Evidence map›Paper›PMID 22967056›Full record

ArticleJournal of the American Chemical Society2012

Density variant glycan microarray for evaluating cross-linking of mucin-like glycoconjugates by lectins.

Kamil Godula, Carolyn R Bertozzi

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.0field-weighted citation impact, top 2% of its field
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

59 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
  2. Monosaccharide Binding to Synthetic Carbohydrate Receptor Microarrays.The journal of physical chemistry. C, Nanomaterials and interfaces · 2025
    Article
  3. Article
  4. Understanding Viral-Glycocalyx Interactions Using Brush-Linked to Cross-Linked Models.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Mannose Ligands for Mannose Receptor Targeting.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
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  15. Review
  16. Article
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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

2 authors at 2 institutions in 1 country.

Kamil GodulaDepartment of Chemistry, University of California, Berkeley, California 94720, United States.
Carolyn R Bertozzi
Howard Hughes Medical Institute · USLawrence Berkeley National Laboratory · US

Funding

Investigations of Golgi EnzymesR01GM059907 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 1999 to 2016
$5.9M
NeoProteoglycans as synthetic materials for regenerative medicine and bioimagingK99EB013446 · NIBIB · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI GODULA, KAMIL · 2011 to 2012
$165k
NIBIB NIH HHS 5 K99 EB013446-02NIBIB NIH HHS K99 EB013446NIGMS NIH HHS GM59907NIGMS NIH HHS R01 GM059907
6 · The paper itself

Abstract

Interactions of mucin glycoproteins with cognate receptors are dictated by the structures and spatial organization of glycans that decorate the mucin polypeptide backbone. The glycan-binding proteins, or lectins, that interact with mucins are often oligomeric receptors with multiple ligand binding domains. In this work, we employed a microarray platform comprising synthetic glycopolymers that emulate natural mucins arrayed at different surface densities to evaluate how glycan valency and spatial separation affect the preferential binding mode of a particular lectin. We evaluated a panel of four lectins (Soybean agglutinin (SBA), Wisteria floribunda lectin (WFL), Vicia villosa-B-4 agglutinin (VVA), and Helix pomatia agglutin (HPA)) with specificity for α-N-acetylgalactosamine (α-GalNAc), an epitope displayed on mucins overexpressed in many adenocarcinomas. While these lectins possess the ability to agglutinate A(1)-blood cells carrying the α-GalNAc epitope and cross-link low valency glycoconjugates, only SBA showed a tendency to form intermolecular cross-links among the arrayed polyvalent mucin mimetics. These results suggest that glycopolymer microarrays can reveal discrete higher-order binding preferences beyond the recognition of individual glycan epitopes. Our findings indicate that glycan valency can set thresholds for cross-linking by lectins. More broadly, well-defined synthetic glycopolymers enable the integration of glycoconjugate structural and spatial diversity in a single microarray screening platform.

Indexed as

Fluorescent DyesGlycoconjugatesLectinsMolecular MimicryMucinsPolysaccharidesFluorescent DyesGlycoconjugatesLectinsMucinsPolysaccharides

Identifiers

PMID22967056
PMCPMC3458438
OpenAlexW2044215803

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.