Evidence map›Paper›PMID 30657688›Full record

ArticleAnalytical chemistry2019

O-GlcNAc Site Mapping by Using a Combination of Chemoenzymatic Labeling, Copper-Free Click Chemistry, Reductive Cleavage, and Electron-Transfer Dissociation Mass Spectrometry.

Junfeng Ma, Wei-Han Wang, Zengxia Li, Jeffrey Shabanowitz, Donald F Hunt, Gerald W Hart

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025
    Review
  3. Article
  4. Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Cells · 2022
    Review
  13. Article
  14. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  15. Role ofPhysiological reviews · 2021
    Review
  16. Mass Spectrometry for O-GlcNAcylation.Frontiers in chemistry · 2021
    Review
  17. Review
  18. Review
  19. Calculating Glycoprotein Similarities From Mass Spectrometric Data.Molecular & cellular proteomics : MCP · 2021
    Review
  20. Precision Mapping of O-LinkedJournal of the American Chemical Society · 2020
    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

6 authors at 3 institutions in 2 countries.

Junfeng MaDepartment of Biological Chemistry , The Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.ORCID 0000-0002-5183-5425
Wei-Han WangDepartment of Chemistry , University of Virginia , Charlottesville , Virginia 22904 , United States.
Zengxia LiDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences , Fudan University , Shanghai 200032 , China.
Jeffrey ShabanowitzDepartment of Chemistry , University of Virginia , Charlottesville , Virginia 22904 , United States.
Donald F HuntDepartment of Chemistry , University of Virginia , Charlottesville , Virginia 22904 , United States.
Gerald W HartDepartment of Biological Chemistry , The Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.
University of Virginia · USJohns Hopkins University · USFudan University · CN

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Cytosolic O-Glycosylation and Insulin SignalingR01DK061671 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2002 to 2014
$4.0M
Nutrient Regulation of Cell Physiology by O-GlcNAcylationR01GM116891 · NIGMS · UNIVERSITY OF GEORGIA · PI HART, GERALD WARREN · 2016 to 2023
$2.4M
NHLBI NIH HHS P01 HL107153NIDDK NIH HHS R01 DK061671NIGMS NIH HHS R01 GM037537NIGMS NIH HHS R01 GM116891
6 · The paper itself

Abstract

As a dynamic post-translational modification, O-linked β- N-acetylglucosamine ( O-GlcNAc) modification (i.e., O-GlcNAcylation) of proteins regulates many biological processes involving cellular metabolism and signaling. However, O-GlcNAc site mapping, a prerequisite for site-specific functional characterization, has been a challenge since its discovery. Herein we present a novel method for O-GlcNAc enrichment and site mapping. In this method, the O-GlcNAc moiety on peptides was labeled with UDP-GalNAz followed by copper-free azide-alkyne cycloaddition with a multifunctional reagent bearing a terminal cyclooctyne, a disulfide bridge, and a biotin handle. The tagged peptides were then released from NeutrAvidin beads upon reductant treatment, alkylated with (3-acrylamidopropyl)trimethylammonium chloride, and subjected to electron-transfer dissociation mass spectrometry analysis. After validation by using standard synthetic peptide gCTD and model protein α-crystallin, such an approach was applied to the site mapping of overexpressed TGF-β-activated kinase 1/MAP3K7 binding protein 2 (TAB2), with four O-GlcNAc sites unambiguously identified. Our method provides a promising tool for the site-specific characterization of O-GlcNAcylation of important proteins.

Indexed as

AcetylglucosamineAdaptor Proteins, Signal TransducingAlkynesalpha-CrystallinsAzidesClick ChemistryCycloaddition ReactionGlycosylationHEK293 CellsHumansOxidation-ReductionPeptidesProtein Processing, Post-TranslationalTandem Mass SpectrometryUridine Diphosphate N-AcetylgalactosamineAcetylglucosamineAdaptor Proteins, Signal TransducingAlkynesalpha-CrystallinsAzidesPeptidesTAB2 protein, humanUDP-N-azidoacetylgalactosamineUridine Diphosphate N-Acetylgalactosamine

Identifiers

PMID30657688
PMCPMC6756848
OpenAlexW2909102663

What OpenQuestion holds

Textmetadata
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.