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@ARTICLE{Mohrlder:60125,
      author       = {Mohrlüder, J. and Stangler, T. and Wiesehan, K. and
                      Hoffmann, Y. and Mataruga, A. and Willbold, D.},
      title        = {{I}dentification of calreticulin as ligand of {GABARAP} by
                      phage display screening of a peptide library},
      journal      = {The FEBS journal},
      volume       = {274},
      number       = {21},
      issn         = {1742-464X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {PreJuSER-60125},
      pages        = {5543 - 5555},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {4-Aminobutyrate type A (GABA(A)) receptor-associated
                      protein (GABARAP) is a ubiquitin-like modifier implicated in
                      the intracellular trafficking of GABA(A) receptors, and
                      belongs to a family of proteins involved in intracellular
                      vesicular transport processes, such as autophagy and
                      intra-Golgi transport. In this article, it is demonstrated
                      that calreticulin is a high affinity ligand of GABARAP.
                      Calreticulin, although best known for its functions as a
                      Ca(2+) -dependent chaperone and a Ca(2+) -buffering protein
                      in the endoplasmic reticulum, is also localized to the
                      cytosol and exerts a variety of extra-endoplasmic reticulum
                      functions. By phage display screening of a randomized
                      peptide library, peptides that specifically bind GABARAP
                      were identified. Their amino acid sequences allowed us to
                      identify calreticulin as a potential GABARAP binding
                      protein. GABARAP binding to calreticulin was confirmed by
                      pull-down experiments with brain lysate and colocalization
                      studies in N2a cells. Calreticulin and GABARAP interact with
                      a dissociation constant K(d) = 64 nm and a mean lifetime of
                      the complex of 20 min. Thus, the interaction between GABARAP
                      and calreticulin is the strongest so far reported for each
                      protein.},
      keywords     = {Amino Acid Motifs / Amino Acid Sequence / Animals / Binding
                      Sites / Calreticulin: chemistry / Calreticulin: metabolism /
                      Cells, Cultured / Immunohistochemistry / Ligands /
                      Microtubule-Associated Proteins: chemistry /
                      Microtubule-Associated Proteins: metabolism / Models,
                      Molecular / Molecular Sequence Data / Peptide Fragments:
                      chemistry / Peptide Fragments: metabolism / Peptide Library
                      / Rats / Surface Plasmon Resonance / Calreticulin (NLM
                      Chemicals) / GABARAP protein, rat (NLM Chemicals) / Ligands
                      (NLM Chemicals) / Microtubule-Associated Proteins (NLM
                      Chemicals) / Peptide Fragments (NLM Chemicals) / Peptide
                      Library (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2 / JARA-SIM},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB805 / I:(DE-Juel1)VDB1045},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17916189},
      UT           = {WOS:000250297600009},
      doi          = {10.1111/j.1742-4658.2007.06073.x},
      url          = {https://juser.fz-juelich.de/record/60125},
}