Evidence map›Paper›PMID 40305210›Full record

ArticleBiomolecules2025

Salt-Induced Membrane-Bound Conformation of the NAC Domain of α-Synuclein Leads to Structural Polymorphism of Amyloid Fibrils.

Ryota Imaura, Koichi Matsuo

Abstract read
In one paragraph

Article in Biomolecules, 2025. 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.

Ryota ImauraGraduate School of Advanced Science and Engineering, Hiroshima University, Higashi-Hiroshima 739-8511, Japan.
Koichi MatsuoGraduate School of Advanced Science and Engineering, Hiroshima University, Higashi-Hiroshima 739-8511, Japan.ORCID 0000-0001-8166-544X

Funding

Japan Society for the Promotion of Science 22 K06163 and 23H04597
6 · The paper itself

Abstract

α-Synuclein (αS) interacts with lipid membranes in neurons to form amyloid fibrils that contribute to Parkinson's disease, and its non-amyloid-β component domain is critical in the fibrillation. In this study, the salt (NaCl) effect on the membrane interaction and fibril formation of αS

Indexed as

alpha-SynucleinAmyloidSodium ChlorideHumansProtein ConformationProtein Domainsalpha-SynucleinAmyloidSodium Chloridelipid membranemembrane interaction mechanismnon-amyloid-β componentParkinson’s diseasepolymorphismprotein aggregationsynchrotron radiation circular dichroismα-synuclein

Identifiers

PMID40305210
PMCPMC12024755

What OpenQuestion holds

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LicenceCC BY
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.