ArticleMolecular & cellular proteomics : MCP2025
Spatial Organization of the Sperm Cell Glycoproteome.
Article in Molecular & cellular proteomics : MCP, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- The maternal immune response to semen: implications for reproductive success in livestock.Reproduction & fertility · 2026Review
- Sperm Cell Membranes of Bulls and Bucks Associated with Sperm Fertility and Freezability.Animals : an open access journal from MDPI · 2025Review
- From glycosylation to deglycosylation: Unraveling the complete deglycosylation processing pathway ofScience progressReview
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sperm cells are terminally differentiated cells that are essential for reproduction in sexually reproducing species. Consistent with their highly specialized function, sperm cells harbor a unique proteome containing many proteins not expressed in somatic cells. In contrast, the post-translational landscape of the sperm proteome remains largely unexplored, limiting our understanding of how modifications such as glycosylation impact sperm function and sperm-egg interactions. Here, we used glycopeptide-centric glycoproteomics to comprehensively characterize protein N-glycosylation in sperm from three mammalian species, revealing clear conservation of glycosylation profiles. We find that glycosylation patterns in sperm proteins are distinct from those in plasma, with as clear distinctive features less sialyation and more paucimannosylation in sperm. Moreover, based on their subcellular location, sperm protein glycosylation varies, with paucimannose species enriched in the acrosomal vesicle, oligomannose species in the sperm head membrane, and complex glycan species in the acrosomal membrane.
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Registered trials
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