dehydrogenases/reductases (SDR) constitute one of the largest enzyme superfamilies with presently over 46,000 members. In phylogenetic comparisons, members of this superfamily show early divergence where the majority have only low pairwise sequence identity, although sharing common structural properties. The SDR enzymes are present in virtually all genomes investigated, and in humans over 70 SDR genes have been identified. In humans, these enzymes are involved in the metabolism of a large variety of compounds, including steroid hormones, prostaglandins, retinoids, lipids and xenobiotics. It is now clear that SDRs represent one of the oldest protein families and contribute to essential functions and interactions of all forms of life. As this field continues to grow rapidly, a systematic nomenclature is essential for future annotation and reference purposes. A functional subdivision of the SDR superfamily into at least 200 SDR families based upon hidden Markov models forms a suitable foundation for such a nomenclature system, which we present in this paper using human SDRs as examples.


BMC Biology | 2007

Broadening the horizon – level 2.5 of the HUPO-PSI format for molecular interactions

Samuel Kerrien; Sandra Orchard; Luisa Montecchi-Palazzi; Bruno Aranda; Antony F. Quinn; Nisha Vinod; Gary D. Bader; Ioannis Xenarios; Jérôme Wojcik; David James Sherman; Mike Tyers; John J. Salama; Susan Moore; Arnaud Ceol; Andrew Chatr-aryamontri; Matthias Oesterheld; Volker Stümpflen; Lukasz Salwinski; Jason Nerothin; Ethan Cerami; Michael E. Cusick; Marc Vidal; Michael K. Gilson; John Armstrong; Peter Woollard; Christopher W. V. Hogue; David Eisenberg; Gianni Cesareni; Rolf Apweiler; Henning Hermjakob

BackgroundMolecular interaction Information is a key resource in modern biomedical research. Publicly available data have previously been provided in a broad array of diverse formats, making access to this very difficult. The publication and wide implementation of the Human Proteome Organisation Proteomics Standards Initiative Molecular Interactions (HUPO PSI-MI) format in 2004 was a major step towards the establishment of a single, unified format by which molecular interactions should be presented, but focused purely on protein-protein interactions.ResultsThe HUPO-PSI has further developed the PSI-MI XML schema to enable the description of interactions between a wider range of molecular types, for example nucleic acids, chemical entities, and molecular complexes. Extensive details about each supported molecular interaction can now be captured, including the biological role of each molecule within that interaction, detailed description of interacting domains, and the kinetic parameters of the interaction. The format is supported by data management and analysis tools and has been adopted by major interaction data providers. Additionally, a simpler, tab-delimited format MITAB2.5 has been developed for the benefit of users who require only minimal information in an easy to access configuration.ConclusionThe PSI-MI XML2.5 and MITAB2.5 formats have been jointly developed by interaction data producers and providers from both the academic and commercial sector, and are already widely implemented and well supported by an active development community. PSI-MI XML2.5 enables the description of highly detailed molecular interaction data and facilitates data exchange between databases and users without loss of information. MITAB2.5 is a simpler format appropriate for fast Perl parsing or loading into Microsoft Excel.

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Rolf Apweiler

European Bioinformatics Institute

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Pierre-Alain Binz

Swiss Institute of Bioinformatics

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Samuel Kerrien

European Bioinformatics Institute

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Chris F. Taylor

European Bioinformatics Institute

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Marine Dumousseau

European Bioinformatics Institute

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Luisa Montecchi-Palazzi

University of Rome Tor Vergata

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