Evidence map›Paper›PMID 36076282›Full record

ArticleActa neuropathologica communications2022

Protein citrullination marks myelin protein aggregation and disease progression in mouse ALS models.

Issa O Yusuf, Tao Qiao, Sepideh Parsi, Ronak Tilvawala, Paul R Thompson, Zuoshang Xu

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-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

21 citing papers in PubMed, 23 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

6 authors at 3 institutions in 3 countries.

Issa O YusufDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Medical School, Worcester, MA, 01605, USA.
Tao QiaoDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Medical School, Worcester, MA, 01605, USA.
Sepideh ParsiDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Medical School, Worcester, MA, 01605, USA.
Ronak TilvawalaDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Medical School, Worcester, MA, 01605, USA.
Paul R ThompsonDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Medical School, Worcester, MA, 01605, USA.
Zuoshang XuDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Medical School, Worcester, MA, 01605, USA. zuoshang.xu@umassmed.edu.ORCID 0000-0003-1209-334X
University of Massachusetts Chan Medical School · USAstellas Pharma (Japan) · JPHarvard University · US

Funding

Synthetic Chemical Biology CoreP20GM113117 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI OROZCO, ROBIN C. · 2016 to 2025
$23.9M
Chemical probes to decipher PAD biologyR35GM118112 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Paul R Thompson · 2016 to 2026
$9.5M
Protein Arginine Deiminase 2 (PAD2) and Protein Citrullination in ALSR01NS118145 · NINDS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI XU, ZUOSHANG · 2021 to 2025
$2.4M
An in vivo approach to understanding mutant PFN1 toxicity on motor neuronsR01NS101895 · NINDS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI XU, ZUOSHANG · 2017 to 2021
$1.8M
NIGMS NIH HHS P20 GM113117NIGMS NIH HHS R35 GM118112NINDS NIH HHS R01 NS101895NINDS NIH HHS R01 NS118145
6 · The paper itself

Abstract

Increased protein citrullination (PC) and dysregulated protein arginine deiminase (PAD) activity have been observed in several neurodegenerative diseases. PC is a posttranslational modification catalyzed by the PADs. PC converts peptidyl-arginine to peptidyl-citrulline, thereby reducing the positive charges and altering structure and function of proteins. Of the five PADs, PAD2 is the dominant isoform in the central nervous system (CNS). Abnormal PC and PAD dysregulation are associated with numerous pathological conditions, including inflammatory diseases and neurodegeneration. Animal model studies have shown therapeutic efficacy from inhibition of PADs, thus suggesting a role of PC in pathogenesis. To determine whether PC contribute to amyotrophic lateral sclerosis (ALS), a deadly neurodegenerative disease characterized by loss of motor neurons, paralysis, and eventual death, we investigated alterations of PC and PAD2 in two different transgenic mouse models of ALS expressing human mutant SOD1

Indexed as

Amyotrophic Lateral SclerosisNeurodegenerative DiseasesAnimalsCitrullinationDisease Models, AnimalDisease ProgressionGliosisHumansMiceMice, TransgenicMotor NeuronsMyelin ProteinsMyelin SheathProfilinsProtein AggregatesSpinal CordMyelin ProteinsPFN1 protein, humanProfilinsProtein AggregatesSuperoxide DismutaseAstrogliosisDeiminationMyelin degenerationNeurodegenerationNeurodegenerative diseaseProtein aggregation

Identifiers

PMID36076282
PMCPMC9458309
OpenAlexW4294970390

What OpenQuestion holds

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LicenceCC BY
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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.