Evidence map›Paper›PMID 35064139›Full record

ArticleScientific reports2022

Phosphorylation of endogenous α-synuclein induced by extracellular seeds initiates at the pre-synaptic region and spreads to the cell body.

Shiori Awa, Genjiro Suzuki, Masami Masuda-Suzukake, Takashi Nonaka, Minoru Saito, Masato Hasegawa

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. 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
5.0field-weighted citation impact, top 4% 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. Article
  2. PET imaging of alpha-synuclein: from radiotracer design through in vitro and in vivo translation.European journal of nuclear medicine and molecular imaging · 2026
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  11. Posttranslational Modifications ofPharmacological reviews · 2024
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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

6 authors at 3 institutions in 1 country.

Shiori Awa *Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Genjiro Suzuki *Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan. suzuki-gj@igakuken.or.jp.
Masami Masuda-SuzukakeDepartment of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Takashi NonakaDepartment of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Minoru SaitoDepartment of Biosciences, College of Humanities and Sciences, Nihon University, Tokyo, Japan.
Masato HasegawaDepartment of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan. hasegawa-ms@igakuken.or.jp.
Tokyo Metropolitan Institute of Medical Science · JPNihon University · JPUbe Frontier University · JP

Funding

Core Research for Evolutional Science and Technology JPMJCR18H3Japan Agency for Medical Research and Development JP18dm0207019Japan Society for the Promotion of Science 21K07288
6 · The paper itself

Abstract

Accumulation of phosphorylated α-synuclein aggregates has been implicated in several diseases, such as Parkinson's disease (PD) and dementia with Lewy bodies (DLB), and is thought to spread in a prion-like manner. Elucidating the mechanisms of prion-like transmission of α-synuclein is important for the development of therapies for these diseases, but little is known about the details. Here, we injected α-synuclein fibrils into the brains of wild-type mice and examined the early phase of the induction of phosphorylated α-synuclein accumulation. We found that phosphorylated α-synuclein appeared within a few days after the intracerebral injection. It was observed initially in presynaptic regions and subsequently extended its localization to axons and cell bodies. These results suggest that extracellular α-synuclein fibrils are taken up into the presynaptic region and seed-dependently convert the endogenous normal α-synuclein that is abundant there to an abnormal phosphorylated form, which is then transported through the axon to the cell body.

Indexed as

alpha-SynucleinAnimalsAxonsCells, CulturedCerebral CortexDisease Models, AnimalEmbryo, MammalianHippocampusHumansMaleMiceNeurodegenerative DiseasesPhosphorylationPrimary Cell CultureRecombinant ProteinsSynapsesalpha-SynucleinRecombinant ProteinsSnca protein, mouse

Identifiers

PMID35064139
PMCPMC8782830
OpenAlexW4206989713

What OpenQuestion holds

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LicenceCC BY
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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.