Evidence map›Paper›PMID 21374780›Full record

ArticleChembiochem : a European journal of chemical biology2011

Unusual transglycosylation activity of Flavobacterium meningosepticum endoglycosidases enables convergent chemoenzymatic synthesis of core fucosylated complex N-glycopeptides.

Wei Huang, Jie Li, Lai-Xi Wang

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Revealing the Biological Effect of theJournal of the American Chemical Society · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Structural basis for the specific cleavage of core-fucosylatedThe Journal of biological chemistry · 2019
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Endoglycosidases for the Synthesis of Polysaccharides and Glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2016
    Review
  18. A common glycan structure on immunoglobulin G for enhancement of effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Wei HuangInstitute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201 (USA), Fax: (+1) 410-706-4694.
Jie Li
Lai-Xi Wang
University of Maryland, Baltimore · US

Funding

Covergent Chemoenzymatic Synthesis of Glycopeptides and GlycoproteinsR01GM080374 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2007 to 2021
$3.9M
NIGMS NIH HHS R01 GM080374
6 · The paper itself

Abstract

Structurally well defined, homogeneous glycopeptides and glycoproteins are indispensable tools for functional glycomics studies. By screening of various endo-β-N-acetylglucosaminidases through the use of appropriate synthetic donor and acceptor substrates, we have found that the Flavobacterium meningosepticum endo-β-N-acetyl-glucosaminidases (GH family 18), including Endo-F2 and Endo-F3, were able to glycosylate α-1,6-fucosylated GlcNAc derivative to provide natural, core-fucosylated complex-type N-glycopeptides. The Endo-F2 and Endo-F3 were efficient for transferring both sialylated and asia-lylated glycans and were highly specific for an α-1,6-fucosylated GlcNAc-peptide as acceptor for transglycosylation, showing only marginal activity with non-fucosylated GlcNAc-peptides. In contrast, we found that the commonly used endoglycosidases such as Endo-A and Endo-M, which belong to GH family 85, were unable to take α-1,6-fucosyl-GlcNAc derivative as acceptors for transglycosylation. The novel activity of Endo-F2 and Endo-F3 was successfully applied for a highly convergent chemoenzymatic synthesis of a full-sized CD52 glycopeptide antigen carrying both terminal sialic acid and core fucose. This is the first report on endoglycosidases that are able to glycosylate α-1,6-fucosylated GlcNAc derivatives to form natural core-fucosylated glycopeptides.

Indexed as

ChryseobacteriumFucoseGlycoproteinsGlycoside HydrolasesGlycosylationOxazolesFucoseGlycoproteinsGlycoside HydrolasesOxazolesoxazolidine

Identifiers

PMID21374780
PMCPMC3449086
OpenAlexW2144168918

What OpenQuestion holds

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LicenceTDM
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.