Evidence map›Paper›PMID 33031746›Full record

ArticleCell2020

Assembly Mechanism of Mucin and von Willebrand Factor Polymers.

Gabriel Javitt, Lev Khmelnitsky, Lis Albert, Lavi Shlomo Bigman, Nadav Elad, David Morgenstern, Tal Ilani, Yaakov Levy, Ron Diskin, Deborah Fass

Abstract read
In one paragraph

Article in Cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

78 citing papers in PubMed.

  1. Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A Coarse-Grained MARTINI Model for Mucins.Journal of chemical theory and computation · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. TheScience (New York, N.Y.) · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Mucins and Their Roles in Asthma.Immunological reviews · 2025
    Review
  20. Article

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Gabriel JavittDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Lev KhmelnitskyDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Lis AlbertDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Lavi Shlomo BigmanDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Nadav EladDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot 7610001, Israel.
David MorgensternDe Botton Institute for Protein Profiling, Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
Tal IlaniDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Yaakov LevyDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ron DiskinDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
Deborah FassDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel. Electronic address: deborah.fass@weizmann.ac.il.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food. Likewise, the vasculature is threatened by inflammation and trauma. Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems. Colon mucins additionally house and feed the gut microbiome. Here, we present an integrated structural analysis of the intestinal mucin MUC2. Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels. Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus. Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2. The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.

Indexed as

Amino Acid SequenceAnimalsBiopolymersCryoelectron MicroscopyDisulfidesFemaleGlycosylationHEK293 CellsHumansHydrogen-Ion ConcentrationMice, Inbred C57BLModels, MolecularMucinsPeptidesProtein DomainsProtein MultimerizationBiopolymersDisulfidesMucinsPeptidesvon Willebrand Factorcryo-EMdisulfide bondsmucinsmucusO-glycosylationpolymerprotein assemblyquaternary structurevon Willebrand factorX-ray crystallography

Identifiers

PMID33031746
PMCPMC7599080

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

None linked

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.