Evidence map›Paper›PMID 27650323›Full record

ArticleProteomics2016

Development and application of a novel recombinant Aleuria aurantia lectin with enhanced core fucose binding for identification of glycoprotein biomarkers of hepatocellular carcinoma.

Pamela Norton, Mary Ann Comunale, Harmin Herrera, Mengjun Wang, Josef Houser, Michaela Wimmerova, Patrick R Romano, Anand Mehta

Abstract read
In one paragraph

Article in Proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Trial
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  11. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Core-Fucosylated Tetra-AntennaryInternational journal of molecular sciences · 2019
    Article
  16. Article
  17. Review
  18. Article
  19. 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

8 authors at 4 institutions in 2 countries.

Pamela NortonDepartment of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA, USA.
Mary Ann ComunaleDepartment of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA, USA.
Harmin HerreraGraduate School of Biomedical Sciences and Professional Studies, Microbiology and Immunology Graduate Program, Drexel University College of Medicine, Philadelphia, PA, USA.
Mengjun WangDepartment of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA, USA.
Josef HouserCentral European Institute of Technology, Masaryk University, Brno, Czech Republic.
Michaela WimmerovaCentral European Institute of Technology, Masaryk University, Brno, Czech Republic.
Patrick R RomanoBaruch S. Blumberg Institute, Doylestown, PA, USA.
Anand MehtaDepartment of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA, USA.
Drexel University · USBaruch S. Blumberg Institute · USCentral European Institute of Technology · CZCentral European Institute of Technology – Masaryk University · CZ

Funding

Predicting HCC through GlycomicsR01CA120206 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MEHTA, ANAND S. · 2006 to 2016
$4.3M
Aberrantly secreted glycoproteins as markers of liver cancerU01CA168856 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MEHTA, ANAND S. · 2012 to 2016
$1.5M
NCI NIH HHS R01 CA120206NCI NIH HHS U01 CA168856
6 · The paper itself

Abstract

The Aleuria aurantia lectin (AAL) derived from orange peel fungus contains five fucose-binding sites that recognizes fucose bound in α-1,2, α-1,3, α-1,4, and α-1,6 linkages to N-acetylglucosamine and galactose. Recently, we have created several recombinant AAL (rAAL) proteins that had altered binding affinity to fucose linkages. In this report, we further characterize the binding specificity of one of the mutated lectins, N224Q lectin. This lectin was characterized by lectin Western blotting, surface plasmon resonance, and glycan microarray and shown to have increased binding to fucosylated glycan. Subsequently, we used this lectin to identify secreted fucosylated glycoproteins from a fetal hepatic cell line. Proteomic analysis revealed several glycoproteins secreted by the fetal cell line that were bound by N224Q lectin. These findings were confirmed by subsequent proteomic analysis of human serum from control patients or patients with hepatocellular carcinoma. These represent candidate oncofetal markers for liver cancer.

Indexed as

AscomycotaBiomarkers, TumorCarcinoma, HepatocellularCell LineCells, CulturedFucoseGlycoproteinsHepatocytesHumansLectinsLiverLiver NeoplasmsPolysaccharidesProtein BindingProteomicsRecombinant ProteinsBiomarkers, TumorFucoseGlycoproteinslectin, Aleuria aurantiaLectinsPolysaccharidesRecombinant ProteinsAleuria aurantia lectinBiomarkerGlycoproteomicsGlycosylationHepatocellular carcinomaLiver cancer

Identifiers

PMID27650323
PMCPMC5869706
OpenAlexW2523615885

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.