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@ARTICLE{Huser:120175,
      author       = {R. Häuser$^*$ and A. Ceol and S. V. Rajagopala and R.
                      Mosca and G. Siszler and N. Wermke$^*$ and P. Sikorski and
                      F. Schwarz$^*$ and M. Schick$^*$ and S. Wuchty and P. Aloy
                      and P. Uetz},
      title        = {{A} second-generation protein-protein interaction network
                      of {H}elicobacter pylori.},
      journal      = {Molecular $\&$ cellular proteomics},
      volume       = {13},
      number       = {5},
      issn         = {1535-9484},
      address      = {Bethesda, Md.},
      publisher    = {The American Society for Biochemistry and Molecular
                      Biology},
      reportid     = {DKFZ-2017-00757},
      pages        = {1318 - 1329},
      year         = {2014},
      abstract     = {Helicobacter pylori infections cause gastric ulcers and
                      play a major role in the development of gastric cancer. In
                      2001, the first protein interactome was published for this
                      species, revealing over 1500 binary protein interactions
                      resulting from 261 yeast two-hybrid screens. Here we roughly
                      double the number of previously published interactions using
                      an ORFeome-based, proteome-wide yeast two-hybrid screening
                      strategy. We identified a total of 1515 protein-protein
                      interactions, of which 1461 are new. The integration of all
                      the interactions reported in H. pylori results in 3004
                      unique interactions that connect about $70\%$ of its
                      proteome. Excluding interactions of promiscuous proteins we
                      derived from our new data a core network consisting of 908
                      interactions. We compared our data set to several other
                      bacterial interactomes and experimentally benchmarked the
                      conservation of interactions using 365 protein pairs
                      (interologs) of E. coli of which one third turned out to be
                      conserved in both species.},
      keywords     = {Bacterial Proteins (NLM Chemicals) / Proteome (NLM
                      Chemicals)},
      cin          = {W150 / W110},
      ddc          = {540},
      cid          = {I:(DE-He78)W150-20160331 / I:(DE-He78)W110-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24627523},
      pmc          = {pmc:PMC4014287},
      doi          = {10.1074/mcp.O113.033571},
      url          = {https://inrepo02.dkfz.de/record/120175},
}