Evidence map›Paper›PMID 28644609›Full record

ArticleACS chemical biology2017

GalNAc-Tyrosine Is a Ligand of Plant Lectins, Antibodies, and Human and Murine Macrophage Galactose-Type Lectins.

Ruslan Gibadullin, David Wayne Farnsworth, Joseph J Barchi, Jeffrey C Gildersleeve

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Implications of Mucin-TypeMolecules (Basel, Switzerland) · 2025
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. ASGR1 and Its Enigmatic Relative, CLEC10A.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Ruslan GibadullinChemical Biology Laboratory, National Cancer Institute, National Institutes of Health , 376 Boyles St., Frederick, Maryland 21702, United States.
David Wayne FarnsworthChemical Biology Laboratory, National Cancer Institute, National Institutes of Health , 376 Boyles St., Frederick, Maryland 21702, United States.
Joseph J BarchiChemical Biology Laboratory, National Cancer Institute, National Institutes of Health , 376 Boyles St., Frederick, Maryland 21702, United States.
Jeffrey C GildersleeveChemical Biology Laboratory, National Cancer Institute, National Institutes of Health , 376 Boyles St., Frederick, Maryland 21702, United States.ORCID 0000-0002-3744-6423
National Institutes of Health · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
Carbohydrate Microarray Profiling of Glycan-Binding Antibodies and LectinsZIABC010740 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GILDERSLEEVE, JEFFREY · 2009 to 2025
$10.7M
Development of a Carbohydrate MicroarrayZIABC010675 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GILDERSLEEVE, JEFFREY · 2009 to 2025
$6.1M
Intramural NIH HHS ZIA BC010740NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

In 2011, a new type of protein O-glycosylation was discovered in which N-acetylgalactosamine is attached to the side chain of tyrosine (GalNAc-Tyr). While present on dozens of proteins, the biological roles of GalNAc-Tyr are unknown. To gain insight into this new type of modification, we synthesized a group of GalNAc-Tyr glycopeptides, constructed microarrays, and evaluated potential recognition of GalNAc-Tyr by a series of glycan-binding proteins. Through a series of >150 microarray experiments, we assessed binding properties of a variety of plant lectins, monoclonal antibodies, and endogenous lectins. VVL, HPA, and SBA were all found to bind tightly to GalNAc-Tyr, and several Tn binding antibodies and blood group A antibodies were found to cross-react with GalNAc-Tyr. Thus, detection of GalNAc-Tyr modified proteins is an important consideration when analyzing results from these reagents. Additionally, we evaluated potential recognition by two mammalian lectins, human (hMGL) and murine (mMGL-2) macrophage galactose type C-type lectins. Both hMGL and mMGL-2 bound tightly to GalNAc-Tyr determinants. The apparent K

Indexed as

LigandsAcetylgalactosamineAnimalsAntibodies, MonoclonalCarbohydrate SequenceFemaleFlow CytometryHumansLectinsLectins, C-TypeMagnetic Resonance SpectroscopyMiceMice, Inbred C57BLMicroarray AnalysisPlant LectinsTyrosineAcetylgalactosamineAntibodies, MonoclonalLectinsLectins, C-TypeLigandsMGL2 protein, mousePlant LectinsTyrosine

Identifiers

PMID28644609
PMCPMC7891759
OpenAlexW2668409896

What OpenQuestion holds

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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.