Evidence map›Paper›PMID 29924993›Full record

ArticleCell reports2018

Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers.

Daniel R Whiten, Dezerae Cox, Mathew H Horrocks, Christopher G Taylor, Suman De, Patrick Flagmeier, Laura Tosatto, Janet R Kumita, Heath Ecroyd, Christopher M Dobson and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.6field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 76 citations in OpenAlex.

  1. Intracellular Signaling Regulated by Activated αInternational journal of molecular sciences · 2026
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  7. Clusterin: structure, function and roles in disease.International journal of medical sciences · 2025
    Review
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  11. Article
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  14. Sequestration of TDP-43ACS chemical neuroscience · 2022
    Article
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  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

12 authors at 3 institutions in 2 countries.

Daniel R WhitenDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK; Illawarra Health and Medical Research Institute, School of Biological Sciences, University of Wollongong, Wollongong 2522, NSW, Australia.
Dezerae CoxIllawarra Health and Medical Research Institute, School of Biological Sciences, University of Wollongong, Wollongong 2522, NSW, Australia.
Mathew H HorrocksDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK; Illawarra Health and Medical Research Institute, School of Biological Sciences, University of Wollongong, Wollongong 2522, NSW, Australia.
Christopher G TaylorDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Suman DeDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Patrick FlagmeierDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Laura TosattoDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Janet R KumitaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Heath EcroydIllawarra Health and Medical Research Institute, School of Biological Sciences, University of Wollongong, Wollongong 2522, NSW, Australia.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
David KlenermanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK; UK Dementia Research Institute, University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: dk10012@cam.ac.uk.
Mark R WilsonIllawarra Health and Medical Research Institute, School of Biological Sciences, University of Wollongong, Wollongong 2522, NSW, Australia. Electronic address: mrw@uow.edu.au.
University of Cambridge · GBUniversity of Wollongong · AUIllawarra Health and Medical Research Institute · AU

Funding

European Research Council 669237Wellcome Trust
6 · The paper itself

Abstract

The aberrant aggregation of α-synuclein is associated with several human diseases, collectively termed the α-synucleinopathies, which includes Parkinson's disease. The progression of these diseases is, in part, mediated by extracellular α-synuclein oligomers that may exert effects through several mechanisms, including prion-like transfer, direct cytotoxicity, and pro-inflammatory actions. In this study, we show that two abundant extracellular chaperones, clusterin and α

Indexed as

Protein Multimerizationalpha-SynucleinExtracellular SpaceHydrophobic and Hydrophilic InteractionsMolecular ChaperonesProtein Bindingalpha-SynucleinMolecular ChaperonesclusterinneurodegenerationoligomerParkinson’s diseaseα2-macroglobulinα-synuclein

Identifiers

PMID29924993
PMCPMC6024880
OpenAlexW2808814503

What OpenQuestion holds

Textmetadata
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.