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- 22Electrospray ionization mass spectrometry
- 12Affinity
- 6Library screening
- 6Norovirus
- 5Mass-spectrometry
- 30Chemistry, Department of
- 30Chemistry, Department of/Journal Articles (Chemistry)
- 12Graduate and Postdoctoral Studies (GPS), Faculty of
- 12Graduate and Postdoctoral Studies (GPS), Faculty of/Theses and Dissertations
- 1Agricultural, Food and Nutritional Science, Department of
- 1Agricultural, Food and Nutritional Science, Department of/Journal Articles (Agricultural, Food and Nutritional Science)
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2015
Boraston, Alisdair, B., Kitova, Elena N., Klassen, John S., Tan, Ming, Pluvinage, Benjamin, Han, Ling, Jiang, Xi
The binding profiles of many human noroviruses (huNoVs) for human histo-blood group antigens have been characterized. However, quantitative-binding data for these important virus–host interactions are lacking. Here, we report on the intrinsic (per binding site) affinities of HBGA oligosaccharides...
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2015
Tan, Ming, Jiang, Xi, Han, Ling, Kitova, Elena N., Klassen, John S., Boraston, Alisdair, B., Pluvinage, Benjamin
The binding profiles of many human noroviruses (huNoVs) for human histo-blood group antigens have been characterized. However, quantitative-binding data for these important virus–host interactions are lacking. Here, we report on the intrinsic (per binding site) affinities of HBGA oligosaccharides...
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2013
Klassen, John S., Xia, Ming, Tan, Ming, Wang, Leyi, Han, Ling, Kitova, Elena N., Jiang, Xi, Kitov, Pavel I.
Noroviruses (NoVs), the major cause of viral acute gastroenteritis, recognize histo-blood group antigens (HBGAs) as receptors or attachment factors. To gain a deeper understanding of the interplay between NoVs and their hosts, the affinities of recombinant P dimers (P2's) of a GII.4 NoV (VA387)...
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2013
Jiang, Xi, Klassen, John S., Kitova, Elena N., Wang, Leyi, Han, Ling, Kitov, Pavel I., Xia, Ming, Tan, Ming
Noroviruses (NoVs), the major cause of viral acute gastroenteritis, recognize histo-blood group antigens (HBGAs) as receptors or attachment factors. To gain a deeper understanding of the interplay between NoVs and their hosts, the affinities of recombinant P dimers (P2's) of a GII.4 NoV (VA387)...
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Carbohydrate-lipid interactions: Affinities of methylmannose polysaccharides for lipids in aqueous solution
Download2012
Sun, Nian, Klassen, John S., Bai, Yu, Liu, Lan, Xia, Li, Lowary, Todd L.
The interactions between 3-O-methyl-mannose polysaccharides (MMPs), extracted from Mycobacterium smegmatis (consisting of a mixture of MMP-10, -11, -12 and -13) or obtained by chemical synthesis (MMP-5s, -8s, -11s and -14s), and linear saturated and unsaturated fatty acids (FAs), and a commercial...
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Carbohydrate-lipid interactions: Affinities of methylmannose polysaccharides for lipids in aqueous solution
Download2012
Xia, Li, Sun, Nian, Klassen, John S., Liu, Lan, Bai, Yu, Lowary, Todd L.
The interactions between 3-O-methyl-mannose polysaccharides (MMPs), extracted from Mycobacterium smegmatis (consisting of a mixture of MMP-10, -11, -12 and -13) or obtained by chemical synthesis (MMP-5s, -8s, -11s and -14s), and linear saturated and unsaturated fatty acids (FAs), and a commercial...
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Chemical, Enzymatic and Chemo-enzymatic Synthesis of Complex Oligosaccharides as Probes of Glycan Functions
DownloadSpring 2016
Carbohydrates, an essential class of biomolecules, mediate a variety of biological processes. Recent advances in chemical, enzymatic and chemo-enzymatic synthesis have facilitated access to an increasing number of structurally well-defined oligosaccharides. These molecules are serving as...
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Comparative genomics of Lactobacillus reuteri from sourdough reveals adaptation of an intestinal symbiont to food fermentations
Download2015
Zhao, Xin, Gänzle, Michael G., Lin, Xiaoxi B., Zheng, Jinshui
Lactobacillus reuteri is a dominant member of intestinal microbiota of vertebrates, and occurs in food fermentations. The stable presence of L. reuteri in sourdough provides the opportunity to study the adaptation of vertebrate symbionts to an extra-intestinal habitat. This study evaluated this...
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Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases
Download2009
Klassen, John S., Shoemaker, Glen K., Palcic, Monica M., Soya, Naoto
The first comparative thermodynamic study of the human blood group glycosyltransferases, α-(1→3)-N-acetylgalactosaminyltransferase (GTA) and α-(1→3)-galactosyltransferase (GTB), interacting with donor substrates, donor and acceptor analogs, and trisaccharide products in vitro is reported. The...
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Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases
Download2009
Shoemaker, Glen K., Klassen, John S., Palcic, Monica M., Soya, Naoto
The first comparative thermodynamic study of the human blood group glycosyltransferases, α-(1→3)-N-acetylgalactosaminyltransferase (GTA) and α-(1→3)-galactosyltransferase (GTB), interacting with donor substrates, donor and acceptor analogs, and trisaccharide products in vitro is reported. The...