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@ARTICLE{Aladag:153336,
      author       = {Aladag, Amine and Hoffmann, Silke and Stoldt, Matthias and
                      Bösing, Christina and Willbold, Dieter and Schwarten,
                      Melanie},
      title        = {{H}epatitis {C} virus {NS}5{A} is able to competitively
                      displace c-{M}yc from the {B}in1 {SH}3 domain in vitro},
      journal      = {Journal of peptide science},
      volume       = {20},
      number       = {5},
      issn         = {1075-2617},
      address      = {New York, NY [u.a.]},
      publisher    = {Wiley},
      reportid     = {FZJ-2014-02968},
      pages        = {334 - 340},
      year         = {2014},
      abstract     = {We studied the interaction of the SH3 domain of Bin1 with a
                      15-mer peptide of HCV NS5A and show its potency to
                      competitively displace a 15-mer human c-Myc fragment, which
                      is a physiological ligand of Bin1, using NMR spectroscopy.
                      Fluorescence spectroscopy and ITC were employed to determine
                      the affinity of Bin1 SH3 to NS5A(347–361), yielding a
                      submicromolar affinity to NS5A. Our study compares the
                      binding dynamics and affinities of the relevant regions for
                      binding of c-Myc and NS5A to Bin1 SH3. The result gives
                      further insights into the potential role of NS5A in
                      Bin1-mediated apoptosis.Copyright © 2014 European Peptide
                      Society and John Wiley $\&$ Sons, Ltd.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000334824900004},
      pubmed       = {pmid:24616074},
      doi          = {10.1002/psc.2618},
      url          = {https://juser.fz-juelich.de/record/153336},
}