Evidence map›Paper›PMID 36306991›Full record

ArticleFree radical biology & medicine2022

A deep redox proteome profiling workflow and its application to skeletal muscle of a Duchenne Muscular Dystrophy model.

Nicholas J Day, Tong Zhang, Matthew J Gaffrey, Rui Zhao, Thomas L Fillmore, Ronald J Moore, George G Rodney, Wei-Jun Qian

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 20 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Nicholas J DayBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
Tong ZhangBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
Matthew J GaffreyBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
Rui ZhaoBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
Thomas L FillmoreBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
Ronald J MooreBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
George G RodneyDepartment of Integrative Physiology, Baylor College of Medicine, Houston, TX, 77030, USA.
Wei-Jun QianBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA. Electronic address: Weijun.Qian@pnnl.gov.
Pacific Northwest National Laboratory · USBaylor College of Medicine · US

Funding

ProMoTr: A Proteomics Center for MoTrPACU24DK112349 · NIDDK · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI Joshua N. Adkins · 2017 to 2026
$17.5M
Nox2-Calcium Signaling in Skeletal MuscleR01AR061370 · NIAMS · BAYLOR COLLEGE OF MEDICINE · PI RODNEY, GEORGE G · 2012 to 2021
$4.1M
Pathways and Regulators Driving Progressive Islet Cell Dysfunction in Type 1 DiabetesR01DK122160 · NIDDK · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI ROHIT N. KULKARNI, CLAYTON E MATHEWS · 2019 to 2026
$3.7M
Oxidized glutathione regulation of epithelial sodium channels in newborn lung injuryR01HL137033 · NHLBI · UNIVERSITY OF UTAH · PI HELMS, MY N. · 2018 to 2021
$1.5M
NHLBI NIH HHS R01 HL137033NIAMS NIH HHS R01 AR061370NIDDK NIH HHS R01 DK122160NIDDK NIH HHS U24 DK112349
6 · The paper itself

Abstract

Perturbation to the redox state accompanies many diseases and its effects are viewed through oxidation of biomolecules, including proteins, lipids, and nucleic acids. The thiol groups of protein cysteine residues undergo an array of redox post-translational modifications (PTMs) that are important for regulation of protein and pathway function. To better understand what proteins are redox regulated following a perturbation, it is important to be able to comprehensively profile protein thiol oxidation at the proteome level. Herein, we report a deep redox proteome profiling workflow and demonstrate its application in measuring the changes in thiol oxidation along with global protein expression in skeletal muscle from mdx mice, a model of Duchenne Muscular Dystrophy (DMD). In-depth coverage of the thiol proteome was achieved with >18,000 Cys sites from 5,608 proteins in muscle being quantified. Compared to the control group, mdx mice exhibit markedly increased thiol oxidation, where a ∼2% shift in the median oxidation occupancy was observed. Pathway analysis for the redox data revealed that coagulation system and immune-related pathways were among the most susceptible to increased thiol oxidation in mdx mice, whereas protein abundance changes were more enriched in pathways associated with bioenergetics. This study illustrates the importance of deep redox profiling in gaining greater insight into oxidative stress regulation and pathways/processes that are perturbed in an oxidizing environment.

Indexed as

Muscular Dystrophy, DuchenneAnimalsCysteineMiceMice, Inbred mdxMuscle, SkeletalOxidation-ReductionProteomeSulfhydryl CompoundsWorkflowCysteineProteomeSulfhydryl CompoundsPost-translational modificationsProtein thiolsRedox proteomicsSite occupancyStoichiometryThiol oxidation

Identifiers

PMID36306991
PMCPMC10072164
OpenAlexW4307585117

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.