ArticleProceedings of the National Academy of Sciences of the United States of America2017
Recognition of protein-linked glycans as a determinant of peptidase activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
59 citing papers in PubMed, 95 citations in OpenAlex.
- Discovery of a secretedGut microbes · 2026Article
- Functional conservation of divergent peptidase_M60 O-glycopeptidases in enterococcus.Glycobiology · 2026Article
- Longitudinal analysis of human milk oligosaccharides and mucin-2-glycans in infants reveals enrichment of sulfated and glucuronic acid-bearing HMOs.The Journal of biological chemistry · 2026Article
- Enhanced microbiota-derived mucinases in colorectal cancer patients revealed by gut metagenome probing coupled with functional validation.Applied and environmental microbiology · 2026Article
- What Is the Functional Role of the Acyltransferase-like Domain in the Svx Peptidase of the Phytopathogenic BacteriumInternational journal of molecular sciences · 2026Article
- Degradation of mucinbioRxiv : the preprint server for biology · 2026Article
- Bacterial zinc metalloproteases as facilitators of pathogenic success: a review.Archives of microbiology · 2026Review
- EatA mediated degradation of intestinal mucus is species-specific and driven by MUC2 structural features.Nature communications · 2025Article
- A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism.Nature communications · 2025Article
- Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities.Nature communications · 2025Article
- GlycoIP: an integrated platform for simultaneous and site-specificFrontiers in chemistry · 2025Article
- Mucin-driven ecological interactions in an in vitro synthetic community of human gut microbes.Glycobiology · 2024Article
- Clinical glycoproteomics: methods and diseases.MedComm · 2024Review
- Cellulose binding and the timing of expression influence protein targeting to the double-layered cyst wall ofmSphere · 2024Article
- Article
- Design of a mucin-selective protease for targeted degradation of cancer-associated mucins.Nature biotechnology · 2024Article
- Combined analysis of secreted proteins and glycosylation identifies prognostic features in cholangiocarcinoma.Journal of cellular physiology · 2024Article
- Cultivation of Microorganisms in Media Supplemented with Mucin Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Toxinotyping ofIranian journal of veterinary research · 2024Article
- Glycoproteomic landscape and structural dynamics of TIM family immune checkpoints enabled by mucinase SmE.Nature communications · 2023Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The vast majority of proteins are posttranslationally altered, with the addition of covalently linked sugars (glycosylation) being one of the most abundant modifications. However, despite the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Earth, the fundamental details of how peptidases accommodate posttranslational modifications, including glycosylation, has not been addressed. Through biochemical analyses and X-ray crystallographic structures we show that to hydrolyze their substrates, three structurally related metallopeptidases require the specific recognition of O-linked glycan modifications via carbohydrate-specific subsites immediately adjacent to their peptidase catalytic machinery. The three peptidases showed selectivity for different glycans, revealing protein-specific adaptations to particular glycan modifications, yet always cleaved the peptide bond immediately preceding the glycosylated residue. This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular understanding of glycoprotein degradation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.