Evidence map›Paper›PMID 28073262›Full record

ArticleNano letters2017

Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells.

WeiYue Chen, Laurence J Young, Meng Lu, Alessio Zaccone, Florian Ströhl, Na Yu, Gabriele S Kaminski Schierle, Clemens F Kaminski

Open access · hybridAbstract read
In one paragraph

Article in Nano letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
9.6field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
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  5. Discovery of TDP-43 aggregation inhibitorsbioRxiv : the preprint server for biology · 2026
    Article
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  14. Bioorthogonal Reactions in Bioimaging.Topics in current chemistry (Cham) · 2024
    Review
  15. BaGlobal challenges (Hoboken, NJ) · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. 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

8 authors at 1 institution in 1 country.

WeiYue ChenDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.ORCID 0000-0001-5004-4376
Laurence J YoungDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.ORCID 0000-0002-0269-7548
Meng LuDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.
Alessio ZacconeDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.
Florian StröhlDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.
Na YuDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.
Gabriele S Kaminski SchierleDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.
Clemens F KaminskiDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Pembroke Street, Cambridge CB2 3RA, United Kingdom.
University of Cambridge · GB

Funding

Medical Research Council MR/K02292X/1Wellcome Trust 089703/Z/09/ZWellcome Trust 203249/Z/16/Z
6 · The paper itself

Abstract

The characterization of the aggregation kinetics of protein amyloids and the structural properties of the ensuing aggregates are vital in the study of the pathogenesis of many neurodegenerative diseases and the discovery of therapeutic targets. In this article, we show that the fluorescence lifetime of synthetic dyes covalently attached to amyloid proteins informs on the structural properties of amyloid clusters formed both in vitro and in cells. We demonstrate that the mechanism behind such a "lifetime sensor" of protein aggregation is based on fluorescence self-quenching and that it offers a good dynamic range to report on various stages of aggregation without significantly perturbing the process under investigation. We show that the sensor informs on the structural density of amyloid clusters in a high-throughput and quantitative manner and in these aspects the sensor outperforms super-resolution imaging techniques. We demonstrate the power and speed of the method, offering capabilities, for example, in therapeutic screenings that monitor biological self-assembly. We investigate the mechanism and advantages of the lifetime sensor in studies of the K18 protein fragment of the Alzheimer's disease related protein tau and its amyloid aggregates formed in vitro. Finally, we demonstrate the sensor in the study of aggregates of polyglutamine protein, a model used in studies related to Huntington's disease, by performing correlative fluorescence lifetime imaging microscopy and structured-illumination microscopy experiments in cells.

Indexed as

Protein AggregatesAlzheimer DiseaseAmyloidFluorescenceFluorescent DyesHEK293 CellsHumansHuntington DiseaseKineticsOptical ImagingPeptidesProtein ConformationAmyloidFluorescent DyesPeptidespolyglutamineProtein Aggregatesamyloid aggregationFLIMSelf-quenchingSIMsuper-resolution

Identifiers

PMID28073262
PMCPMC5338000
OpenAlexW2558411892

What OpenQuestion holds

Textmetadata
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.