% 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{Galkin:19044,
      author       = {Galkin, V.E. and Orlova, A. and Kudryashov, D.S. and
                      Solodukhin, A. and Reisler, E. and Schröder, G.F. and
                      Egelman, E.H.},
      title        = {{R}emodeling of actin filaments by {ADF}/cofilin proteins},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {108},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-19044},
      pages        = {20568 - 20572},
      year         = {2011},
      note         = {This work was supported by National Institutes of Health
                      Grants GM081303 (E. H. E.) and GM077190 (E.R.).},
      abstract     = {Cofilin/ADF proteins play key roles in the dynamics of
                      actin, one of the most abundant and highly conserved
                      eukaryotic proteins. We used cryoelectron microscopy to
                      generate a 9-Å resolution three-dimensional reconstruction
                      of cofilin-decorated actin filaments, the highest resolution
                      achieved for a complex of F-actin with an actin-binding
                      protein. We show that the cofilin-induced change in the
                      filament twist is due to a unique conformation of the actin
                      molecule unrelated to any previously observed state. The
                      changes between the actin protomer in naked F-actin and in
                      the actin-cofilin filament are greater than the
                      conformational changes between G- and F-actin. Our results
                      show the structural plasticity of actin, suggest that other
                      actin-binding proteins may also induce large but different
                      conformational changes, and show that F-actin cannot be
                      described by a single molecular model.},
      keywords     = {Actin Depolymerizing Factors: chemistry / Actins: chemistry
                      / Cofilin 2: chemistry / Cryoelectron Microscopy: methods /
                      Cytoskeleton: chemistry / Gene Library / Humans /
                      Microscopy, Electron: methods / Models, Molecular /
                      Molecular Conformation / Muscle, Skeletal: metabolism /
                      Polymers: chemistry / Protein Conformation / Protein
                      Structure, Secondary / Actin Depolymerizing Factors (NLM
                      Chemicals) / Actins (NLM Chemicals) / Cofilin 2 (NLM
                      Chemicals) / Polymers (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22158895},
      pmc          = {pmc:PMC3251117},
      UT           = {WOS:000298289400064},
      doi          = {10.1073/pnas.1110109108},
      url          = {https://juser.fz-juelich.de/record/19044},
}