Evidence map›Paper›PMID 28488703›Full record

ReviewNature reviews. Molecular cell biology2017

Protein O-GlcNAcylation: emerging mechanisms and functions.

Xiaoyong Yang, Kevin Qian

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 727 papers.

0numbers the graph read from it
0cells of the map it votes in
727citing papers in PubMed
34.5field-weighted citation impact, top 1% 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

727 citing papers in PubMed, 1,181 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Cracking the code to O-GlcNAcylation networks.Nature chemical biology · 2026
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

667 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Xiaoyong YangProgram in Integrative Cell Signaling and Neurobiology of Metabolism, Department of Comparative Medicine, Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
Kevin QianProgram in Integrative Cell Signaling and Neurobiology of Metabolism, Department of Comparative Medicine, Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
Yale University · US

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Yale Liver CenterP30DK034989 · NIDDK · YALE UNIVERSITY · PI YASUKO IWAKIRI · 1986 to 2026
$31.1M
UCLA-Caltech Medical Scientist Training ProgramT32GM008042 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AJIJOLA, OLUJIMI A, DAWSON, DAVID WAYNE · 1985 to 2023
$29.9M
Translational CoreP01DK057751 · NIDDK · YALE UNIVERSITY · PI NATHANSON, MICHAEL H · 2001 to 2020
$25.6M
O-GlcNAc Modification in Metabolic HomeostasisR01DK089098 · NIDDK · YALE UNIVERSITY · PI YANG, XIAOYONG · 2010 to 2021
$3.0M
O-GlcNAc Signaling in Central Control of Energy BalanceR01DK102648 · NIDDK · YALE UNIVERSITY · PI YANG, XIAOYONG · 2016 to 2019
$1.8M
NCATS NIH HHS UL1 TR001863NIDDK NIH HHS P01 DK057751NIDDK NIH HHS P30 DK034989NIDDK NIH HHS R01 DK089098NIDDK NIH HHS R01 DK102648
6 · The paper itself

Abstract

O-GlcNAcylation - the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to cytoplasmic, nuclear and mitochondrial proteins - is a post-translational modification that regulates fundamental cellular processes in metazoans. A single pair of enzymes - O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) - controls the dynamic cycling of this protein modification in a nutrient- and stress-responsive manner. Recent years have seen remarkable advances in our understanding of O-GlcNAcylation at levels that range from structural and molecular biology to cell signalling and gene regulation to physiology and disease. New mechanisms and functions of O-GlcNAcylation that are emerging from these recent developments enable us to begin constructing a unified conceptual framework through which the significance of this modification in cellular and organismal physiology can be understood.

Indexed as

AcetylglucosamineAnimalsHumansN-AcetylglucosaminyltransferasesProtein Processing, Post-TranslationalProteinsSignal TransductionAcetylglucosamineN-AcetylglucosaminyltransferasesO-GlcNAc transferaseProteins

Identifiers

PMID28488703
PMCPMC5667541
OpenAlexW2613539552

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.