% 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{Caruso:889873,
      author       = {Caruso, Icaro P. and Guimarães, Giovana C. and Machado,
                      Vitor B. and Fossey, Marcelo A. and Willbold, Dieter and
                      Almeida, Fabio C. L. and Souza, Fátima P.},
      title        = {{B}iophysical and {D}ynamic {C}haracterization of
                      {F}ine-{T}uned {B}inding of the {H}uman {R}espiratory
                      {S}yncytial {V}irus {M}2-1 {C}ore {D}omain to {L}ong {RNA}s},
      journal      = {Journal of virology},
      volume       = {94},
      number       = {23},
      issn         = {1098-5514},
      address      = {Baltimore, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2021-00481},
      pages        = {e01505-20},
      year         = {2020},
      abstract     = {The human respiratory syncytial virus (hRSV) M2-1 protein
                      functions as a processivity and antitermination factor of
                      the viral polymerase complex. Here, the first evidence that
                      the hRSV M2-1 core domain (cdM2-1) alone has an unfolding
                      activity for long RNAs is presented and the biophysical and
                      dynamic characterization of the cdM2-1/RNA complex is
                      provided. The main contact region of cdM2-1 with RNA was the
                      α1-α2-α5-α6 helix bundle, which suffered local
                      conformational changes and promoted the RNA unfolding
                      activity. This activity may be triggered by base-pairing
                      recognition. RNA molecules wrap around the whole cdM2-1,
                      protruding their termini over the domain. The α2-α3 and
                      α3-α4 loops of cdM2-1 were marked by an increase in
                      picosecond internal motions upon RNA binding, even though
                      they are not directly involved in the interaction. The
                      results revealed that the cdM2-1/RNA complex originates from
                      a fine-tuned binding, contributing to the unraveling
                      interaction aspects necessary for M2-1 activity.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32938771},
      UT           = {WOS:000595866900011},
      doi          = {10.1128/JVI.01505-20},
      url          = {https://juser.fz-juelich.de/record/889873},
}