Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–8 of 8 results
Advanced filters: Author: Katrine Schjoldager 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

  • Access to defined human glycans is crucial for biomedical research. Here, authors report Glycocarriers, a mammalian cell-based method for the sustainable and scalable production of O-, N-glycans, and glycosaminoglycans in various formats including free glycans, glycopeptides, and multimer glycomodules.

    • Thapakorn Jaroentomeechai
    • Richard Karlsson
    • Yoshiki Narimatsu
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Venomous animals typically disrupt nervous, locomotor, and cardiovascular systems to incapacitate prey, but certain fish-hunting cone snails evolved toxins that specifically target glucose homeostasis. Here, the authors show the combinatorial nature of weaponized insulin and somatostatin mimetics, exemplifying the use of combinatorial chemical mimicry for prey capture.

    • Ho Yan Yeung
    • Iris Bea L. Ramiro
    • Helena Safavi-Hemami
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Here, the authors discover small molecules that inhibit glycosylation processes that occur in the Golgi apparatus of cells. The molecules reversibly inhibit formation of elaborate glycan structures without affecting secretion of glycoproteins.

    • Daniel Madriz Sørensen
    • Christian Büll
    • Yoshiki Narimatsu
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • Owing to a lack of tools and a lack of a consensus sequence for O-glycosylation, studies of the O-glycoproteome have been few and far between, despite the biological importance of O-glycosylation. This method to analyze O-glycan attachment sites to proteins using glycoengineered cell lines with simplified, homogenous O-glycoproteomes should facilitate future O-glycoproteomics studies.

    • Catharina Steentoft
    • Sergey Y Vakhrushev
    • Henrik Clausen
    Research
    Nature Methods
    Volume: 8, P: 977-982

  • Glycosylation is the most abundant and diverse form of protein post-translational modification. Recent technical developments are enabling the dissection of the glycome in single cells, providing new insights into its regulation and roles in physiology and disease, and new possibilities for controlling glycosylation for therapy.

    • Katrine T. Schjoldager
    • Yoshiki Narimatsu
    • Henrik Clausen
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 21, P: 729-749

  • Glycoproteomic techniques give information on the structure and location of glycan protein modifications. In this Primer, Bagdonaite et al. summarize these techniques, discuss best practices for their use and explore their applications, including identifying biomarkers of disease.

    • Ieva Bagdonaite
    • Stacy A. Malaker
    • Nichollas E. Scott
    Reviews
    Nature Reviews Methods Primers
    Volume: 2, P: 1-29