Evidence map›Paper›PMID 41287418›Full record

ArticleChembiochem : a European journal of chemical biology2026

Multifaceted Effects of a Multiple Nitric Oxide Photoreleaser and its Photoproducts on Amyloid-β Aggregation.

Francesca Laneri, Cristina Parisi, Salvatore Sortino

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 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

3 authors.

Francesca LaneriPhotoChemLab, Department of Drug and Health Sciences, University of Catania, I-95125, Catania, Italy.
Cristina ParisiPhotoChemLab, Department of Drug and Health Sciences, University of Catania, I-95125, Catania, Italy.
Salvatore SortinoPhotoChemLab, Department of Drug and Health Sciences, University of Catania, I-95125, Catania, Italy.ORCID https://orcid.org/0000-0002-2086-1276

Funding

European Union-NextGenerationEU through the MUR-PNRR Projects PE_00000019 "HEAL ITALIA"
6 · The paper itself

Abstract

Aberrant aggregation of β-amyloid (Aβ) peptides into insoluble fibrils is recognized as one of the hallmarks of Alzheimer's disease (AD). Among the post-translational modifications influencing Aβ behavior, nitration and nitrosation by nitric oxide (NO) derivatives play a key role, though their impact on aggregation and toxicity remains unclear. This contribution explores the effects on Aβ aggregation induced by an NO photodonor (NOPD) releasing two NO molecules via a stepwise mechanism under the control of visible blue light. Significant reduction of protein aggregation is observed when a considerable amount NO (≈120 µM) is photoreleased during the early stages of the protein aggregation. In contrast, long-term release of a similar NO concentration is ineffective. On the other hand, proaggregative effect is induced by the NOPD kept in the dark. The stable photoproducts formed after the release of the first and the second molecule of NO also show a protein aggregation inhibitory effect both individually and in combination. Dynamic simulation studies are also reported to shed light on the binding of NOPD and its photoproducts with key Aβ

Indexed as

Amyloid beta-PeptidesNitric OxidePeptide FragmentsAlzheimer DiseaseHumansLightMolecular Dynamics SimulationPhotochemical ProcessesProtein AggregatesAmyloid beta-PeptidesNitric OxidePeptide FragmentsProtein AggregatesAlzheimeramyloidlightnitric oxideorganofluoride

Identifiers

PMID41287418
PMCPMC12781159

What OpenQuestion 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 OpenQuestion graph.