Evidence map›Paper›PMID 28550528›Full record

ArticleMolecular neurobiology2018

Prion-Like Seeding of Misfolded α-Synuclein in the Brains of Dementia with Lewy Body Patients in RT-QUIC.

Kazunori Sano, Ryuichiro Atarashi, Katsuya Satoh, Daisuke Ishibashi, Takehiro Nakagaki, Yasushi Iwasaki, Mari Yoshida, Shigeo Murayama, Kenichi Mishima, Noriyuki Nishida

Open access · hybridAbstract read
In one paragraph

Article in Molecular neurobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
4.9field-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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Research models to study lewy body dementia.Molecular neurodegeneration · 2025
    Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. From Synaptic Physiology to Synaptic Pathology: The Enigma of α-Synuclein.International journal of molecular sciences · 2024
    Review
  17. Article
  18. Review
  19. Article
  20. 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

10 authors at 5 institutions in 1 country.

Kazunori SanoDepartment of Physiology and Pharmacology, Faculty of Pharmaceutical Sciences, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka, 814-0180, Japan. ksano@fukuoka-u.ac.jp.ORCID http://orcid.org/0000-0002-5198-5642
Ryuichiro AtarashiDivision of Microbiology, Department of Infectious Diseases, Faculty of Medicine, University of Miyazaki, Miyazaki, 889-1692, Japan.
Katsuya SatohDepartment of Locomotive Rehabilitation Science, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, 852-8523, Japan.
Daisuke IshibashiDepartment of Molecular Microbiology and Immunology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, 852-8523, Japan.
Takehiro NakagakiDepartment of Molecular Microbiology and Immunology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, 852-8523, Japan.
Yasushi IwasakiDepartment of Neuropathology, Institute for Medical Science of Aging, Aichi Medical University, Aichi, 480-1195, Japan.
Mari YoshidaDepartment of Neuropathology, Institute for Medical Science of Aging, Aichi Medical University, Aichi, 480-1195, Japan.
Shigeo MurayamaDepartment of Neuropathology, Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology, Tokyo, 173-0015, Japan.
Kenichi MishimaDepartment of Physiology and Pharmacology, Faculty of Pharmaceutical Sciences, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka, 814-0180, Japan.
Noriyuki NishidaDepartment of Molecular Microbiology and Immunology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, 852-8523, Japan.
Nagasaki University · JPAichi Medical University · JPFukuoka University · JPTokyo Metropolitan Geriatric Hospital · JPUniversity of Miyazaki · JP

Funding

ministry of education culture sports science and technology of japan 25640029
6 · The paper itself

Abstract

The prion-like seeding of misfolded α-synuclein (αSyn) involved in the pathogenesis of Lewy body diseases (LBD) remains poorly understood at the molecular level. Using the real-time quaking-induced conversion (RT-QUIC) seeding assay, we investigated whether brain tissues from cases of dementia with Lewy bodies (DLB), which contain serine 129 (Ser129)-phosphorylated insoluble aggregates of αSyn, can convert Escherichia coli-derived recombinant αSyn (r-αSyn) to fibrils. Diffuse neocortical DLB yielded 50% seeding dose (SD

Indexed as

Protein Foldingalpha-SynucleinBiological AssayBrainDementiaHumansLewy Body DiseasePhosphorylationPhosphoserinePrionsProtein AggregatesRecombinant ProteinsSolubilityalpha-SynucleinPhosphoserinePrionsProtein AggregatesRecombinant ProteinsDementia with Lewy bodies (DLB)PrionReal-time quaking-induced conversion (RT-QUIC)α-synuclein

Identifiers

PMID28550528
PMCPMC5884914
OpenAlexW2618281342

What OpenQuestion holds

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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.