Evidence map›Paper›PMID 30979935›Full record

ArticleScientific reports2019

Ultrasonication-based rapid amplification of α-synuclein aggregates in cerebrospinal fluid.

Keita Kakuda, Kensuke Ikenaka, Katsuya Araki, Masatomo So, César Aguirre, Yuta Kajiyama, Kuni Konaka, Kentaro Noi, Kousuke Baba, Hiroshi Tsuda and 8 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.6field-weighted citation impact, top 7% of its field
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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
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  7. Lysophagy protects against propagation of α-synuclein aggregation through ruptured lysosomal vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  16. Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022
    Review
  17. Article
  18. Article
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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

18 authors at 3 institutions in 2 countries.

Keita KakudaDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Kensuke IkenakaDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Katsuya ArakiDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Masatomo SoInstitute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka, 565-0871, Japan.
César AguirreInstitute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka, 565-0871, Japan.
Yuta KajiyamaDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Kuni KonakaDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Kentaro NoiDepartment of Precision Science and Technology, Graduate School of Engineering, Osaka University, Yamadaoka 2-1, Suita, Osaka, 565-0871, Japan.
Kousuke BabaDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Hiroshi TsudaDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Seiichi NaganoDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Takuma OhmichiDepartment of Neurology, Kyoto Prefectural University of Medicine, 465 Kajii-cho, Kamikyo-ku, Kyoto, 602-8566, Japan.
Yoshitaka NagaiDepartment of Neurotherapeutics, Graduate school of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan.
Takahiko TokudaDepartment of Molecular Pathobiology of Brain Diseases, Kyoto Prefectural University of Medicine, 465 Kajii-cho, Kamikyo-ku, Kyoto, 602-8566, Japan.
Omar M A El-AgnafLife Sciences Division, College of Science and Engineering, Hamad Bin Khalifa University (HBKU), Education City, Qatar.
Hirotsugu OgiDepartment of Precision Science and Technology, Graduate School of Engineering, Osaka University, Yamadaoka 2-1, Suita, Osaka, 565-0871, Japan.
Yuji GotoInstitute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka, 565-0871, Japan.
Hideki MochizukiDepartment of Neurology, Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka, 565-0871, Japan. hmochizuki@neurol.med.osaka-u.ac.jp.ORCID http://orcid.org/0000-0002-0874-7542
The University of Osaka · JPKyoto Prefectural University of Medicine · JPHamad bin Khalifa University · QA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein aggregates, a key hallmark of the pathogenesis of Parkinson's disease, can be amplified by using their seeding activity, and the evaluation of the seeding activity of cerebrospinal fluid (CSF) is reportedly useful for diagnosis. However, conventional shaking-based assays are time-consuming procedures, and the clinical significance of the diversity of seeding activity among patients remains to be clarified. Previously, we reported a high-throughput ultrasonication-induced amyloid fibrillation assay. Here, we adapted this assay to amplify and detect α-synuclein aggregates from CSF, and investigated the correlation between seeding activity and clinical indicators. We confirmed that this assay could detect α-synuclein aggregates prepared in vitro and also aggregates released from cultured cells. The seeding activity of CSF correlated with the levels of α-synuclein oligomers measured by an enzyme-linked immunosorbent assay. Moreover, the seeding activity of CSF from patients with Parkinson's disease was higher than that of control patients. Notably, the lag time of patients with Parkinson's disease was significantly correlated with the MIBG heart-to-mediastinum ratio. These findings showed that our ultrasonication-based assay can rapidly amplify misfolded α-synuclein and can evaluate the seeding activity of CSF.

Indexed as

Protein AggregatesSonicationalpha-SynucleinCell Line, TumorHumansalpha-SynucleinProtein Aggregates

Identifiers

PMID30979935
PMCPMC6461702
OpenAlexW2939921565

What OpenQuestion holds

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Registered trials

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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.