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@ARTICLE{Thielmann:5170,
      author       = {Thielmann, Y. and Weiergräber, O.H. and Mohrlüder, J. and
                      Willbold, D.},
      title        = {{S}tructural framework of the {GABARAP}-calreticulin
                      interface - implications for substrate binding to
                      endoplasmic reticulum chaperones},
      journal      = {The FEBS journal},
      volume       = {276},
      issn         = {1742-464X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {PreJuSER-5170},
      pages        = {1140 - 1152},
      year         = {2009},
      note         = {The authors wish to thank Olga Dietz for excellent
                      technical assistance. O. H. WeiergrAber is grateful to Georg
                      Buldt for continuous generous support. Moreover, assistance
                      by the ESRF staff at beamline ID14-1 is acknowledged. This
                      study was supported by a research grant from the Deutsche
                      Forschungsgemeinschaft (DFG) to D. Willbold (Wi1472/5).},
      abstract     = {The 4-aminobutyrate type A receptor-associated protein
                      (GABARAP) is a versatile adaptor protein that plays an
                      important role in intracellular vesicle trafficking,
                      particularly in neuronal cells. We have investigated the
                      structural determinants underlying the interaction of
                      GABARAP with calreticulin using spectroscopic and
                      crystallographic techniques. Specifically, we present the
                      crystal structure of GABARAP in complex with its major
                      binding epitope on the chaperone. Molecular modeling of a
                      complex containing full-length calreticulin suggests a novel
                      mode of substrate interaction, which may have functional
                      implications for the calreticulin/calnexin family in
                      general.},
      keywords     = {Adaptor Proteins, Signal Transducing: chemistry / Adaptor
                      Proteins, Signal Transducing: metabolism / Calreticulin:
                      chemistry / Calreticulin: metabolism / Endoplasmic
                      Reticulum: metabolism / Humans / Microtubule-Associated
                      Proteins: chemistry / Microtubule-Associated Proteins:
                      metabolism / Models, Molecular / Molecular Chaperones:
                      chemistry / Molecular Chaperones: metabolism / Protein
                      Binding / Substrate Specificity / Adaptor Proteins, Signal
                      Transducing (NLM Chemicals) / Calreticulin (NLM Chemicals) /
                      GABARAP protein, human (NLM Chemicals) /
                      Microtubule-Associated Proteins (NLM Chemicals) / Molecular
                      Chaperones (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2 / JARA-HPC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ISB-2-20090406 / $I:(DE-82)080012_20140620$},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19154346},
      UT           = {WOS:000262666900022},
      doi          = {10.1111/j.1742-4658.2008.06857.x},
      url          = {https://juser.fz-juelich.de/record/5170},
}