Evidence map›Paper›PMID 34502531›Full record

ArticleInternational journal of molecular sciences2021

OGT Protein Interaction Network (OGT-PIN): A Curated Database of Experimentally Identified Interaction Proteins of OGT.

Junfeng Ma, Chunyan Hou, Yaoxiang Li, Shufu Chen, Ci Wu

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.7field-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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Pooled it
  2. Cracking the code to O-GlcNAcylation networks.Nature chemical biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025
    Review
  7. Article
  8. Review
  9. Dissecting OGT's TPR domain to identify determinants of cellular function.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Article
  12. Review
  13. Cells · 2023
    Review
  14. Review
  15. Article
  16. Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022
    Article
  17. Article
  18. Targeting ProteinCells · 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

5 authors at 3 institutions in 2 countries.

Junfeng MaLombardi Comprehensive Cancer Center, Department of Oncology, Georgetown University Medical Center, Washington, DC 20057, USA.ORCID 0000-0002-5183-5425
Chunyan HouDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Yaoxiang LiLombardi Comprehensive Cancer Center, Department of Oncology, Georgetown University Medical Center, Washington, DC 20057, USA.ORCID 0000-0001-9200-1016
Shufu ChenSchool of Engineering, Pennsylvania State University Behrend, Erie, PA 16563, USA.
Ci WuLombardi Comprehensive Cancer Center, Department of Oncology, Georgetown University Medical Center, Washington, DC 20057, USA.
Georgetown University · USDalian Institute of Chemical Physics · CNPennsylvania State University · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI Louis M Weiner · 1990 to 2026
$71.5M
NCI NIH HHS P30 CA051008
6 · The paper itself

Abstract

Interactions between proteins are essential to any cellular process and constitute the basis for molecular networks that determine the functional state of a cell. With the technical advances in recent years, an astonishingly high number of protein-protein interactions has been revealed. However, the interactome of O-linked N-acetylglucosamine transferase (OGT), the sole enzyme adding the O-linked β-N-acetylglucosamine (O-GlcNAc) onto its target proteins, has been largely undefined. To that end, we collated OGT interaction proteins experimentally identified in the past several decades. Rigorous curation of datasets from public repositories and O-GlcNAc-focused publications led to the identification of up to 929 high-stringency OGT interactors from multiple species studied (including

Indexed as

Protein Interaction MapsProtein Processing, Post-TranslationalAcetylglucosamineAnimalsArabidopsis ProteinsDatabases, ProteinData CurationDrosophila ProteinsHumansMiceN-AcetylglucosaminyltransferasesRatsAcetylglucosamineArabidopsis ProteinsDrosophila ProteinsN-AcetylglucosaminyltransferasesUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferasedatabaseO-GlcNAcOGTOGT interactomeprotein–protein interactions

Identifiers

PMID34502531
PMCPMC8431785
OpenAlexW3198700986

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.