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 1–7 of 7 results
Advanced filters: Author: Tongzhong Ju Clear advanced filters

  • This study identifies several O-glycanases, termed Peptide:O-Glycosidases (POGases), with broad substrate specificities. POGases are dual-functional, exhibiting glycan cleavage as well as adhesin-like glycan binding capabilities for diverse glycans.

    • Linjiao Zhou
    • Uriel Ortega-Rodriguez
    • Tongzhong Ju
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-19

  • 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

  • Migration and homing of B cells to lymph nodes are important for B cell functions, but their regulation is poorly understood. Here, the authors show that B cell-specific deletion of Cosmc results in decreased protein O-glycosylation, loss of B cell homing to both lymphoid and nonlymphoid organs, and altered transendothelial migration implicated in this loss.

    • Junwei Zeng
    • Mahmoud Eljalby
    • Richard D. Cummings
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • The expression of blood group antigens causes deletion of cells that generate self-specific antibodies to those antigens, but this deletion could limit adaptive immunity toward pathogens bearing cognate antigens. Two innate immune lectins, galectin-4 and galectin-8, are now reported to recognize and kill human blood group antigen–expressing bacteria.

    • Sean R Stowell
    • Connie M Arthur
    • Richard D Cummings
    Research
    Nature Medicine
    Volume: 16, P: 295-301