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@ARTICLE{Fedorov:93921,
      author       = {Fedorov, Roman and Böhl, Markus and Tsiavaliaris, Georgios
                      and Hartmann, Falk K and Taft, Manuel H and Baruch, Petra
                      and Brenner, Bernhard and Martin, René and Knölker,
                      Hans-Joachim and Gutzeit, Herwig O and Manstein, Dietmar J
                      and DESY},
      title        = {{T}he mechanism of pentabromopseudilin inhibition of myosin
                      motor activity},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {16},
      number       = {1},
      issn         = {1072-8368},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {PHPPUBDB-11987},
      pages        = {80 - 88},
      year         = {2009},
      note         = {©Nature America, INC},
      abstract     = {We have identified pentabromopseudilin (PBP) as a potent
                      inhibitor of myosin-dependent processes such as isometric
                      tension development and unloaded shortening velocity.
                      PBP-induced reductions in the rate constants for ATP
                      binding, ATP hydrolysis and ADP dissociation extend the time
                      required per myosin ATPase cycle in the absence and presence
                      of actin. Additionally, coupling between the actin and
                      nucleotide binding sites is reduced in the presence of the
                      inhibitor. The selectivity of PBP differs from that observed
                      with other myosin inhibitors. To elucidate the binding mode
                      of PBP, we crystallized the Dictyostelium myosin-2 motor
                      domain in the presence of Mg2+-ADP–meta-vanadate and PBP.
                      The electron density for PBP is unambiguous and shows PBP to
                      bind at a previously unknown allosteric site near the tip of
                      the 50-kDa domain, at a distance of 16 Å from the
                      nucleotide binding site and 7.5 Å away from the
                      blebbistatin binding pocket.},
      cin          = {EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:00},
      pubmed       = {pmid:19122661},
      doi          = {10.1038/nsmb.1542},
      url          = {https://bib-pubdb1.desy.de/record/93921},
}