Evidence map›Paper›PMID 40780286›Full record

ReviewACS nano2025

Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.

María G Herrera, Lidia Ciccone, Lara H Moleiro, Nicolo Tonali, Verónica Isabel Dodero

Abstract readReview
In one paragraph

Review in ACS nano, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  3. 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

5 authors.

María G HerreraLaboratorio de Genómica e Ingeniería de Sistemas Biológicos, Instituto de Biociencias, Biotecnología y Biología Traslacional (iB3), Departamento de Fisiología y Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Intendente Güiraldes 2160, Ciudad Autónoma de Buenos Aires C1428EGA, Argentina.ORCID 0000-0002-8874-7410
Lidia CicconeUniversity of Pisa, Department of Pharmacy, Via Bonanno 6, 56124 Pisa, Italy.ORCID 0000-0002-2762-1929
Lara H MoleiroDepartment of Physical Chemistry, Universidad Complutense de Madrid, Ciudad Universitaria s/n E28040 Madrid, Spain.ORCID 0000-0002-5580-9574
Nicolo TonaliCEA Saclay, DRF/JOLIOT/DMTS/SIMoS, 91191 Gif-sur-Yvette, France.ORCID 0000-0002-1435-5676
Verónica Isabel DoderoBielefeld University, Faculty of Chemistry, Universitätsstr. 25, 33615 Bielefeld, Germany.ORCID 0000-0001-7937-1880

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The self-assembly of endogenous and exogenous peptides into proteolysis-resistant oligomers can trigger toxic cellular events and diseases. In Alzheimer's disease (AD), the structural polymorphisms of endogenous amyloid-β (Aβ) 1-40 and 1-42 aggregates are essential for their neurotoxic effects. Recent findings on structural differences between brain-derived and

Indexed as

Amyloid beta-PeptidesGliadinGlutensTriticumAlzheimer DiseaseCeliac DiseaseHumansNanostructuresPeptide FragmentsPolymerizationProtein Structure, TertiaryAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)GliadinGlutensPeptide FragmentsAlzheimer’s diseaseataxiaAβ40/42celiac diseasegliadin peptidesgluten-related disordersoligomerspolyproline helix IIβ-sheet

Identifiers

PMID40780286
PMCPMC12410374

What Socratic holds

Textmetadata
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 Socratic graph.