% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Risi:836818,
      author       = {Risi, Cristina and Eisner, Jamie and Belknap, Betty and
                      Heeley, David H. and White, Howard D. and Schröder, Gunnar
                      and Galkina, Vitold E.},
      title        = {{C}a2+-induced movement of tropomyosin on native cardiac
                      thin filaments revealed by cryoelectron microscopy},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {114},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2017-05860},
      pages        = {6782-6787},
      year         = {2017},
      abstract     = {Muscle contraction relies on the interaction of myosin
                      motors with F-actin, which is regulated through a
                      translocation of tropomyosin by the troponin complex in
                      response to Ca2+ The current model of muscle regulation
                      holds that at relaxing (low-Ca2+) conditions tropomyosin
                      blocks myosin binding sites on F-actin, whereas at
                      activating (high-Ca2+) conditions tropomyosin translocation
                      only partially exposes myosin binding sites on F-actin so
                      that binding of rigor myosin is required to fully activate
                      the thin filament (TF). Here we used a single-particle
                      approach to helical reconstruction of frozen hydrated native
                      cardiac TFs under relaxing and activating conditions to
                      reveal the azimuthal movement of the tropomyosin on the
                      surface of the native cardiac TF upon Ca2+ activation. We
                      demonstrate that at either relaxing or activating conditions
                      tropomyosin is not constrained in one structural state, but
                      rather is distributed between three structural positions on
                      the surface of the TF. We show that two of these tropomyosin
                      positions restrain actomyosin interactions, whereas in the
                      third position, which is significantly enhanced at high
                      Ca2+, tropomyosin does not block myosin binding sites on
                      F-actin. Our data provide a structural framework for the
                      enhanced activation of the cardiac TF over the skeletal TF
                      by Ca2+ and lead to a mechanistic model for the regulation
                      of the cardiac TF.},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000404108400058},
      pubmed       = {pmid:28607071},
      doi          = {10.1073/pnas.1700868114},
      url          = {https://juser.fz-juelich.de/record/836818},
}