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Bioinformatics Advance Access originally published online on May 27, 2004
Bioinformatics 2004 20(16):2509-2512; doi:10.1093/bioinformatics/bth332
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Bioinformatics vol. 20 issue 16 © Oxford University Press 2004; all rights reserved.

Discovery Note

Data mining techniques to study the disulfide-bonding state in proteins: signal peptide is a strong descriptor

Dominique Tessier *, Benjamin Bardiaux , Colette Larré and Yves Popineau

Unité de Recherche sur les Protéines Végétales et leurs Interactions, INRA Rue de la Géraudière, BP 71627, 44316 Nantes Cedex 3, France

Received on February 4, 2004; revised on March 5, 2004; accepted on May 6, 2004
Advance Access Publication May 27, 2004

In the eucaryotic cell, the formation of disulfide bonds takes place in general inside the endoplasmic reticulum which provides a unique folding environment. The DisulfideDB database gathers information about this biological process with structural, evolutionary and neighborhood information on cysteines in proteins. Mining this information with an association rule discovery program permits to extract some strong rules for the prediction of the disulfide-bonding state of cysteines.

Supplementary information: The web supplement to this paper, including the UML diagram of the database and some procedures used with the association rule discovery tool, may be found at http://www.nantes.inra.fr/centre/unites-recherche/urpvi/bioinformatique/publi.html.

Contact: tessier{at}nantes.inra.fr

* To whom correspondence should be addressed.


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