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@ARTICLE{Schwarten:276647,
      author       = {Schwarten, Melanie and Mohrlüder, Jeannine and Ma,
                      Peixiang and Stoldt, Matthias and Thielmann, Yvonne and
                      Stangler, Thomas and Hersch, Nils and Hoffmann, Bernd and
                      Merkel, Rudolf and Willbold, Dieter},
      title        = {{N}ix directly binds to {GABARAP}: {A} possible crosstalk
                      between apoptosis and autophagy},
      journal      = {Autophagy},
      volume       = {5},
      number       = {5},
      issn         = {1554-8635},
      address      = {Abingdon, Oxon},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {FZJ-2015-06975},
      pages        = {690 - 698},
      year         = {2009},
      abstract     = {Autophagy, a pathway primarily relevant for cell survival,
                      and apoptosis, a process invariably leading to cell death,
                      are the two main mechanisms of cellular self-destruction,
                      which are essential in cell growth, neurodegeneration, tumor
                      suppression, stress and immune response. Currently, a
                      potential crosstalk between apoptosis and autophagy is
                      subject to intensive investigations since recently some
                      direct junctions became obvious. The respective
                      protein-protein interaction network, however, remains to be
                      elucidated in detail. The γ-aminobutyric acid type A
                      (GABAA) receptor-associated protein GABARAP belongs to a
                      family of proteins implicated in intracellular transport
                      events and was shown to be associated to autophagic
                      processes. Using a phage display screening against the
                      target protein GABARAP, we identified the proapoptotic
                      protein Nix/Bnip3L to be a potential GABARAP ligand. In
                      vitro binding studies, pull-down
                      analysis,coimmunoprecipitation assays and colocalization
                      studies confirmed a direct interaction of both proteins in
                      mammalian cells.},
      cin          = {ICS-6 / ICS-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)ICS-7-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19363302},
      UT           = {WOS:000268205300011},
      doi          = {10.4161/auto.5.5.8494},
      url          = {https://juser.fz-juelich.de/record/276647},
}