Evidence map›Paper›PMID 27655845›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2016

Global Analysis of O-GlcNAc Glycoproteins in Activated Human T Cells.

Peder J Lund, Joshua E Elias, Mark M Davis

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Frontiers in immunology · 2025
    Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. ProteinFrontiers in immunology · 2022
    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

3 authors at 2 institutions in 1 country.

Peder J LundInterdepartmental Program in Immunology, Stanford University, Stanford, CA 94305.ORCID 0000-0002-2146-8724
Joshua E EliasDepartment of Chemical and Systems Biology, Stanford University, Stanford, CA 94305.ORCID 0000-0002-8063-3259
Mark M DavisDepartment of Microbiology and Immunology, Stanford University, Stanford, CA 94305; mmdavis@stanford.edu.
Stanford University · USHoward Hughes Medical Institute · US

Funding

Using a tonsil organoid system to probe conditions for the induction of protective antibody and T cell responses to influenza.U19AI057229 · NIAID · STANFORD UNIVERSITY · PI Mark Morris Davis · 2003 to 2026
$88.5M
Vaccination and infection: indicators of immunological health and responsivenessU19AI090019 · NIAID · STANFORD UNIVERSITY · PI DAVIS, MARK MORRIS · 2010 to 2015
$17.3M
VECTOR COREP30NS069375 · NINDS · STANFORD UNIVERSITY · PI STEINBERG, GARY K · 2011 to 2019
$6.3M
T CELL RECEPTOR STRUCTURE AND EXPRESSIONR01AI022511 · NIAID · STANFORD UNIVERSITY · PI DAVIS, MARK MORRIS · 1985 to 2014
$3.3M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI022511NIAID NIH HHS U19 AI057229NIAID NIH HHS U19 AI090019NINDS NIH HHS P30 NS069375
6 · The paper itself

Abstract

T cell activation in response to Ag is largely regulated by protein posttranslational modifications. Although phosphorylation has been extensively characterized in T cells, much less is known about the glycosylation of serine/threonine residues by O-linked N-acetylglucosamine (O-GlcNAc). Given that O-GlcNAc appears to regulate cell signaling pathways and protein activity similarly to phosphorylation, we performed a comprehensive analysis of O-GlcNAc during T cell activation to address the functional importance of this modification and to identify the modified proteins. Activation of T cells through the TCR resulted in a global elevation of O-GlcNAc levels and in the absence of O-GlcNAc, IL-2 production and proliferation were compromised. T cell activation also led to changes in the relative expression of O-GlcNAc transferase (OGT) isoforms and accumulation of OGT at the immunological synapse of murine T cells. Using a glycoproteomics approach, we identified >200 O-GlcNAc proteins in human T cells. Many of the identified proteins had a functional relationship to RNA metabolism, and consistent with a connection between O-GlcNAc and RNA, inhibition of OGT impaired nascent RNA synthesis upon T cell activation. Overall, our studies provide a global analysis of O-GlcNAc dynamics during T cell activation and the first characterization, to our knowledge, of the O-GlcNAc glycoproteome in human T cells.

Indexed as

AcetylglucosamineAnimalsCell LineGlycoproteinsGlycosylationHumansLymphocyte ActivationMiceN-AcetylglucosaminyltransferasesProtein IsoformsProtein Processing, Post-TranslationalProteomicsReceptors, Antigen, T-CellSignal TransductionT-LymphocytesAcetylglucosamineGlycoproteinsN-AcetylglucosaminyltransferasesProtein IsoformsReceptors, Antigen, T-CellUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase

Identifiers

PMID27655845
PMCPMC5055199
OpenAlexW2522365421

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.