Evidence map›Paper›PMID 31155058›Full record

ArticleMethods in enzymology2019

Identifying potentially O-GlcNAcylated proteins using metabolic labeling, bioorthogonal enrichment, and Western blotting.

Narek Darabedian, Matthew R Pratt

Abstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. [Precise identification ofSe pu = Chinese journal of chromatography · 2021
    Article
  6. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  7. Precision Mapping of O-LinkedJournal of the American Chemical Society · 2020
    Article
  8. 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

2 authors at 1 institution in 1 country.

Narek DarabedianDepartment of Chemistry, University of Southern California, Los Angeles, CA, United States.
Matthew R PrattDepartment of Chemistry, University of Southern California, Los Angeles, CA, United States; Department of Biological Sciences, University of Southern California, Los Angeles, CA, United States. Electronic address: matthew.pratt@usc.edu.
University of Southern California · US

Funding

Chemical Tools for the Investigation and Manipulation of Protein GlycosylationR01GM125939 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2017 to 2025
$2.4M
NIGMS NIH HHS R01 GM125939
6 · The paper itself

Abstract

O-GlcNAcylation is a widespread posttranslational modification of intracellular proteins. Phenotypic and genetic experiments have established key roles for O-GlcNAc in development, mammalian cell survival, and several human diseases. However, the underlying mechanisms by which this modification alters biological pathways are still being discovered. An important part of this discovery process is the discovery of O-GlcNAcylated proteins, where chemical approaches have been particularly powerful. Here we describe how to combine one of these approaches, metabolic chemical reporters (MCRs), with bioorthogonal chemistry and Western blotting to identify potentially O-GlcNAcylated proteins.

Indexed as

AcetylglucosamineAnimalsBlotting, WesternClick ChemistryElectrophoresis, Polyacrylamide GelGlycosylationHumansProtein Processing, Post-TranslationalProteinsAcetylglucosamineProteinsBioorthogonalBiotin enrichmentClick chemistryMetabolic chemical reporterO-GlcNAc

Identifiers

PMID31155058
PMCPMC6860911
OpenAlexW2922259687

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.