Evidence map›Paper›PMID 41641241›Full record

ArticleRSC advances2026

A Ru(ii)-arene complex with promising anti-Aβ activity.

Ryan M Hacker, Jacob J Smith, David C Platt, Maria I Loughlin, Emma N Grabowski, William W Brennessel, Marjorie A Jones, Michael I Webb

Abstract read
In one paragraph

Article in RSC advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Ryan M HackerDepartment of Chemistry & Biochemistry, SUNY Geneseo Geneseo NY 14454 USA mwebb@geneseo.edu.
Jacob J SmithDepartment of Chemistry & Biochemistry, SUNY Geneseo Geneseo NY 14454 USA mwebb@geneseo.edu.
David C PlattDepartment of Chemistry, Illinois State University Normal IL 61790 USA.
Maria I LoughlinDepartment of Chemistry & Biochemistry, SUNY Geneseo Geneseo NY 14454 USA mwebb@geneseo.edu.
Emma N GrabowskiDepartment of Chemistry & Biochemistry, SUNY Geneseo Geneseo NY 14454 USA mwebb@geneseo.edu.
William W BrennesselDepartment of Chemistry, University of Rochester Rochester NY 14627 USA.ORCID https://orcid.org/0000-0001-5461-1825
Marjorie A JonesDepartment of Chemistry, Illinois State University Normal IL 61790 USA.ORCID https://orcid.org/0000-0002-6306-0700
Michael I WebbDepartment of Chemistry & Biochemistry, SUNY Geneseo Geneseo NY 14454 USA mwebb@geneseo.edu.ORCID https://orcid.org/0000-0002-4708-2694

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Agents that target the amyloid-beta (Aβ) peptide associated with Alzheimer's disease have seen renewed interest following recent the clinical success of monoclonal antibody therapeutics. Metal complexes are particularly promising for development, given their relative ease of preparation and modular scaffold. Additionally, Aβ has been shown to coordinate endogenous metal ions in solution, while metal complexes can exploit this affinity, thereby modulating the aggregation of the peptide. Herein, a series of five ruthenium(ii)-arene complexes with 1,10-phenanthroline (phen) ligands were prepared and studied for their respective abilities to impact the aggregation of Aβ. Overall, the complex with the 4,7-diamino-1,10-phenanthroline ligand (RuPA) had the greatest impact on Aβ aggregation. Furthermore, this complex also displayed interactions with imidazole in aqueous media, which suggests that coordinate interactions with the peptide occur

Identifiers

PMID41641241
PMCPMC12865786

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.