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Warren W. Wakarchuk

Researcher at University of Alberta

Publications -  206
Citations -  9543

Warren W. Wakarchuk is an academic researcher from University of Alberta. The author has contributed to research in topics: Campylobacter jejuni & Sialyltransferase. The author has an hindex of 56, co-authored 200 publications receiving 9051 citations. Previous affiliations of Warren W. Wakarchuk include University of British Columbia & Ryerson University.

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Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs.

TL;DR: The 2 Å crystal structures of the complex of LgtC with manganese and UDP 2-deoxy-2-fluoro-galactose in the presence and absence of the acceptor sugar analog 4′-deoxylactose give valuable insights into the unique catalytic mechanism and, as the first structure of a glycosyltransferase in complex with both the donor and acceptor sugars, provide a starting point for inhibitor design.
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The genetic bases for the variation in the lipo-oligosaccharide of the mucosal pathogen, Campylobacter jejuni. Biosynthesis of sialylated ganglioside mimics in the core oligosaccharide

TL;DR: Compared the lipo-oligosaccharide biosynthesis loci from 11 Campylobacter jejunistrains expressing a total of 8 different ganglioside mimics in their LOS outer cores, at least five distinct mechanisms that allow C. jejuni to vary the structure of the LOSouter core are identified.
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Biosynthesis of ganglioside mimics in Campylobacter jejuni OH4384. Identification of the glycosyltransferase genes, enzymatic synthesis of model compounds, and characterization of nanomole amounts by 600-mhz (1)h and (13)c NMR analysis.

TL;DR: Two strategies for the cloning of four genes responsible for the biosynthesis of the GT1a ganglioside mimic in the lipooligosaccharide (LOS) of a bacterial pathogen,Campylobacter jejuni OH4384, which has been associated with Guillain-Barré syndrome are applied.
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Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase.

TL;DR: It is proposed that Glu 78 is the nucleophile and that GLU 172 is the acid‐base catalyst in the reaction, on the basis of the work investigated.
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The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of bacillus circulans xylanase.

TL;DR: 13C-NMR titrations of xylanase have revealed pKa values that are consistent with the role of Glu172 as a general base catalyst in the deglycosylation step and appears to be a consequence of both reduced electrostatic repulsion due to neutralization of GLU78 and a conformational change in the protein.