@article{Oberli2010-08-04Molec-12611,
  year={2010},
  doi={10.1021/ja104027w},
  title={Molecular analysis of Carbohydrate−Antibody interactions : case study using a Bacillus anthracis Tetrasaccharide},
  number={30},
  volume={132},
  issn={0002-7863},
  journal={Journal of the American Chemical Society},
  pages={10239--10241},
  author={Oberli, Matthias A. and Tamborrini, Marco and Tsai, Yu-Hsuan and Werz, Daniel B. and Horlacher, Tim and Adibekian, Alexander and Gauss, Dominik and Möller, Heiko M. and Pluschke, Gerd and Seeberger, Peter H.}
}

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    <dcterms:bibliographicCitation>First publ. in: Journal of the American Chemical Society 132 (2010), 30, pp. 10239–10241</dcterms:bibliographicCitation>
    <dc:contributor>Pluschke, Gerd</dc:contributor>
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    <dc:contributor>Möller, Heiko M.</dc:contributor>
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    <dc:contributor>Seeberger, Peter H.</dc:contributor>
    <dcterms:title>Molecular analysis of Carbohydrate−Antibody interactions : case study using a Bacillus anthracis Tetrasaccharide</dcterms:title>
    <dc:contributor>Tamborrini, Marco</dc:contributor>
    <dc:creator>Adibekian, Alexander</dc:creator>
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    <dcterms:abstract xml:lang="eng">The process for selecting potent and effective carbohydrate antigens is not well-established. A combination of synthetic glycan microarray screening, surface plasmon resonance analysis, and saturation transfer difference NMR spectroscopy was used to dissect the antibody-binding surface of a carbohydrate antigen, revealing crucial binding elements with atomic-level detail. This analysis takes the first step toward uncovering the rules for structure-based design of carbohydrate antigens.</dcterms:abstract>
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