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@ARTICLE{Michel:280772,
      author       = {Michel, Max and Schwarten, Melanie and Decker, Christina
                      and Nagel-Steger, Luitgard and Willbold, Dieter and
                      Weiergräber, Oliver H.},
      title        = {{T}he mammalian autophagy initiator complex contains 2
                      {HORMA} domain proteins.},
      journal      = {Autophagy},
      volume       = {11},
      number       = {12},
      issn         = {1554-8635},
      address      = {Abingdon, Oxon},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {FZJ-2016-00528},
      pages        = {2300 - 2308},
      year         = {2015},
      abstract     = {ATG101 is an essential component of the ULK complex
                      responsible for initiating cellular autophagy in mammalian
                      cells; its 3-dimensional structure and molecular function,
                      however, are currently unclear. Here we present the X-ray
                      structure of human ATG101. The protein displays an open
                      HORMA domain fold. Both structural properties and
                      biophysical evidence indicate that ATG101 is locked in this
                      conformation, in contrast to the prototypical HORMA domain
                      protein MAD2. Moreover, we discuss a potential mode of
                      dimerization with ATG13 as a fundamental aspect of ATG101
                      function.},
      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},
      pubmed       = {pmid:26236954},
      UT           = {WOS:000367806300014},
      doi          = {10.1080/15548627.2015.1076605},
      url          = {https://juser.fz-juelich.de/record/280772},
}