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@ARTICLE{Thielmann:7510,
      author       = {Thielmann, Y. and Weiergräber, O.H. and Ma, P. and
                      Schwarten, M. and Mohrlüder, J. and Willbold, D.},
      title        = {{C}omparative modeling of human {NSF} reveals a possible
                      binding mode of {GABARAP} and {GATE}-16},
      journal      = {Proteins},
      volume       = {77},
      issn         = {0887-3585},
      address      = {New York, NY},
      publisher    = {Wiley-Liss},
      reportid     = {PreJuSER-7510},
      pages        = {637 - 646},
      year         = {2009},
      note         = {Grant sponsor: Deutsche Forschungsgememschaft (DFG); Grant
                      number: Wil472/5.},
      abstract     = {Vesicular trafficking is an important homeostatic process
                      in eukaryotic cells which critically relies on membrane
                      fusion. One of the essential components of the universal
                      membrane fusion machinery is NSF (N-ethylmaleimide-sensitive
                      factor), a large hexameric ATPase involved in disassembly of
                      SNARE (soluble NSF attachment protein receptor) complexes.
                      To improve our understanding of this sophisticated molecular
                      machine, we have modeled the structure of the NSF hexamer in
                      two alternative assemblies. Our data suggest a mechanistic
                      concept of the operating mode of NSF which helps to explain
                      the functional impact of post-translational modifications
                      and mutations reported previously. Furthermore, we propose a
                      binding site for the ubiquitin-like proteins GABARAP and
                      GATE-16, which is supported by experimental evidence,
                      yielding a complex with favorable surface complementarity.},
      keywords     = {Adaptor Proteins, Signal Transducing: chemistry / Adenosine
                      Triphosphate: chemistry / Binding Sites / Humans /
                      Hydrolysis / Microfilament Proteins: chemistry /
                      Microtubule-Associated Proteins: chemistry / Models,
                      Molecular / N-Ethylmaleimide-Sensitive Proteins: chemistry /
                      Peptides: chemistry / Phosphorylation / Protein Binding /
                      Protein Conformation / Protein Interaction Mapping / Protein
                      Structure, Tertiary / Ubiquitin: chemistry / Adaptor
                      Proteins, Signal Transducing (NLM Chemicals) / GABARAP
                      protein, human (NLM Chemicals) / GABARAPL2 protein, human
                      (NLM Chemicals) / Microfilament Proteins (NLM Chemicals) /
                      Microtubule-Associated Proteins (NLM Chemicals) / Peptides
                      (NLM Chemicals) / Ubiquitin (NLM Chemicals) / Adenosine
                      Triphosphate (NLM Chemicals) / N-Ethylmaleimide-Sensitive
                      Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19533740},
      UT           = {WOS:000270849900013},
      doi          = {10.1002/prot.22477},
      url          = {https://juser.fz-juelich.de/record/7510},
}