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@ARTICLE{StencelBaerenwald:202141,
      author       = {Stencel-Baerenwald, Jennifer E and Reiss, Kerstin and
                      Reiter, Dirk M and Stehle, Thilo and Dermody, Terence S},
      title        = {{T}he sweet spot: defining virus-sialic acid interactions},
      journal      = {Nature reviews / Microbiology},
      volume       = {12},
      number       = {11},
      issn         = {1740-1534},
      address      = {Basingstoke},
      publisher    = {Nature Publ. Group},
      reportid     = {FZJ-2015-04430},
      pages        = {739 - 749},
      year         = {2014},
      abstract     = {Viral infections are initiated by attachment of the virus
                      to host cell surface receptors, including sialic
                      acid-containing glycans. It is now possible to rapidly
                      identify specific glycan receptors using glycan array
                      screening, to define atomic-level structures of virus-glycan
                      complexes and to alter the glycan-binding site to determine
                      the function of glycan engagement in viral disease. This
                      Review highlights general principles of virus-glycan
                      interactions and provides specific examples of sialic acid
                      binding by viruses with stalk-like attachment proteins,
                      including influenza virus, reovirus, adenovirus and
                      rotavirus. Understanding virus-glycan interactions is
                      essential to combating viral infections and designing
                      improved viral vectors for therapeutic applications.},
      keywords     = {Polysaccharides (NLM Chemicals) / Receptors, Cell Surface
                      (NLM Chemicals) / Receptors, Virus (NLM Chemicals) /
                      N-Acetylneuraminic Acid (NLM Chemicals)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16 / PUB:(DE-HGF)36},
      pubmed       = {pmid:25263223},
      UT           = {WOS:000343916900008},
      doi          = {10.1038/nrmicro3346},
      url          = {https://juser.fz-juelich.de/record/202141},
}