Evidence map›Paper›PMID 23594172›Full record

ArticleACS chemical neuroscience2013

Superresolution imaging of amyloid fibrils with binding-activated probes.

Jonas Ries, Vinod Udayar, Alice Soragni, Simone Hornemann, K Peter R Nilsson, Roland Riek, Christoph Hock, Helge Ewers, Adriano A Aguzzi, Lawrence Rajendran

Abstract read
In one paragraph

Article in ACS chemical neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
–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

35 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021
    Review
  19. 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

10 authors.

Jonas RiesCell Biology and Biophysics, EMBL Heidelberg, Meyerhofstrasse 1, Heidelberg, Germany. jonas.ries@embl.de.
Vinod Udayar
Alice Soragni
Simone Hornemann
K Peter R Nilsson
Roland Riek
Christoph Hock
Helge Ewers
Adriano A Aguzzi
Lawrence Rajendran

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein misfolding into amyloid-like aggregates underlies many neurodegenerative diseases. Thus, insights into the structure and function of these amyloids will provide valuable information on the pathological mechanisms involved and aid in the design of improved drugs for treating amyloid-based disorders. However, determining the structure of endogenous amyloids at high resolution has been difficult. Here we employ binding-activated localization microscopy (BALM) to acquire superresolution images of α-synuclein amyloid fibrils with unprecedented optical resolution. We propose that BALM imaging can be extended to study the structure of other amyloids, for differential diagnosis of amyloid-related diseases and for discovery of drugs that perturb amyloid structure for therapy.

Indexed as

Acetatesalpha-SynucleinAmyloidHumansMicroscopyThiophenesAcetatesalpha-SynucleinAmyloidpentamer formyl thiophene acetic acidThiophenes

Identifiers

PMID23594172
PMCPMC3715833

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.