Evidence map›Paper›PMID 33123310›Full record

ReviewOxidative medicine and cellular longevity2020

The Antiaggregative and Antiamyloidogenic Properties of Nanoparticles: A Promising Tool for the Treatment and Diagnostics of Neurodegenerative Diseases.

Monika Pichla, Grzegorz Bartosz, Izabela Sadowska-Bartosz

Abstract readReview
In one paragraph

Review in Oxidative medicine and cellular longevity, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
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  7. Article
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  9. Review
  10. Molecular mechanisms of amyloid disaggregation.Journal of advanced research · 2022
    Review
  11. Review
  12. Inhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles.Chemistry of materials : a publication of the American Chemical Society · 2021
    Article
  13. Article
  14. Article
  15. Emerging Nanotechnology for Treatment of Alzheimer's and Parkinson's Disease.Frontiers in bioengineering and biotechnology · 2021
    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

3 authors.

Monika PichlaDepartment of Analytical Biochemistry, Institute of Food Technology and Nutrition, College of Natural Sciences, Rzeszow University, Zelwerowicza Street 4, 35-601 Rzeszów, Poland.
Grzegorz BartoszDepartment of Bioenergetics, Food Analysis and Microbiology, College of Natural Sciences, Rzeszow University, Zelwerowicza Street 4, 35-601 Rzeszów, Poland.ORCID https://orcid.org/0000-0002-0347-0740
Izabela Sadowska-BartoszDepartment of Analytical Biochemistry, Institute of Food Technology and Nutrition, College of Natural Sciences, Rzeszow University, Zelwerowicza Street 4, 35-601 Rzeszów, Poland.ORCID https://orcid.org/0000-0001-9035-6833

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Due to the progressive aging of the society, the prevalence and socioeconomic burden of neurodegenerative diseases are predicted to rise. The most common neurodegenerative disorders nowadays, such as Parkinson's disease, Alzheimer's disease, and amyotrophic lateral sclerosis, can be classified as proteinopathies. They can be either synucleinopathies, amyloidopathies, tauopathies, or TDP-43-related proteinopathies; thus, nanoparticles with a potential ability to inhibit pathological protein aggregation and/or degrade already existing aggregates can be a promising approach in the treatment of neurodegenerative diseases. As it turns out, nanoparticles can be a double-edged sword; they can either promote or inhibit protein aggregation, depending on coating, shape, size, surface charge, and concentration. In this review, we aim to emphasize the need of a breakthrough in the treatment of neurodegenerative disorders and draw attention to nanomaterials, as they can also serve as a diagnostic tool for protein aggregates or can be used in a high-throughput screening for novel antiaggregative compounds.

Indexed as

alpha-SynucleinAmyloidogenic ProteinsAntioxidantsDendrimersHumansNanoparticlesNeurodegenerative DiseasesProtein AggregatesQuantum DotsReactive Oxygen Speciesalpha-SynucleinAmyloidogenic ProteinsAntioxidantsDendrimersProtein AggregatesReactive Oxygen Species

Identifiers

PMID33123310
PMCPMC7582079

What OpenQuestion holds

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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.