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@ARTICLE{Krichel:281360,
      author       = {Krichel, Carsten and Weiergräber, Oliver H. and Pavlidou,
                      Marina and Mohrlüder, Jeannine and Schwarten, Melanie and
                      Willbold, Dieter and Neudecker, Philipp},
      title        = {{S}equence-specific $^{1}${H}, $^{15}${N}, and $^{13}${C}
                      resonance assignments of the autophagy-related protein
                      {LC}$_{3}${C}},
      journal      = {Biomolecular NMR assignments},
      volume       = {10},
      number       = {1},
      issn         = {1874-270X},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Netherlands},
      reportid     = {FZJ-2016-01057},
      pages        = {41-43},
      year         = {2016},
      abstract     = {Autophagy is a versatile catabolic pathway for lysosomal
                      degradation of cytoplasmic material. While the
                      phenomenological and molecular characteristics of autophagic
                      non-selective (bulk) decomposition have been investigated
                      for decades, the focus of interest is increasingly shifting
                      towards the selective mechanisms of autophagy. Both,
                      selective as well as bulk autophagy critically depend on
                      ubiquitin-like modifiers belonging to the Atg8
                      (autophagy-related 8) protein family. During evolution, Atg8
                      has diversified into eight different human genes. While all
                      human homologues participate in the formation of
                      autophagosomal membrane compartments, microtubule-associated
                      protein light chain 3C (LC3C) additionally plays a unique
                      role in selective autophagic clearance of intracellular
                      pathogens (xenophagy), which relies on specific
                      protein–protein recognition events mediated by conserved
                      motifs. The sequence-specific 1H, 15N, and 13C resonance
                      assignments presented here form the stepping stone to
                      investigate the high-resolution structure and dynamics of
                      LC3C and to delineate LC3C’s complex network of molecular
                      interactions with the autophagic machinery by NMR
                      spectroscopy.},
      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:000372227900007},
      pubmed       = {pmid:26280529},
      doi          = {10.1007/s12104-015-9633-z},
      url          = {https://juser.fz-juelich.de/record/281360},
}