Evidence map›Paper›PMID 34122915›Full record

ArticleChemical science2020

ThX - a next-generation probe for the early detection of amyloid aggregates.

Lisa-Maria Needham, Judith Weber, Juan A Varela, James W B Fyfe, Dung T Do, Catherine K Xu, Luke Tutton, Rachel Cliffe, Benjamin Keenlyside, David Klenerman and 7 more

Abstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. BFACS applied bio materials · 2023
    Article
  20. Article
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.

Lisa-Maria NeedhamDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.ORCID https://orcid.org/0000-0002-8139-5862
Judith WeberDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
Juan A VarelaBiomedical Sciences Research Complex, School of Biology, University of St Andrews St Andrews UK.
James W B FyfeDepartment of Chemistry, Indiana University Bloomington 47405 USA tsnaddon@indiana.edu.
Dung T DoDepartment of Chemistry, Indiana University Bloomington 47405 USA tsnaddon@indiana.edu.
Catherine K XuDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
Luke TuttonDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
Rachel CliffeDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
Benjamin KeenlysideDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
David KlenermanDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
Christopher M DobsonDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
Christopher A HunterDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.
Karin H MüllerCambridge Advanced Imaging Centre, University of Cambridge Cambridge CB2 3DY UK.
Kevin O'HolleranCambridge Advanced Imaging Centre, University of Cambridge Cambridge CB2 3DY UK.ORCID https://orcid.org/0000-0003-1039-2127
Sarah E BohndiekDepartment of Physics, University of Cambridge Cambridge CB3 0HE UK.ORCID https://orcid.org/0000-0003-0371-8635
Thomas N SnaddonDepartment of Chemistry, Indiana University Bloomington 47405 USA tsnaddon@indiana.edu.ORCID https://orcid.org/0000-0003-1119-0332
Steven F LeeDepartment of Chemistry, University of Cambridge Cambridge CB2 1EW UK sl591@cam.ac.uk.ORCID https://orcid.org/0000-0003-4492-5139

Funding

Cancer Research UK 16267
6 · The paper itself

Abstract

Neurodegenerative diseases such as Alzheimer's and Parkinson's are associated with protein misfolding and aggregation. Recent studies suggest that the small, rare and heterogeneous oligomeric species, formed early on in the aggregation process, may be a source of cytotoxicity. Thioflavin T (ThT) is currently the gold-standard fluorescent probe for the study of amyloid proteins and aggregation processes. However, the poor photophysical and binding properties of ThT impairs the study of oligomers. To overcome this challenge, we have designed Thioflavin X, (ThX), a next-generation fluorescent probe which displays superior properties; including a 5-fold increase in brightness and 7-fold increase in binding affinity to amyloidogenic proteins. As an extrinsic dye, this can be used to study unique structural amyloid features both in bulk and on a single-aggregate level. Furthermore, ThX can be used as a super-resolution imaging probe in single-molecule localisation microscopy. Finally, the improved optical properties (extinction coefficient, quantum yield and brightness) of ThX can be used to monitor structural differences in oligomeric species, not observed

Identifiers

PMID34122915
PMCPMC8159457

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.