Evidence map›Paper›PMID 29887419›Full record

ReviewCellular immunology2018

Too sweet to resist: Control of immune cell function by O-GlcNAcylation.

Tristan de Jesus, Sudhanshu Shukla, Parameswaran Ramakrishnan

Abstract readReview
In one paragraph

Review in Cellular immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. O-GlcNAcylation: Crosstalk between Hemostasis, Inflammation, and Cancer.International journal of molecular sciences · 2024
    Review
  2. A Metabolic Axis of Immune Intractability.Cancer immunology research · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Differences in Metabolite Composition ofMolecules (Basel, Switzerland) · 2022
    Article
  8. Article
  9. The Beginner's Guide toFrontiers in immunology · 2022
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  17. Regulation of B-cell function by NF-kappaB c-Rel in health and disease.Cellular and molecular life sciences : CMLS · 2020
    Review
  18. Review
  19. Review
  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

3 authors.

Tristan de JesusDepartment of Pathology, School of Medicine, Case Western Reserve University, 6526, Wolstein Research Building, 2103 Cornell Road, Cleveland, OH 44106, USA.
Sudhanshu ShuklaDepartment of Pathology, School of Medicine, Case Western Reserve University, 6526, Wolstein Research Building, 2103 Cornell Road, Cleveland, OH 44106, USA.
Parameswaran RamakrishnanDepartment of Pathology, School of Medicine, Case Western Reserve University, 6526, Wolstein Research Building, 2103 Cornell Road, Cleveland, OH 44106, USA. Electronic address: pxr150@case.edu.

Funding

TRAINING IN INVESTIGATIVE AND MOLECULAR DERMATOLOGYT32AR007569 · NIAMS · CASE WESTERN RESERVE UNIVERSITY · PI COOPER, KEVIN D · 1991 to 2019
$2.7M
Transcriptional regulation by O-GlcNAcylation in T lymphocytesR01AI116730 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI RAMAKRISHNAN, PARAMESWARAN · 2016 to 2020
$2.0M
NIAID NIH HHS R01 AI116730NIAMS NIH HHS T32 AR007569
6 · The paper itself

Abstract

O-linked β-N-acetyl glucosamine modification (O-GlcNAcylation) is a dynamic, reversible posttranslational modification of cytoplasmic and nuclear proteins. O-GlcNAcylation depends on nutrient availability and the hexosamine biosynthetic pathway (HBP), which produces the donor substrate UDP-GlcNAc. O-GlcNAcylation is mediated by a single enzyme, O-GlcNAc transferase (OGT), which adds GlcNAc and another enzyme, O-GlcNAcase (OGA), which removes O-GlcNAc from proteins. O-GlcNAcylation controls vital cellular processes including transcription, translation, the cell cycle, metabolism, and cellular stress. Aberrant O-GlcNAcylation has been implicated in various pathologies including Alzheimer's disease, diabetes, obesity, and cancer. Growing evidences indicate that O-GlcNAcylation plays crucial roles in regulating immunity and inflammatory responses, especially under hyperglycemic conditions. This review will highlight the emerging functions of O-GlcNAcylation in mammalian immunity under physiological and various pathological conditions.

Indexed as

AcylationAnimalsHumansImmunityInflammationN-AcetylglucosaminyltransferasesN-AcetylglucosaminyltransferasesO-GlcNAc transferaseImmunityLymphocytesMacrophagesNeutrophilsNFATNF-κBOGAO-GlcNAcylationOGTPhosphorylation

Identifiers

PMID29887419
PMCPMC6275141

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.