Evidence map›Paper›PMID 27601469›Full record

ArticleThe Journal of biological chemistry2016

Molecular Basis for Recognition of the Cancer Glycobiomarker, LacdiNAc (GalNAc[β1→4]GlcNAc), by Wisteria floribunda Agglutinin.

Omid Haji-Ghassemi, Michel Gilbert, Jenifer Spence, Melissa J Schur, Matthew J Parker, Meredith L Jenkins, John E Burke, Henk van Faassen, N Martin Young, Stephen V Evans

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  7. The Journal of general virology · 2025
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  8. Review
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  13. Review
  14. Article
  15. Article
  16. Systematic synthesis of bisectedChemical science · 2022
    Article
  17. Glycoproteins Presenting Galactose andInternational journal of molecular sciences · 2021
    Article
  18. Review
  19. Article
  20. Review
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 at 2 institutions in 1 country.

Omid Haji-GhassemiFrom the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 3P6, Canada and.
Michel GilbertHuman Health Therapeutics, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada.
Jenifer SpenceFrom the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 3P6, Canada and.
Melissa J SchurHuman Health Therapeutics, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada.
Matthew J ParkerFrom the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 3P6, Canada and.
Meredith L JenkinsFrom the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 3P6, Canada and.
John E BurkeFrom the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 3P6, Canada and.
Henk van FaassenHuman Health Therapeutics, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada.
N Martin YoungHuman Health Therapeutics, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada.
Stephen V EvansFrom the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 3P6, Canada and svevans@uvic.ca.
University of Victoria · CANational Research Council Canada · CA

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Aberrant glycosylation and the overexpression of specific carbohydrate epitopes is a hallmark of many cancers, and tumor-associated oligosaccharides are actively investigated as targets for immunotherapy and diagnostics. Wisteria floribunda agglutinin (WFA) is a legume lectin that recognizes terminal N-acetylgalactosaminides with high affinity. WFA preferentially binds the disaccharide LacdiNAc (β-d-GalNAc-[1→4]-d-GlcNAc), which is associated with tumor malignancy in leukemia, prostate, pancreatic, ovarian, and liver cancers and has shown promise in cancer glycobiomarker detection. The mechanism of specificity for WFA recognition of LacdiNAc is not fully understood. To address this problem, we have determined affinities and structure of WFA in complex with GalNAc and LacdiNAc. Affinities toward Gal, GalNAc, and LacdiNAc were measured via surface plasmon resonance, yielding K

Indexed as

Biomarkers, TumorCrystallography, X-RayHumansLactosePlant LectinsProtein BindingProtein DomainsProtein Structure, SecondaryWisteriaBiomarkers, TumorLactoseN-acetylgalactosaminyl-1-4-N-acetylglucosaminePlant Lectinsagglutininbiomarkercancercarbohydratecarbohydrate-binding proteinglycobiomarkerlectinstructural biologyx-ray crystallography

Identifiers

PMID27601469
PMCPMC5104934
OpenAlexW2518482737

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.