Evidence map›Paper›PMID 42125450›Full record

ArticleScience and technology of advanced materials2026

Characterization and evaluation of the ability of graphene quantum dots to affect α-synuclein aggregation in synucleinopathy models.

Tuba Oz, Anna Alwani, Agnieszka Kamińska, Barbara Jachimska, Makoto Timmon Tanaka, Yasuo Miki, Koichi Wakabayashi, Katarzyna Maziarz, Sheetal Kaushik Bhardwaj, Ajeet Kaushik and 3 more

Abstract read
In one paragraph

Article in Science and technology of advanced materials, 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. 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

13 authors.

Tuba OzDepartment of Toxicology, Poznan University of Medical Sciences, Poznań, Poland.ORCID https://orcid.org/0000-0003-4366-8927
Anna AlwaniDepartment of Brain Biochemistry, Maj Institute of Pharmacology, Polish Academy of Sciences, Kraków, Poland.ORCID https://orcid.org/0000-0002-7611-5467
Agnieszka KamińskaJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Kraków, Poland.ORCID https://orcid.org/0000-0003-0278-725X
Barbara JachimskaJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Kraków, Poland.ORCID https://orcid.org/0000-0002-2445-7318
Makoto Timmon TanakaDepartment of Neuropathology, Hirosaki University Graduate School of Medicine, Hirosaki, Japan.ORCID https://orcid.org/0000-0002-5474-0632
Yasuo MikiDepartment of Neuropathology, Hirosaki University Graduate School of Medicine, Hirosaki, Japan.ORCID https://orcid.org/0000-0001-9375-9590
Koichi WakabayashiDepartment of Neuropathology, Hirosaki University Graduate School of Medicine, Hirosaki, Japan.ORCID https://orcid.org/0000-0002-3756-7209
Katarzyna MaziarzDepartment of Brain Biochemistry, Maj Institute of Pharmacology, Polish Academy of Sciences, Kraków, Poland.ORCID https://orcid.org/0000-0001-9116-7954
Sheetal Kaushik BhardwajVan't Hoff Institute for Molecular Sciences, University of Amsterdam, Amsterdam, The Netherlands.ORCID https://orcid.org/0000-0001-9876-7389
Ajeet KaushikDepartment of Environmental Engineering, Florida Polytechnic University, Lakeland, FL, USA.
Małgorzata FigielDepartment of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland.ORCID https://orcid.org/0000-0001-9390-7418
Piotr ChmielarzDepartment of Brain Biochemistry, Maj Institute of Pharmacology, Polish Academy of Sciences, Kraków, Poland.ORCID https://orcid.org/0000-0001-8935-8591
Małgorzata KujawskaDepartment of Toxicology, Poznan University of Medical Sciences, Poznań, Poland.ORCID https://orcid.org/0000-0002-5306-9904

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synucleinopathies, including Parkinson's disease and multiple system atrophy (MSA), are neurodegenerative disorders characterized by aggregation of α-synuclein (ASN). Nanomaterials capable of modulating protein misfolding represent a potential intervention strategy. Here, we synthesized graphene quantum dots (GQDs) and systematically evaluated their physicochemical properties and biological activity against ASN aggregation. The GQDs were characterized using spectroscopic, electron microscopy, and colloidal techniques to determine surface chemistry, charge, optical properties, and crystalline structure. Biological evaluation demonstrated cytocompatibility in human dermal fibroblasts (IC

Indexed as

amyloid inhibitionbioactive nanomaterialscytocompatibilityGraphene quantum dotsNano–bio interactionsnano–bio interfacenanotoxicology

Identifiers

PMID42125450
PMCPMC13159600

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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.