Evidence map›Paper›PMID 35098223›Full record

ReviewJACS Au2022

Methods for Studying Site-Specific O-GlcNAc Modifications: Successes, Limitations, and Important Future Goals.

Stuart P Moon, Afraah Javed, Eldon R Hard, Matthew R Pratt

Abstract readReview
In one paragraph

Review in JACS Au, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025
    Review
  6. Article
  7. Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules.Journal of the American Chemical Society · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. 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

4 authors.

Stuart P MoonDepartments of Chemistry and Biological Sciences, University of Southern California, Los Angeles, California 90089, United States.
Afraah JavedDepartments of Chemistry and Biological Sciences, University of Southern California, Los Angeles, California 90089, United States.
Eldon R HardDepartments of Chemistry and Biological Sciences, University of Southern California, Los Angeles, California 90089, United States.
Matthew R PrattDepartments of Chemistry and Biological Sciences, University of Southern California, Los Angeles, California 90089, United States.ORCID https://orcid.org/0000-0003-3205-5615

Funding

Functional Analysis of O-GlcNAc using Synthetic Protein ChemistryR01GM114537 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2015 to 2024
$3.1M
Chemical Tools for the Investigation and Manipulation of Protein GlycosylationR01GM125939 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2017 to 2025
$2.4M
CBI: Chemistry Biology InterfaceT32GM118289 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FORSBURG, SUSAN L · 2016 to 2020
$1.2M
NIGMS NIH HHS R01 GM114537NIGMS NIH HHS R01 GM125939NIGMS NIH HHS T32 GM118289
6 · The paper itself

Abstract

O-GlcNAcylation is a dynamic post-translational modification which affects myriad proteins, cellular functions, and disease states. Its presence or absence modulates protein function via differential protein- and site-specific mechanisms, necessitating innovative techniques to probe the modification in highly selective manners. To this end, a variety of biological and chemical methods have been developed to study specific O-GlcNAc modification events both

Identifiers

PMID35098223
PMCPMC8791055

What OpenQuestion holds

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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.