ArticleNature communications2023
The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- A SNP altering the MUC5AC mucin structure is increased in idiopathic pulmonary fibrosis together with the MUC5B SNP.Respiratory research · 2026Article
- Mucin-Based Biomimetic Patches for Dynamic Heart Repair: Auxetic Structures and Translational Challenges.Cardiovascular engineering and technology · 2026Review
- Article
- Mpi-driven N-glycosylation orchestrates mucin O-glycosylation and intestinal homeostasis.Nature communications · 2026Article
- Mucin Type Drives Composition and Mucin Glycan Degradation of an In Vitro Synthetic Microbial Community.Environmental microbiology · 2026Article
- Complexation of Walnut Protein with Adenosine Nucleotides: Effects on Protein Functionality and Novel Insight into the Absorption Mechanism of cAMP.Foods (Basel, Switzerland) · 2026Article
- Article
- Mucinase fromFrontiers in microbiology · 2026Article
- Mucin 2 and unfolded protein response reshape the mucus barrier in inflammatory bowel disease (Review).Molecular medicine reports · 2026Review
- EatA mediated degradation of intestinal mucus is species-specific and driven by MUC2 structural features.Nature communications · 2025Article
- Distinct in vitro utilization and degradation of porcine gastric mucin glycans by human intestinal bacteria.FEMS microbiology ecology · 2025Article
- Macroheterogeneities Induced by Disulfide Bond Reduction in Native Mucus.ACS applied bio materials · 2025Article
- Article
- Structure of the MUC5AC VWD3 assembly responsible for the formation of net-like mucin polymers.EMBO reports · 2025Article
- The structure of FCGBP is formed as a disulfide-mediated homodimer between its C-terminal domains.The FEBS journal · 2025Article
- Article
- Methionine ameliorates intestinal injury in senescence-accelerated mouse prone-8 mice by reducing sulfate-reducing bacteria and enhancing barrier function.Frontiers in nutrition · 2025Article
- Live Multi-Strain Probiotics Enhance Growth Performance by Regulating Intestinal Morphology and Microbiome Population in Weaning Piglets.Microorganisms · 2024Article
- Revealing Glycosylation Patterns inJournal of agricultural and food chemistry · 2024Article
- ThePolymers · 2024Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The MUC2 mucin polymer is the main building unit of the intestinal mucus layers separating intestinal microbiota from the host epithelium. The MUC2 mucin is a large glycoprotein with a C-terminal domain similar to the MUC5AC and MUC5B mucins and the von Willebrand factor (VWF). A structural model of the C-terminal part of MUC2, MUC2-C, was generated by combining Cryo-electron microscopy, AlphaFold prediction, information of its glycosylation, and small angle X-ray scattering information. The globular VWD4 assembly in the N-terminal of MUC2-C is followed by 3.5 linear VWC domains that form an extended flexible structure before the C-terminal cystine-knot. All gel-forming mucins and VWF form tail-tail disulfide-bonded dimers in their C-terminal cystine-knot domain, but interestingly the MUC2 mucin has an extra stabilizing disulfide bond on the N-terminal side of the VWD4 domain, likely essential for a stable intestinal mucus barrier.
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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.