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@ARTICLE{Rajagopala:132592,
      author       = {S. V. Rajagopala and P. Sikorski and A. Kumar and R. Mosca
                      and J. Vlasblom and R. Arnold and J. Franca-Koh and S. B.
                      Pakala and S. Phanse and A. Ceol and R. Häuser$^*$ and G.
                      Siszler$^*$ and S. Wuchty and A. Emili and M. Babu and P.
                      Aloy and R. Pieper and P. Uetz},
      title        = {{T}he binary protein-protein interaction landscape of
                      {E}scherichia coli.},
      journal      = {Nature biotechnology},
      volume       = {32},
      number       = {3},
      issn         = {1546-1696},
      address      = {New York, NY},
      publisher    = {Nature America},
      reportid     = {DKFZ-2018-00256},
      pages        = {285 - 290},
      year         = {2014},
      abstract     = {Efforts to map the Escherichia coli interactome have
                      identified several hundred macromolecular complexes, but
                      direct binary protein-protein interactions (PPIs) have not
                      been surveyed on a large scale. Here we performed yeast
                      two-hybrid screens of 3,305 baits against 3,606 preys
                      $(∼70\%$ of the E. coli proteome) in duplicate to generate
                      a map of 2,234 interactions, which approximately doubles the
                      number of known binary PPIs in E. coli. Integration of
                      binary PPI and genetic-interaction data revealed functional
                      dependencies among components involved in cellular
                      processes, including envelope integrity, flagellum assembly
                      and protein quality control. Many of the binary interactions
                      that we could map in multiprotein complexes were informative
                      regarding internal topology of complexes and indicated that
                      interactions in complexes are substantially more conserved
                      than those interactions connecting different complexes. This
                      resource will be useful for inferring bacterial gene
                      function and provides a draft reference of the basic
                      physical wiring network of this evolutionarily important
                      model microbe.},
      keywords     = {Escherichia coli Proteins (NLM Chemicals)},
      cin          = {W150},
      ddc          = {570},
      cid          = {I:(DE-He78)W150-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24561554},
      pmc          = {pmc:PMC4123855},
      doi          = {10.1038/nbt.2831},
      url          = {https://inrepo02.dkfz.de/record/132592},
}