Evidence map›Paper›PMID 30051958›Full record

ArticleChembiochem : a European journal of chemical biology2018

Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.

Daniel R Whiten, Yukun Zuo, Laura Calo, Minee-Liane Choi, Suman De, Patrick Flagmeier, David C Wirthensohn, Franziska Kundel, Rohan T Ranasinghe, Santiago E Sanchez and 7 more

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

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  11. Live-cell super-resolution imaging of actin using LifeAct-14 with a PAINT-based approach.Protein science : a publication of the Protein Society · 2023
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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

17 authors.

Daniel R WhitenDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Yukun ZuoDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Laura CaloDepartment of Clinical Neurosciences, University of Cambridge, Hills Road, Cambridge, CB2 0AH, UK.
Minee-Liane ChoiUCL Institute of Neurology, Queen Square, London, WC1N 3BG, 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.
David C WirthensohnDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Franziska KundelDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Rohan T RanasingheDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Santiago E SanchezDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Dilan AthaudaUCL Institute of Neurology, Queen Square, London, WC1N 3BG, UK.
Steven F LeeDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Sonia GandhiUCL Institute of Neurology, Queen Square, London, WC1N 3BG, UK.
Maria-Grazia SpillantiniDepartment of Clinical Neurosciences, University of Cambridge, Hills Road, Cambridge, CB2 0AH, UK.
David KlenermanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Mathew H HorrocksDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0001-5495-5492

Funding

Biotechnology and Biological Sciences Research CouncilEuropean Research Council 669237Medical Research Council MR/K015850/1
6 · The paper itself

Abstract

The aberrant misfolding and subsequent conversion of monomeric protein into amyloid aggregates characterises many neurodegenerative disorders, including Parkinson's and Alzheimer's diseases. These aggregates are highly heterogeneous in structure, generally of low abundance and typically smaller than the diffraction limit of light (≈250 nm). To overcome the challenges these characteristics pose to the study of endogenous aggregates formed in cells, we have developed a method to characterise them at the nanometre scale without the need for a conjugated fluorophore. Using a combination of DNA PAINT and an amyloid-specific aptamer, we demonstrate that this technique is able to detect and super-resolve a range of aggregated species, including those formed by α-synuclein and amyloid-β. Additionally, this method enables endogenous protein aggregates within cells to be characterised. We found that neuronal cells derived from patients with Parkinson's disease contain a larger number of protein aggregates than those from healthy controls.

Indexed as

Protein Aggregatesalpha-SynucleinAlzheimer DiseaseAmyloid beta-PeptidesAptamers, PeptideHumansNeuronsParkinson DiseaseProtein Aggregation, Pathologicalalpha-SynucleinAmyloid beta-PeptidesAptamers, PeptideProtein Aggregatesalpha-synucleinamyloid formationaptamersDNA PAINTinduced pluripotent stem cellsneurodegenerative disorders

Identifiers

PMID30051958
PMCPMC6220870

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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.