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Mark R. Wormald

Researcher at University of Oxford

Publications -  180
Citations -  15520

Mark R. Wormald is an academic researcher from University of Oxford. The author has contributed to research in topics: Glycosylation & Glycan. The author has an hindex of 64, co-authored 179 publications receiving 14686 citations. Previous affiliations of Mark R. Wormald include Hokuriku University & Katholieke Universiteit Leuven.

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Polyhydroxylated pyrrolidine and pyrrolizidine alkaloids from Hyacinthoides non-scripta and Scilla campanulata

TL;DR: The 7-O-beta-D xyloside 6 was a stronger competitive inhibitor than 4 of C saccharolyticum beta-glucosidase and rat intestinal lactase, with K(i) values of 0.06 and 0.07 microM, respectively, but a weaker inhibitor of bovine liver beta-galactosidases.
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Complement Regulation at the Molecular Level: The Structure of Decay-Accelerating Factor

TL;DR: X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution and suggest that the interaction with the convertase, and thus complement regulation, depends on the burial of a hydrophobic patch centered on the linker between SCR domains 2 and 3.
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Afamin Is a Novel Human Vitamin E-Binding Glycoprotein Characterization and In Vitro Expression

TL;DR: The purification of a 75-kDa glycoprotein with vitamin E-binding properties by stepwise chromatography of lipoprotein-depleted human plasma and monitoring of vitamin E (alpha-tocopherol)-binding activity complements the in vitro findings for purified native and recombinant afamin and suggests potential roles for afamin in fertility and neuroprotection.
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A nonself sugar mimic of the HIV glycan shield shows enhanced antigenicity.

TL;DR: It is shown here that a designed set of nonself, synthetic monosaccharides are potent antigens, and when introduced to the terminus of the D1 arm of protein glycans recognized by 2G12, their antigenicity is significantly enhanced.
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The conformational effects of N-glycosylation on the tailpiece from serum IgM.

TL;DR: 1H-NMR spectroscopy has been used to study the conformation and dynamics of the isolated tailpiece from human serum immunoglobulin M, a 22-residue peptide containing a single asparagine glycosylation site, and various roles for the different glycoforms of the tail peptide are discussed.