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Titolo:
The protein-protein interaction map of Helicobacter pylori
Autore:
Rain, JC; Selig, L; De Reuse, H; Battaglia, V; Reverdy, C; Simon, S; Lenzen, G; Petel, F; Wojcik, J; Schachter, V; Chemama, Y; Labigne, A; Legrain, P;
Indirizzi:
Hybrigen SA, F-75012 Paris, France Hybrigen SA Paris France F-75012Hybrigen SA, F-75012 Paris, France Inst Pasteur, UnitePathogenie Bacterienne Muqueuses, F-75724 Paris 15, France Inst Pasteur Paris France 15 erienne Muqueuses, F-75724 Paris 15, France
Titolo Testata:
NATURE
fascicolo: 6817, volume: 409, anno: 2001,
pagine: 211 - 215
SICI:
0028-0836(20010111)409:6817<211:TPIMOH>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; COMPLETE GENOME; RNA-POLYMERASE; SEQUENCE; YEAST;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Legrain, P Hybrigen SA, 180 Ave Daumesnil, F-75012 Paris, France Hybrigen SA 180 Ave Daumesnil Paris France F-75012 ris, France
Citazione:
J.C. Rain et al., "The protein-protein interaction map of Helicobacter pylori", NATURE, 409(6817), 2001, pp. 211-215

Abstract

With the availability of complete DNA sequences for many prokaryotic and eukaryotic genomes, and soon for the human genome itself, it is important todevelop reliable proteome-wide approaches for a better understanding of protein function(1). As elementary constituents of cellular protein complexesand pathways, protein-protein interactions are key determinants of proteinfunction. Here we have built a large-scale protein-protein interaction mapof the human gastric pathogen Helicobacter pylori. We have used a high-throughput strategy of the yeast two-hybrid assay to screen 261 H. pylori proteins against a highly complex library of genome-encoded polypeptides(2). Over 1,200 interactions were identired between H. pylori proteins, connecting46.6% of the proteome. The determination of a reliability score for every single protein-protein interaction and the identification of the actual interacting domains permitted the assignment of unannotated proteins to biological pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 12:59:50