Evidence map›Paper›PMID 38253209›Full record

ArticleNeurobiology of disease2024

PAD2 dysregulation and aberrant protein citrullination feature prominently in reactive astrogliosis and myelin protein aggregation in sporadic ALS.

Issa O Yusuf, Sepideh Parsi, Lyle W Ostrow, Robert H Brown, Paul R Thompson, Zuoshang Xu

Open access · goldAbstract read
In one paragraph

Article in Neurobiology of disease, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. 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

6 authors at 3 institutions in 1 country.

Issa O YusufDepartment 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; Center for Systems Biology, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02110, USA.
Lyle W OstrowDepartment of Neurology, Lewis Katz School of Medicine at Temple University, Philadelphia, PA 19140, USA.
Robert H BrownDepartment of Neurology, RNA Therapeutic Institute, Neuroscience Program, University of Massachusetts Medical School, Worcester, MA, USA.
Paul R ThompsonDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Medical School, Worcester, MA 01605, USA; Program in Chemical Biology, 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. Electronic address: zuoshang.xu@umassmed.edu.
University of Massachusetts Chan Medical School · USHarvard University · USTemple University · US

Funding

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
NIGMS NIH HHS R35 GM118112NINDS NIH HHS R01 NS118145
6 · The paper itself

Abstract

Alteration in protein citrullination (PC), a common posttranslational modification (PTM), contributes to pathogenesis in various inflammatory disorders. We previously reported that PC and protein arginine deiminase 2 (PAD2), the predominant enzyme isoform that catalyzes this PTM in the central nervous system (CNS), are altered in mouse models of amyotrophic lateral sclerosis (ALS). We now demonstrate that PAD2 expression and PC are altered in human postmortem ALS spinal cord and motor cortex compared to controls, increasing in astrocytes while trending lower in neurons. Furthermore, PC is enriched in protein aggregates that contain the myelin proteins PLP and MBP in ALS. These results confirm our findings in ALS mouse models and suggest that altered PAD2 and PC contribute to neurodegeneration in ALS.

Indexed as

Amyotrophic Lateral SclerosisCitrullinationAnimalsGliosisHumansHydrolasesMiceMyelin ProteinsMyelin SheathProtein AggregatesProtein-Arginine DeiminasesProtein-Arginine Deiminase Type 2ProteinsSpinal CordHydrolasesMyelin ProteinsPADI2 protein, humanProtein AggregatesProtein-Arginine DeiminasesProtein-Arginine Deiminase Type 2ProteinsDeiminationMyelin degenerationNeurodegenerationNeurodegenerative diseaseNeuroinflammationProtein aggregation

Identifiers

PMID38253209
PMCPMC11003460
OpenAlexW4391062831

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.