RT Journal
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
JF Genome Research 
JO Genome Research 
YR 2005 
FD March 01 
VO 15 
IS 3 
SP 376 
OP 384 
DO 10.1101/gr.2659105 
UL http://genome.cshlp.org/content/15/3/376.abstract 
AB 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.