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Showing 1–4 of 4 results
Advanced filters: Author: Christoffer K. Goth Clear advanced filters

  • O-glycosylation is an abundant post-translational modification but its relevance for bioactive peptides is unclear. Here, the authors detect O-glycans on almost one third of the classified peptide hormones and show that O-glycosylation can modulate peptide half-lives and receptor activation properties.

    • Thomas D. Madsen
    • Lasse H. Hansen
    • Katrine T. Schjoldager
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • The O-glycosylation enzyme Galnt11 has an important role in heterotaxy, a disorder of left–right body patterning or laterality: Galnt11 modulates Notch signalling which alters cilia types at the embryonic left–right organizer, therefore determining laterality.

    • Marko T. Boskovski
    • Shiaulou Yuan
    • Mustafa K. Khokha
    Research
    Nature
    Volume: 504, P: 456-459

  • McKitrick et al engineer and characterize a novel lamprey antibody that recognizes terminal sulfated galactose epitopes on mammalian glycoproteins. This provides a new tool for the exploration of glycoprotein sulfation in mammalian cells, which could aid in the understanding of its functional role and potentially lead to identification of disease biomarkers.

    • Tanya R. McKitrick
    • Steffen M. Bernard
    • Richard D. Cummings
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-14

  • Tanya McKitrick et al. develop a platform for generating libraries of anti-glycan reagents using immunized lampreys. They identify 15 glycan-specific lymphocyte receptor antibodies that can distinguish between different functional groups of the terminal glycan motif.

    • Tanya R. McKitrick
    • Christoffer K. Goth
    • Richard D. Cummings
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-12