ArticleNature chemical biology2022
Sulfated glycan recognition by carbohydrate sulfatases of the human gut microbiota.
Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Review
- Unique adaptations in sulfatases underpin colonic mucin degradation by Akkermansia muciniphila.Nature microbiology · 2026Article
- Fluorogenic Coupled Assays Reveal Catalytic Properties, Inhibition Constants and Cellular Location of Mucin-Active Carbohydrate Sulfatases.Angewandte Chemie (International ed. in English) · 2026Article
- Beyond estrobolome 1.0: unraveling endocrine-microbiome axis as a driver and therapeutic target in hormone-driven cancers.NPJ biofilms and microbiomes · 2026Review
- Defining substrate specificities ofOrganic chemistry frontiers : an international journal of organic chemistry · 2026Article
- The butyrate-producing Gram-positive human gut bacterium, Hoskinsella mucinilytica, selectively targets host mucin N-acetylhexosamines.The Journal of biological chemistry · 2026Article
- PA14 domain of glycosyltransferase B4GALNT3 is a lectin that binds to sulfated glycan ligands.The Journal of biological chemistry · 2026Article
- Prebiotic and Functional Fibers from Micro- and Macroalgae: Gut Microbiota Modulation, Health Benefits, and Food Applications.International journal of molecular sciences · 2025Review
- Structure-function relationship of the GH168 fucanase reveals an unusual enzyme recognition mechanism for sulfated polysaccharide.Nature communications · 2025Article
- Article
- Lipidomics, Microbiota, and IntestinalInternational journal of molecular sciences · 2025Review
- Arylsulfamates inhibit colonic Bacteroidota growth through a sulfatase-independent mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification and Characterization of a New Thermophilic κ-Carrageenan Sulfatase.Journal of agricultural and food chemistry · 2025Article
- Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands.Journal of the American Chemical Society · 2024Article
- Dietary fiber monosaccharide content alters gut microbiome composition and fermentation.Applied and environmental microbiology · 2024Article
- Host-microbiome orchestration of the sulfated metabolome.Nature chemical biology · 2024Review
- An expanded transcriptome atlas for Bacteroides thetaiotaomicron reveals a small RNA that modulates tetracycline sensitivity.Nature microbiology · 2024Article
- Quantifying the adaptive landscape of commensal gut bacteria using high-resolution lineage tracking.Nature communications · 2024Article
- Engineering sulfonate group donor regeneration systems to boost biosynthesis of sulfated compounds.Nature communications · 2023Article
- Intestinal mucus and their glycans: A habitat for thriving microbiota.Cell host & microbe · 2023Review
Corrections and comments
- Erratum issued
Authors and funding
14 authors at 6 institutions in 8 countries.
Funding
Abstract
Sulfated glycans are ubiquitous nutrient sources for microbial communities that have coevolved with eukaryotic hosts. Bacteria metabolize sulfated glycans by deploying carbohydrate sulfatases that remove sulfate esters. Despite the biological importance of sulfatases, the mechanisms underlying their ability to recognize their glycan substrate remain poorly understood. Here, we use structural biology to determine how sulfatases from the human gut microbiota recognize sulfated glycans. We reveal seven new carbohydrate sulfatase structures spanning four S1 sulfatase subfamilies. Structures of S1_16 and S1_46 represent novel structures of these subfamilies. Structures of S1_11 and S1_15 demonstrate how non-conserved regions of the protein drive specificity toward related but distinct glycan targets. Collectively, these data reveal that carbohydrate sulfatases are highly selective for the glycan component of their substrate. These data provide new approaches for probing sulfated glycan metabolism while revealing the roles carbohydrate sulfatases play in host glycan catabolism.
Indexed as
Identifiers
What OpenQuestion holds
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.