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@ARTICLE{Peters:474421,
      author       = {Peters, Thomas and Creutznacher, Robert and Maass, Thorben
                      and Mallagaray, Alvaro and Ogrissek, Patrick and Taube,
                      Stefan and Thiede, Lars and Uetrecht, Charlotte},
      title        = {{N}orovirus–glycan interactions — how strong are they
                      really?},
      journal      = {Biochemical Society transactions},
      volume       = {50},
      number       = {1},
      issn         = {0300-5127},
      address      = {London},
      publisher    = {Biochemical Society},
      reportid     = {PUBDB-2022-00779},
      pages        = {347 – 359},
      year         = {2022},
      abstract     = {Infection with human noroviruses requires attachment to
                      histo blood group antigens (HBGAs) via the major capsid
                      protein VP1 as a primary step. Several crystal structures of
                      VP1 protruding domain dimers, so called P-dimers, complexed
                      with different HBGAs have been solved to atomic resolution.
                      Corresponding binding affinities have been determined for
                      HBGAs and other glycans exploiting different biophysical
                      techniques, with mass spectrometry (MS) and nuclear magnetic
                      resonance (NMR) spectroscopy being most widely used.
                      However, reported binding affinities are inconsistent. At
                      the extreme, for the same system MS detects binding whereas
                      NMR spectroscopy does not, suggesting a fundamental source
                      of error. In this short essay, we will explain the reason
                      for the observed differences and compile reliable and
                      reproducible binding affinities. We will then highlight how
                      a combination of MS techniques and NMR experiments affords
                      unique insights into the process of HBGA binding by
                      norovirus capsid proteins.},
      cin          = {FS-CS / U Lübeck / CSSB-LIV/DESY-CU},
      ddc          = {540},
      cid          = {I:(DE-H253)FS-CS-20210408 / $I:(DE-H253)U_L__beck-20211012$
                      / $I:(DE-H253)CSSB-LIV_DESY-CU-20220525$},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34940787},
      UT           = {WOS:000736185200001},
      doi          = {10.1042/BST20210526},
      url          = {https://bib-pubdb1.desy.de/record/474421},
}