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Skip to Search Results- 22Electrospray ionization mass spectrometry
- 13Binding
- 12Affinity
- 7Electrospray ionization
- 7Norovirus
- 6Carbohydrates
- 34Chemistry, Department of
- 34Chemistry, Department of/Journal Articles (Chemistry)
- 6Graduate and Postdoctoral Studies (GPS), Faculty of
- 6Graduate and Postdoctoral Studies (GPS), Faculty of/Theses and Dissertations
- 4Biological Sciences, Department of
- 4Biological Sciences, Department of/Journal Articles (Biological Sciences)
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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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1994
Wright, G.E., Reha-Krantz, L.J., Khan, N.N.
Bacteriophage T4 DNA polymerase was Inhibited by butylphenyl nucleotldes, aphldlcolin and pyrophosphate analogs, but with lower sensitivities than other members of the B family DNA polymerases. The nucleotides N2-{p-n-butylphenyl)dGTP (BuPdGTP) and 2-{p-n-butylanilino)dATP (BuAdATP) inhibited T4...
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Fall 2014
Carbohydrate–protein interactions play key roles in a range of biological processes. Noticeable advancements have been made in understanding the features associated with the recognition of pyranosides (six-membered ring sugars) by proteins. In contrast, similar detailed studies about the...
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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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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...