Evidence map›Paper›PMID 23535562›Full record

ArticleBioorganic & medicinal chemistry2013

One-pot multi-enzyme (OPME) chemoenzymatic synthesis of sialyl-Tn-MUC1 and sialyl-T-MUC1 glycopeptides containing natural or non-natural sialic acid.

Hamed Malekan, Gabriel Fung, Vireak Thon, Zahra Khedri, Hai Yu, Jingyao Qu, Yanhong Li, Li Ding, Kit S Lam, Xi Chen

Abstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Exploring the Scope of FunctionalizedMolecules (Basel, Switzerland) · 2025
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  5. A bifunctionalOrganic & biomolecular chemistry · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Synthesis of glycopeptides and glycopeptide conjugates.Organic & biomolecular chemistry · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Enzymatic Synthesis of Glycans and Glycoconjugates.Advances in biochemical engineering/biotechnology · 2021
    Review
  16. Article
  17. Article
  18. Redox-Controlled Site-Specific α2-6-Sialylation.Journal of the American Chemical Society · 2019
    Article
  19. Article
  20. Synthesis ofFrontiers in immunology · 2019
    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 1 institution in 1 country.

Hamed MalekanDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Gabriel Fung
Vireak Thon
Zahra Khedri
Hai Yu
Jingyao Qu
Yanhong Li
Li Ding
Kit S Lam
Xi Chen
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
Oligosaccharides as antimicrobials and prebioticsR01HD065122 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2010 to 2013
$1.8M
NCI NIH HHS P30 CA093373NICHD NIH HHS R01 HD065122NICHD NIH HHS R01HD065122
6 · The paper itself

Abstract

A series of STn-MUC1 and ST-MUC1 glycopeptides containing naturally occurring and non-natural sialic acids have been chemoenzymatically synthesized from Tn-MUC1 glycopeptide using one-pot multienzyme (OPME) approaches. In situ generation of the sialyltransferase donor cytidine 5'-monophosphate-sialic acid (CMP-Sia) using a CMP-sialic acid synthetase in the presence of an extra amount of cytidine 5'-triphosphate (CTP) and removal of CMP from the reaction mixture by flash C18 cartridge purification allow the complete consumption of Tn-MUC1 glycopeptide for quantitative synthesis of STn-MUC1. A Campylobacter jejuni β1-3GalT (CjCgtBΔ30-His6) mutant has been found to catalyze the transfer of one or more galactose residues to Tn-MUC1 for the synthesis of T-MUC1 and galactosylated T-MUC1. Sialylation of T-MUC1 using Pasteurella multocida α2-3-sialyltransferase 3 (PmST3) with Neisseria meningitidis CMP-sialic acid synthetase (NmCSS) and Escherichia coli sialic acid aldolase in one pot produced ST-MUC1 efficiently. These glycopeptides are potential cancer vaccine candidates.

Indexed as

Antigens, Viral, TumorBacterial ProteinsBase SequenceCampylobacter jejuniCloning, MolecularEscherichia coliGlycopeptidesMolecular Sequence DataMutationNeisseria meningitidisOxo-Acid-LyasesPasteurella multocidaRecombinant Fusion ProteinsSialic AcidsSialyltransferasesAntigens, Viral, TumorBacterial ProteinsGlycopeptidesN-acetyllactosaminide alpha-2,3-sialyltransferaseN-acetylneuraminate lyaseN-acetylneuraminate synthaseOxo-Acid-LyasesRecombinant Fusion ProteinsSialic Acidssialyl-Tn-MUC1SialyltransferasesCarbohydrateChemoenzymatic synthesisEnzymatic synthesisGlycopeptideST antigenSTn antigenT antigenTn antigen

Identifiers

PMID23535562
PMCPMC3722252
OpenAlexW2013495203

What OpenQuestion holds

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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.