Evidence map›Paper›PMID 34004049›Full record

ArticleCurrent protocols2021

Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.

Kamau Fahie, Bhargavi Narayanan, Fiddia Zahra, Russell Reeves, Steve M Fernandes, Gerald W Hart, Natasha E Zachara

Open access · hybridAbstract read
In one paragraph

Article in Current protocols, 2021. 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
0.9field-weighted citation impact, top 27% 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, 11 citations in OpenAlex.

  1. Tissue-Specific Profiling ofBio-protocol · 2025
    Article
  2. Review
  3. Article
  4. Best practices in assessing cardiac proteinAmerican journal of physiology. Heart and circulatory physiology · 2023
    Article
  5. Article
  6. Review
  7. 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

7 authors at 4 institutions in 1 country.

Kamau FahieThe Johns Hopkins University School of Medicine, Baltimore, Maryland.
Bhargavi NarayananThe Johns Hopkins University School of Medicine, Baltimore, Maryland.
Fiddia ZahraThe Johns Hopkins University School of Medicine, Baltimore, Maryland.
Russell ReevesThe Johns Hopkins University School of Medicine, Baltimore, Maryland.
Steve M FernandesThe Johns Hopkins University School of Medicine, Baltimore, Maryland.
Gerald W HartComplex Carbohydrate Research Center, University of Georgia, Athens, Georgia.
Natasha E ZacharaThe Johns Hopkins University School of Medicine, Baltimore, Maryland.
Johns Hopkins Medicine · USJohns Hopkins University · USThomas Jefferson University Hospital · USUniversity of Georgia · US

Funding

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 R01 HL139640NIH HHS K12HL141952NIH HHS RO1HL139640NIH HHS U01 CA230978
6 · The paper itself

Abstract

O-GlcNAc is a common post-translational modification of nuclear, mitochondrial, and cytoplasmic proteins that regulates normal physiology and the cell stress response. Dysregulation of O-GlcNAc cycling is implicated in the etiology of type II diabetes, heart failure, hypertension, and Alzheimer's disease, as well as cardioprotection. These protocols cover simple and comprehensive techniques for detecting proteins modified by O-GlcNAc and studying the enzymes that add or remove O-GlcNAc. © 2021 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Increasing the stoichiometry of O-GlcNAc on proteins before analysis Basic Protocol 2: Detection of proteins modified by O-GlcNAc using antibodies Basic Protocol 3: Detection of proteins modified by O-GlcNAc using the lectin sWGA Support Protocol 1: Control for O-linked glycosylation Basic Protocol 4: Detection and enrichment of proteins using WGA-agarose Support Protocol 2: Digestion of proteins with hexosaminidase Alternate Protocol: Detection of proteins modified by O-GlcNAc using galactosyltransferase Support Protocol 3: Autogalactosylation of galactosyltransferase Support Protocol 4: Assay of galactosyltransferase activity Basic Protocol 5: Characterization of labeled glycans by β-elimination and chromatography Basic Protocol 6: Detection of O-GlcNAc in 96-well plates Basic Protocol 7: Assay for OGT activity Support Protocol 5: Desalting of O-GlcNAc transferase Basic Protocol 8: Assay for O-GlcNAcase activity.

Indexed as

AcetylglucosamineDiabetes Mellitus, Type 2Cell NucleusGlycosylationHumansProtein Processing, Post-TranslationalAcetylglucosamineanalysisdetectiongalactosyltransferaseglycosylationO-GlcNAcO-linkedsignal transduction

Identifiers

PMID34004049
PMCPMC8862748
OpenAlexW3169112280

What OpenQuestion holds

Textmetadata
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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.