A quantitative, high-throughput method identifies protein-glycan interactions via mass spectrometry.
Autorzy:
KitovPI; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Kitova EN; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Han L; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Li Z; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Jung J; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Rodrigues E; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Hunter CD; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Cairo CW; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada. Macauley MS; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada.; 2Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB T6G 2E1 Canada. Klassen JS; 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2 Canada.
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Źródło:
Communications biology [Commun Biol] 2019 Jul 22; Vol. 2, pp. 268. Date of Electronic Publication: 2019 Jul 22 (Print Publication: 2019).
Impact of the nature and size of the polymeric backbone on the ability of heterobifunctional ligands to mediate shiga toxin and serum amyloid p component ternary complex formation.
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