% 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{Bianchi:859105,
      author       = {Bianchi, Federico and Comez, Lucia and Biehl, Ralf and
                      D’Amico, Francesco and Gessini, Alessandro and Longo,
                      Marialucia and Masciovecchio, Claudio and Petrillo, Caterina
                      and Radulescu, Aurel and Rossi, Barbara and Sacchetti,
                      Francesco and Sebastiani, Federico and Violini, Nicolo and
                      Paciaroni, Alessandro},
      title        = {{S}tructure of human telomere {G}-quadruplex in the
                      presence of a model drug along the thermal unfolding
                      pathway},
      journal      = {Nucleic acids research},
      volume       = {46},
      number       = {22},
      issn         = {0301-5610},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2019-00049},
      pages        = {11927 - 11938},
      year         = {2018},
      abstract     = {A multi-technique approach, combining circular dichroism
                      spectroscopy, ultraviolet resonance Raman spectroscopy and
                      small angle scattering techniques, has been deployed to
                      elucidate how the structural features of the human telomeric
                      G-quadruplex d[A(GGGTTA)3GGG] (Tel22) change upon thermal
                      unfolding. The system is studied both in the free form and
                      when it is bound to Actinomycin D (ActD), an anticancer
                      ligand with remarkable conformational flexibility. We find
                      that at room temperature binding of Tel22 with ActD involves
                      end-stacking upon the terminal G-tetrad. Structural evidence
                      for drug-driven dimerization of a significant fraction of
                      the G-quadruplexes is provided. When the temperature is
                      raised, both free and bound Tel22 undergo melting through a
                      multi-state process. We show that in the intermediate states
                      of Tel22 the conformational equilibrium is shifted toward
                      the (3+1) hybrid-type, while a parallel structure is
                      promoted in the complex. The unfolded state of the free
                      Tel22 is consistent with a self-avoiding random-coil
                      conformation, whereas the high-temperature state of the
                      complex is observed to assume a quite compact form. Such an
                      unprecedented high-temperature arrangement is caused by the
                      persistent interaction between Tel22 and ActD, which
                      stabilizes compact conformations even in the presence of
                      large thermal structural fluctuations.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G15 /
                      G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30407585},
      UT           = {WOS:000456714000026},
      doi          = {10.1093/nar/gky1092},
      url          = {https://juser.fz-juelich.de/record/859105},
}