Evidence map›Paper›PMID 17370997›Full record

ArticleBioconjugate chemistry

Direct identification of nonreducing GlcNAc residues on N-glycans of glycoproteins using a novel chemoenzymatic method.

Elizabeth Boeggeman, Boopathy Ramakrishnan, Charlton Kilgore, Nelly Khidekel, Linda C Hsieh-Wilson, John T Simpson, Pradman K Qasba

Open access · greenAbstract read
In one paragraph

Article in Bioconjugate chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

34 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  5. Precision Modification of Native Antibodies.Bioconjugate chemistry · 2021
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Identification ofFrontiers in endocrinology · 2019
    Article
  12. Article
  13. A Chemoenzymatic Histology Method for O-GlcNAc Detection.Chembiochem : a European journal of chemical biology · 2017
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Glycosyltransferase engineering for carbohydrate synthesis.Biochemical Society transactions · 2016
    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

7 authors at 3 institutions in 1 country.

Elizabeth BoeggemanStructural Glycobiology Section, CCR-Nanobiology Program, Center for Cancer Research, NCI-Frederick, Frederick, Maryland 21702, USA.
Boopathy Ramakrishnan
Charlton Kilgore
Nelly Khidekel
Linda C Hsieh-Wilson
John T Simpson
Pradman K Qasba
Howard Hughes Medical Institute · USScience Applications International Corporation (United States) · USCalifornia Institute of Technology · US

Funding

Role of Fucosyl Saccharides and O-GlcNAc Glycosylation in Neuronal CommunicationR01GM084724 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HSIEH-WILSON, LINDA C · 2007 to 2016
$3.6M
Intramural NIH HHSNCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400NIGMS NIH HHS R01 GM084724
6 · The paper itself

Abstract

The mutant beta1,4-galactosyltransferase (beta4Gal-T1), beta4Gal-T1-Y289L, in contrast to wild-type beta4Gal-T1, can transfer GalNAc from the sugar donor UDP-GalNAc to the acceptor, GlcNAc, with efficiency as good as that of galactose from UDP-Gal. Furthermore, the mutant can also transfer a modified sugar, C2 keto galactose, from its UDP derivative to O-GlcNAc modification on proteins that provided a functional handle for developing a highly sensitive chemoenzymatic method for detecting O-GlcNAc post-translational modification on proteins. We report herein that the modified sugar, C2 keto galactose, can be transferred to free GlcNAc residues on N-linked glycoproteins, such as ovalbumin or asialo-agalacto IgG1. The transfer is strictly dependent on the presence of both the mutant enzyme and the ketone derivative of the galactose. Moreover, the PNGase F treatment of the glycoproteins, which cleaves the N-linked oligosaccharide chain, shows that the modified sugar has been transferred to the N-glycan chains of the glycoproteins and not to the protein portion. The application of the mutant galactosyltransferase, beta4Gal-T1-Y289L, to produce glycoconjugates carrying sugar moieties with reactive groups, is demonstrated. We envision a broad potential for this technology such as the possibilities to link cargo molecules to glycoproteins, such as monoclonal antibodies, via glycan chains, thereby assisting in the glycotargeting of drugs to the site of action or used as biological probes.

Indexed as

AcetylglucosamineAnimalsBiotinylationGalactoseGalactosyltransferasesGlycoconjugatesGlycoproteinsImmunoglobulin GKetosesMutationOvalbuminOxidation-ReductionPeptidesPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAcetylglucosaminebeta-1,4-galactosyltransferase IGalactoseGalactosyltransferasesGlycoconjugatesGlycoproteinsImmunoglobulin GKetosesOvalbuminPeptidesPolysaccharides

Identifiers

PMID17370997
PMCPMC3534963
OpenAlexW1972074273

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.