Evidence map›Paper›PMID 27413767›Full record

ArticleNeurophotonics2016

Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease.

Clemens F Kaminski, Gabriele S Kaminski Schierle

Abstract read
In one paragraph

Article in Neurophotonics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Nanoscale regulation of CaNature communications · 2022
    Article
  6. Review
  7. Article
  8. Review
  9. Super-Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

2 authors.

Clemens F KaminskiUniversity of Cambridge , Department of Chemical Engineering and Biotechnology, Pembroke Street, Cambridge CB2 3RA, United Kingdom.
Gabriele S Kaminski SchierleUniversity of Cambridge , Department of Chemical Engineering and Biotechnology, Pembroke Street, Cambridge CB2 3RA, United Kingdom.

Funding

Medical Research Council MR/N012453/1Wellcome Trust
6 · The paper itself

Abstract

The misfolding and self-assembly of intrinsically disordered proteins into insoluble amyloid structures are central to many neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Optical imaging of this self-assembly process in vitro and in cells is revolutionizing our understanding of the molecular mechanisms behind these devastating conditions. In contrast to conventional biophysical methods, optical imaging and, in particular, optical superresolution imaging, permits the dynamic investigation of the molecular self-assembly process in vitro and in cells, at molecular-level resolution. In this article, current state-of-the-art imaging methods are reviewed and discussed in the context of research into neurodegeneration.

Indexed as

Alzheimer’s diseaseprotein aggregationprotein misfoldingsuperresolution microscopy

Identifiers

PMID27413767
PMCPMC4925874

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.