Evidence map›Paper›PMID 24713701›Full record

ArticleThe Journal of biological chemistry2014

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

Ee Phie Tan, Maria T Villar, Lezi E, Jianghua Lu, J Eva Selfridge, Antonio Artigues, Russell H Swerdlow, Chad Slawson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

61 citing papers in PubMed, 86 citations in OpenAlex.

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  14. Cells · 2022
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  16. MitochondrialCancers · 2021
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  17. ExcessiveCirculation · 2021
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  19. Review
  20. Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article

1 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

8 authors at 1 institution in 1 country.

Ee Phie TanFrom the Department of Biochemistry and Molecular Biology.
Maria T VillarFrom the Department of Biochemistry and Molecular Biology.
Lezi EDepartment of Neurology, and.
Jianghua LuDepartment of Neurology, and.
J Eva SelfridgeDepartment of Neurology, and.
Antonio ArtiguesFrom the Department of Biochemistry and Molecular Biology.
Russell H SwerdlowFrom the Department of Biochemistry and Molecular Biology, Department of Neurology, and University of Kansas Alzheimer's Disease Center, University of Kansas Medical Center, Kansas City, Kansas 64108.
Chad SlawsonFrom the Department of Biochemistry and Molecular Biology, University of Kansas Alzheimer's Disease Center, University of Kansas Medical Center, Kansas City, Kansas 64108 University of Kansas Cancer Center, cslawson@kumc.edu.
University of Kansas Medical Center · US

Funding

University of Kansas Alzheimer's Disease Core CentersP30AG035982 · NIA · UNIVERSITY OF KANSAS MEDICAL CENTER · PI SWERDLOW, RUSSELL H. · 2011 to 2020
$16.6M
Transgenic and Gener-Targeting CoreP20GM104936 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI SAADI, IRFAN · 2012 to 2016
$10.9M
Regulation of Globin Gene Switching by O-GlcNAc Post-Translational ModificationR01DK100595 · NIDDK · UNIVERSITY OF KANSAS MEDICAL CENTER · PI PETERSON, KENNETH R, SLAWSON, CHAD ERIC · 2014 to 2016
$788k
JEOL JEM-1400 Transmission Electron Microscope with AMT-XR611M Digital Camera SysS10RR027564 · NCRR · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ABRAHAMSON, DALE R · 2010 to 2010
$418k
NCRR NIH HHS S10 RR027564NIA NIH HHS P30 AG035982NIA NIH HHS P30AG035982NIDDK NIH HHS DK100595NIDDK NIH HHS R01 DK100595NIGMS NIH HHS 9P20GM104936NIGMS NIH HHS P20 GM104936NIGMS NIH HHS P20GM12345
6 · The paper itself

Abstract

Mitochondrial impairment is commonly found in many diseases such as diabetes, cancer, and Alzheimer disease. We demonstrate that the enzymes responsible for the addition or removal of the O-GlcNAc modification, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), respectively, are critical regulators of mitochondrial function. Using a SILAC (stable isotope labeling of amino acids in cell culture)-based proteomics screen, we quantified the changes in mitochondrial protein expression in OGT- and OGA-overexpressing cells. Strikingly, overexpression of OGT or OGA showed significant decreases in mitochondria-localized proteins involved in the respiratory chain and the tricarboxylic acid cycle. Furthermore, mitochondrial morphology was altered in these cells. Both cellular respiration and glycolysis were reduced in OGT/OGA-overexpressing cells. These data demonstrate that alterations in O-GlcNAc cycling profoundly affect energy and metabolite production.

Indexed as

Citric Acid CycleAcetylglucosaminebeta-N-AcetylhexosaminidasesCell Line, TumorElectron TransportGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticGlycolysisHumansImmunoblottingMass SpectrometryMicroscopy, ElectronMitochondriaMitochondrial ProteinsN-AcetylglucosaminyltransferasesProteomicsAcetylglucosaminebeta-N-Acetylhexosaminidaseshexosaminidase CMitochondrial ProteinsN-AcetylglucosaminyltransferasesUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferaseGlycobiologyGlycosylationMass Spectrometry (MS)MetabolomicsMitochondriaMitochondrial Metabolism

Identifiers

PMID24713701
PMCPMC4031527
OpenAlexW2068663943

What OpenQuestion holds

Textmetadata
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.