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N. Martin Young

Researcher at National Research Council

Publications -  62
Citations -  3822

N. Martin Young is an academic researcher from National Research Council. The author has contributed to research in topics: Campylobacter jejuni & Antigen. The author has an hindex of 30, co-authored 62 publications receiving 3661 citations. Previous affiliations of N. Martin Young include John Radcliffe Hospital.

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Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

TL;DR: Comparison of thepgl locus with that of Neisseria meningitidissuggested that most of the homologous genes are probably involved in the biosynthesis of bacillosamine, and at least 22 glycoproteins were identified.
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Definition of the bacterial N-glycosylation site consensus sequence.

TL;DR: Bacterial N‐glycosylation site selection is more specific than the eukaryotic equivalent with respect to the polypeptide acceptor sequence.
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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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Quantitative Analysis of Bacterial Toxin Affinity and Specificity for Glycolipid Receptors by Surface Plasmon Resonance

TL;DR: In this paper, surface plasmon resonance (SPR) was used for real-time analysis of toxin binding under conditions that mimic the natural cell surface venue of these interactions and without any requirement for labeling of toxin or receptor.