Evidence map›Paper›PMID 30414174›Full record

ReviewFEBS letters2018

Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O-GlcNAc).

Natasha E Zachara

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Trial
  2. Review
  3. PERM1 regulates mitochondrial energetics through O-GlcNAcylation in the heart.Journal of molecular and cellular cardiology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  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

1 author at 1 institution in 1 country.

Natasha E ZacharaDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Johns Hopkins Medicine · US

Funding

VERSICAN PROTEOLYSIS AND REGULATION OF VASCULAR SMOOTH MUSCLEP01HL107147 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI DWEIK, RAED A. · 2011 to 2017
$16.1M
Immersive Training in GlycosciencesK12HL141952 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HASCALL, VINCENT CHARLES, SCHNAAR, RONALD L · 2018 to 2022
$4.8M
Regulation of O-GlcNAcylation During InjuryR01HL139640 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI ZACHARA, NATASHA ELIZABETH · 2018 to 2021
$1.6M
Tuning and Tagging the O-GlcNAc ModificationU01CA230978 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZACHARA, NATASHA ELIZABETH · 2018 to 2020
$1.3M
NCI NIH HHS U01 CA230978NHLBI NIH HHS K12 HL141952NHLBI NIH HHS P01 HL107147NHLBI NIH HHS R01 HL139640
6 · The paper itself

Abstract

Almost 100 years after the first descriptions of proteins conjugated to carbohydrates (mucins), several studies suggested that glycoproteins were not restricted to the serum, extracellular matrix, cell surface, or endomembrane system. In the 1980s, key data emerged demonstrating that intracellular proteins were modified by monosaccharides of O-linked β-N-acetylglucosamine (O-GlcNAc). Subsequently, this modification was identified on thousands of proteins that regulate cellular processes as diverse as protein aggregation, localization, post-translational modifications, activity, and interactions. In this Review, we will highlight critical discoveries that shaped our understanding of the molecular events underpinning the impact of O-GlcNAc on protein function, the role that O-GlcNAc plays in maintaining cellular homeostasis, and our understanding of the mechanisms that regulate O-GlcNAc-cycling.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAcetylglucosamineAnimalsCytoplasmGlycoproteinsGlycosylationHomeostasisHumansN-AcetylglucosaminyltransferasesAcetylglucosamineGlycoproteinsN-Acetylglucosaminyltransferaseschaperoneglycosylationmetabolismphosphorylationsignal transduction

Identifiers

PMID30414174
PMCPMC6492276
OpenAlexW2899811847

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.