TY  - JOUR
A1  - Formstecher, Etienne
A1  - Aresta, Sandra
A1  - Collura, Vincent
A1  - Hamburger, Alexandre
A1  - Meil, Alain
A1  - Trehin, Alexandra
A1  - Reverdy, Céline
A1  - Betin, Virginie
A1  - Maire, Sophie
A1  - Brun, Christine
A1  - Jacq, Bernard
A1  - Arpin, Monique
A1  - Bellaiche, Yohanns
A1  - Bellusci, Saverio
A1  - Benaroch, Philippe
A1  - Bornens, Michel
A1  - Chanet, Roland
A1  - Chavrier, Philippe
A1  - Delattre, Olivier
A1  - Doye, Valérie
A1  - Fehon, Richard
A1  - Faye, Gérard
A1  - Galli, Thierry
A1  - Girault, Jean-Antoine
A1  - Goud, Bruno
A1  - de Gunzburg, Jean
A1  - Johannes, Ludger
A1  - Junier, Marie-Pierre
A1  - Mirouse, Vincent
A1  - Mukherjee, Ashim
A1  - Papadopoulo, Dora
A1  - Perez, Franck
A1  - Plessis, Anne
A1  - Rossé, Carine
A1  - Saule, Simon
A1  - Stoppa-Lyonnet, Dominique
A1  - Vincent, Alain
A1  - White, Michael
A1  - Legrain, Pierre
A1  - Wojcik, Jérôme
A1  - Camonis, Jacques
A1  - Daviet, Laurent
T1  - Protein interaction mapping: A Drosophila case study
Y1  - 2005/03/01 
JF  - Genome Research 
JO  - Genome Research 
SP  - 376 
EP  - 384 
DO  - 10.1101/gr.2659105 
VL  - 15 
IS  - 3 
UR  - http://genome.cshlp.org/content/15/3/376.abstract 
N2  - The Drosophila (fruit fly) model system has been instrumental in our current understanding of human biology, development, and diseases. Here, we used a high-throughput yeast two-hybrid (Y2H)-based technology to screen 102 bait proteins from Drosophila melanogaster, most of them orthologous to human cancer-related and/or signaling proteins, against high-complexity fly cDNA libraries. More than 2300 protein-protein interactions (PPI) were identified, of which 710 are of high confidence. The computation of a reliability score for each protein-protein interaction and the systematic identification of the interacting domain combined with a prediction of structural/functional motifs allow the elaboration of known complexes and the identification of new ones. The full data set can be visualized using a graphical Web interface, the PIMRider (http://pim.hybrigenics.com), and is also accessible in the PSI standard Molecular Interaction data format. Our fly Protein Interaction Map (PIM) is surprisingly different from the one recently proposed by Giot et al. with little overlap between the two data sets. Analysis of the differences in data sets and methods suggests alternative strategies to enhance the accuracy and comprehensiveness of the post-genomic generation of broad-scale protein interaction maps. 
ER  -