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@ARTICLE{Ma:276569,
      author       = {Ma, Peixiang and Schillinger, Oliver and Schwarten, Melanie
                      and Lecher, Justin and Hartmann, Rudolf and Stoldt, Matthias
                      and Mohrlüder, Jeannine and Olubiyi, Olujide and Strodel,
                      Birgit and Willbold, Dieter and Weiergräber, Oliver H.},
      title        = {{C}onformational {P}olymorphism in {A}utophagy-{R}elated
                      {P}rotein {GATE}-16},
      journal      = {Biochemistry},
      volume       = {54},
      number       = {35},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2015-06934},
      pages        = {5469 - 5479},
      year         = {2015},
      abstract     = {Autophagy is a fundamental homeostatic process in
                      eukaryotic organisms, fulfilling essential roles in
                      development and adaptation to stress. Among other factors,
                      formation of autophagosomes critically depends on proteins
                      of the Atg8 (autophagy-related protein 8) family, which are
                      reversibly conjugated to membrane lipids. We have applied
                      Xray crystallography, nuclear magnetic resonance
                      spectroscopy, and molecular dynamics simulations to study
                      the conformational dynamics of Atg8-type proteins, using
                      GATE-16 (Golgiassociated ATPase enhancer of 16 kDa), also
                      known as GABARAPL2, as a model system. This combination of
                      complementary approaches provides new insight into a
                      structural transition centered on the C-terminus, which is
                      crucial for the biological activity of these proteins.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000361086500009},
      pubmed       = {pmid:26284781},
      doi          = {10.1021/acs.biochem.5b00366},
      url          = {https://juser.fz-juelich.de/record/276569},
}