Publications by authors named "B Schumann"

Correct elaboration of N-linked glycans in the secretory pathway of human cells is essential in physiology. Early N-glycan biosynthesis follows an assembly line principle before undergoing crucial elaboration points that feature the sequential incorporation of the sugar -acetylglucosamine (GlcNAc). The activity of GlcNAc transferase V (MGAT5) primes the biosynthesis of an N-glycan antenna that is heavily upregulated in cancer.

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Glycosylation is a ubiquitous modification of proteins, necessitating approaches for its visualization and characterization. Bioorthogonally tagged monosaccharides have been instrumental to this end, offering a chemical view into the cell biology of glycans. Understanding the use of such monosaccharides by cellular biosynthetic pathways has expanded their applicability in cell biology, for instance through the strategy named Bio-Orthogonal Cell-specific TAgging of Glycoproteins (BOCTAG).

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Article Synopsis
  • - Mammalian cells communicate through surface interactions, and proteoglycans play a key role by carrying large sugar chains that help recruit signaling molecules, yet only a few proteoglycans are currently identified.
  • - Two enzymes, XT1 and XT2, are responsible for the initial step of adding sugars to proteins but their redundancy complicates the study of proteoglycans.
  • - The research introduces a method called bump-and-hole engineering to modify these enzymes, allowing for the specific addition of a chemically marked sugar to proteins, enabling visualization and detailed analysis of proteoglycan structures in cells.
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Bioorthogonal chemistry was deservedly recognized with the 2022 Nobel Prize in Chemistry, having transformed the way chemists and biologists interrogate biological systems in the past twenty years. This Voices piece asks researchers from a range of backgrounds: what are some major challenges and opportunities facing the field in coming years?

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