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@ARTICLE{Shvetsov:878184,
      author       = {Shvetsov, A. V. and Lebedev, D. V. and Zabrodskaya, Y. A.
                      and Shaldzhyan, A. A. and Egorova, M. A. and Vinogradova, D.
                      S. and Konevega, A. L. and Gorshkov, A. N. and Ramsay, E. S.
                      and Radulescu, Aurel and Sergeeva, M. V. and Plotnikova, M.
                      A. and Komissarov, A. B. and Taraskin, A. S. and Lebedev, K.
                      I. and Garmay, Yu. P. and Kuznetsov, V. V. and Isaev-Ivanov,
                      V. V. and Vasin, A. V. and Tsybalova, L. M. and Egorov, V.
                      V.},
      title        = {{C}old and distant: structural features of the
                      nucleoprotein complex of a cold-adapted influenza {A} virus
                      strain},
      journal      = {Journal of biomolecular structure $\&$ dynamics},
      volume       = {39},
      number       = {12},
      issn         = {0739-1102},
      address      = {Abingdon [u.a.]},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {FZJ-2020-02672},
      pages        = {4375-4384},
      year         = {2021},
      abstract     = {Two influenza A nucleoprotein variants (wild-type: G102R;
                      and mutant: G102R and E292G) were studied with regard to
                      macro-molecular interactions in oligomeric form (24-mers).
                      The E292G mutation has been previously shown to provide cold
                      adaptation. Molecular dynamics simulations of these
                      complexes and trajectory analysis showed that the most
                      significant difference between the obtained models was
                      distance between nucleoprotein complex strands. The isolated
                      complexes of two ribonucleoprotein variants were
                      characterized by transmission electron microscopy and
                      differential scanning fluorimetry (DSF). Presence of the
                      E292G substitution was shown by DSF to affect nucleoprotein
                      complex melting temperature. In the filament interface
                      peptide model, it was shown that the peptide corresponding
                      in primary structure to the wild-type NP (SGYDFEREGYS) is
                      prone to temperature-dependent self-association, unlike the
                      peptide corresponding to E292G substitution (SGYDFGREGYS).
                      It was also shown that the SGYDFEREGYS peptide is capable of
                      interacting with a monomeric nucleoprotein (wild type); this
                      interaction’s equilibrium dissociation constant is five
                      orders of magnitude lower than for the SGYDFGREGYS peptide.
                      Using small-angle neutron scattering (SANS), the
                      supramolecular structures of isolated complexes of these
                      proteins were studied at temperatures of 15, 32, and
                      37 °C. SANS data show that the structures of the studied
                      complexes at elevated temperature differ from the rod-like
                      particle model and react differently to temperature changes.
                      The data suggest that the mechanism behind cold adaptation
                      with E292G is associated with a weakening of the interaction
                      between strands of the ribonucleoprotein complex and, as a
                      result, the appearance of inter-chain interface flexibility
                      necessary for complex function at low temperature.},
      cin          = {JCNS-FRM-II / MLZ / JCNS-4},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-4-20201012},
      pnm          = {632 - Materials – Quantum, Complex and Functional
                      Materials (POF4-632) / 6G4 - Jülich Centre for Neutron
                      Research (JCNS) (FZJ) (POF4-6G4)},
      pid          = {G:(DE-HGF)POF4-632 / G:(DE-HGF)POF4-6G4},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101 / EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32490728},
      UT           = {WOS:000544776000001},
      doi          = {10.1080/07391102.2020.1776636},
      url          = {https://juser.fz-juelich.de/record/878184},
}