Evidence map›Paper›PMID 41992414›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Carboranyl-Curcuminoids for the Neutron Capture-Based Treatment of Amyloid Aggregates in Alzheimer's Disease.

Sebastiano Micocci, Stefano Parisotto, Diego Alberti, Alberto Lanfranco, Valeria Bitonto, Polyssena Renzi, Martina Salmi, Andrea Magnani, Federica Dal Bello, Katiuscia Pagano and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. 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. 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

14 authors.

Sebastiano MicocciDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Torino, Italy.
Stefano ParisottoDepartment of Chemistry, University of Torino, Torino, Italy.
Diego AlbertiDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Torino, Italy.ORCID https://orcid.org/0000-0002-4842-1109
Alberto LanfrancoDepartment of Chemistry, University of Torino, Torino, Italy.
Valeria BitontoDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Torino, Italy.
Polyssena RenziDepartment of Chemistry, University of Torino, Torino, Italy.ORCID https://orcid.org/0000-0002-1326-8183
Martina SalmiDepartment of Chemistry, University of Torino, Torino, Italy.
Andrea MagnaniDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Torino, Italy.
Federica Dal BelloDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Torino, Italy.ORCID https://orcid.org/0000-0003-0726-3025
Katiuscia PaganoIstituto Di Scienze e Tecnologie Chimiche "Giulio Natta" (SCITEC), National Council of Research (CNR), Milano, Italy.
Laura RagonaIstituto Di Scienze e Tecnologie Chimiche "Giulio Natta" (SCITEC), National Council of Research (CNR), Milano, Italy.
Nicoletta ProttiDepartment of Physics "A. Volta", University of Pavia, Pavia, Italy.ORCID https://orcid.org/0000-0002-2415-128X
Annamaria DeagostinoDepartment of Chemistry, University of Torino, Torino, Italy.ORCID https://orcid.org/0000-0003-2622-2798
Simonetta Geninatti CrichDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Torino, Italy.ORCID https://orcid.org/0000-0003-2998-5424

Funding

Compagnia di San Paolo D13C25000220007)Dipartimenti di Eccellenza D13C22003520001H2020 Future and Emerging Technologies 964934
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive cognitive decline. The aggregation of amyloid-beta (Aβ) peptides into oligomers and fibrils is central to its pathogenesis. While oligomers represent the most neurotoxic species, larger aggregates serve as reservoirs, maintaining pathological Aβ levels. To our knowledge, this study is the first to investigate Boron Neutron Capture Therapy (BNCT) as a method to selectively destabilize Aβ aggregates. This is achieved by inducing structural modifications in the Aβ peptide, aiming to convert fibrils into innocuous species. The approach utilizes

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBoron Neutron Capture TherapyCurcuminProtein Aggregation, PathologicalHumansProtein AggregatesAmyloid beta-PeptidesCurcuminProtein AggregatesAlzheimer's diseaseamyloid‐βBNCTmonocarbonyl curcumin derivativesprotein oxidation

Identifiers

PMID41992414
PMCPMC13335006

What OpenQuestion holds

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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.