Evidence map›Paper›PMID 39456860›Full record

ArticleInternational journal of molecular sciences2024

Peptide Activator Stabilizes DJ-1 Structure and Enhances Its Activity.

Jing-Yuan Shih, Yuan-Hao Howard Hsu

Abstract read
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In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

2 authors.

Jing-Yuan ShihDepartment of Chemistry, Tunghai University, No. 1727, Sec. 4, Taiwan Boulevard, Xitun District, Taichung 40704, Taiwan.
Yuan-Hao Howard HsuDepartment of Chemistry, Tunghai University, No. 1727, Sec. 4, Taiwan Boulevard, Xitun District, Taichung 40704, Taiwan.ORCID 0000-0002-3423-2892

Funding

National Science and Technology Council NSTC 112-2113-M-029-002National Science and Technology Council NSTC 113-2113-M-029-011National Science and Technology Council NSTC 113-2923-M-029 -002 -MY3National Science and Technology Countil NSTC 113-2113-M-029-003
6 · The paper itself

Abstract

DJ-1 is a vital enzyme involved in the maintenance of mitochondrial health, and its mutation has been associated with an increased risk of Parkinson's disease (PD). Effective regulation of DJ-1 activity is essential for the well-being of mitochondria, and DJ-1 is thus a potential target for PD drug development. In this study, two peptides (

Indexed as

PeptidesProtein Deglycase DJ-1Catalytic DomainHumansHydrogen Deuterium Exchange-Mass SpectrometryModels, MolecularParkinson DiseaseProtein BindingProtein MultimerizationPARK7 protein, humanPeptidesProtein Deglycase DJ-1DJ-1hydrogen/deuterium mass spectrometryPARK7Parkinson’s disease

Identifiers

PMID39456860
PMCPMC11508141

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.