Evidence map›Paper›PMID 27213235›Full record

ArticleJournal of proteome research2016

Comparative Proteomics Reveals Dysregulated Mitochondrial O-GlcNAcylation in Diabetic Hearts.

Junfeng Ma, Partha Banerjee, Stephen A Whelan, Ting Liu, An-Chi Wei, Genaro Ramirez-Correa, Mark E McComb, Catherine E Costello, Brian O'Rourke, Anne Murphy and 1 more

Abstract readComparative Study
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

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  19. ProteinMetabolites · 2022
    Review
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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

11 authors.

Junfeng Ma
Partha Banerjee
Stephen A WhelanDepartment of Biochemistry, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Ting Liu
An-Chi Wei
Genaro Ramirez-Correa
Mark E McCombDepartment of Biochemistry, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Catherine E CostelloDepartment of Biochemistry, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Brian O'Rourke
Anne Murphy
Gerald W Hart

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Cytosolic O-Glycosylation and Insulin SignalingR01DK061671 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2002 to 2014
$4.0M
ENERGETIC REGULATION OF CARDIAC ION CHANNELSR37HL054598 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI O'ROURKE, BRIAN · 2005 to 2014
$3.7M
Redox Modification of the Arrhythmic Substrate in Heart FailureR01HL105216 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI O'ROURKE, BRIAN, TRAYANOVA, NATALIA A. · 2011 to 2014
$3.0M
ENERGETIC REGULATION OF CARDIAC ION CHANNELSR01HL054598 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI O'ROURKE, BRIAN · 1996 to 2004
$1.6M
Seahorse Bioscience Extracellular Flux AnalyzerS10RR026474 · NCRR · JOHNS HOPKINS UNIVERSITY · PI O'ROURKE, BRIAN · 2011 to 2011
$181k
NCRR NIH HHS S10 RR026474NHLBI NIH HHS HHSN268201000031CNHLBI NIH HHS HHSN268201000032CNHLBI NIH HHS P01 HL107153NHLBI NIH HHS R01 HL054598NHLBI NIH HHS R01 HL105216NIDDK NIH HHS R01 DK061671NIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

O-linked β-N-acetylglucosamine (O-GlcNAc), a post-translational modification on serine and threonine residues of many proteins, plays crucial regulatory roles in diverse biological events. As a nutrient sensor, O-GlcNAc modification (O-GlcNAcylation) on nuclear and cytoplasmic proteins underlies the pathology of diabetic complications including cardiomyopathy. However, mitochondrial O-GlcNAcylation, especially in response to chronic hyperglycemia in diabetes, has been poorly explored. We performed a comparative O-GlcNAc profiling of mitochondria from control and streptozotocin (STZ)-induced diabetic rat hearts by using an improved β-elimination/Michael addition with isotopic DTT reagents (BEMAD) followed by tandem mass spectrometric analysis. In total, 86 mitochondrial proteins, involved in diverse pathways, were O-GlcNAcylated. Among them, many proteins have site-specific alterations in O-GlcNAcylation in response to diabetes, which suggests that protein O-GlcNAcylation is a novel layer of regulation mediating adaptive changes in mitochondrial metabolism during the progression of diabetic cardiomyopathy.

Indexed as

AcetylglucosamineAcylationAnimalsDiabetes Mellitus, ExperimentalDiabetic CardiomyopathiesMitochondriaMitochondrial ProteinsMyocardiumProteomicsRatsTandem Mass SpectrometryAcetylglucosamineMitochondrial Proteinsdiabetic cardiomyopathymass spectrometrymitochondriaO-GlcNAcomeO-GlcNAcylationproteomicspyruvate dehydrogenase

Identifiers

PMID27213235
PMCPMC7814404

What OpenQuestion holds

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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.