Evidence map›Paper›PMID 40097723›Full record

ArticleScientific reports2025

Preclinical assessment of a ganglioside-targeted therapy for Parkinson's disease with the first-in-class adaptive peptide AmyP53.

Jacques Fantini, Fodil Azzaz, Anaïs Aulas, Henri Chahinian, Nouara Yahi

Erratum issuedAbstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. 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. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Jacques FantiniAix Marseille Univ, INSERM UA16, Marseille, France. jacques.fantini@univ-amu.fr.
Fodil AzzazAix Marseille Univ, INSERM UA16, Marseille, France.
Anaïs AulasAmyPore, Septèmes-les-Vallons, France.
Henri ChahinianAix Marseille Univ, INSERM UA16, Marseille, France.
Nouara YahiAix Marseille Univ, INSERM UA16, Marseille, France.

Funding

AmyPore Private funding
6 · The paper itself

Abstract

We propose a new concept for the treatment of Parkinson's disease (PD), which considers that its root cause, α-synuclein, is an intrinsically disordered protein (IDP) difficult to target by classic approaches. Upon binding to lipid raft gangliosides, α-synuclein shifts from random coil to α-helix, forming Ca

Indexed as

alpha-SynucleinGangliosidesParkinson DiseasePeptidesAmyloid beta-PeptidesAnimalsDisease Models, AnimalDopaminergic NeuronsHumansMicealpha-SynucleinAmyloid beta-PeptidesGangliosidesPeptidesAdaptive peptideAlzheimerCalcium homeostasisGangliosideIDPLipid raftParkinsonPore-like annular oligomerSynucleopathiesTherapy

Identifiers

PMID40097723
PMCPMC11914484

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.