Evidence map›Paper›PMID 27443509›Full record

ArticleScientific reports2016

A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration.

Karen E Marshall, Devkee M Vadukul, Liza Dahal, Alina Theisen, Milena W Fowler, Youssra Al-Hilaly, Lenzie Ford, György Kemenes, Iain J Day, Kevin Staras and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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
2.7field-weighted citation impact, top 10% 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, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Adverse Effects of AβBiomolecules · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Nucleation and Growth of Amyloid Fibrils.The journal of physical chemistry. B · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. On the Dependence of Prion and Amyloid Structure on the Folding Environment.International journal of molecular sciences · 2021
    Article
  17. Article
  18. 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

11 authors at 2 institutions in 2 countries.

Karen E MarshallSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Devkee M VadukulSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Liza DahalSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Alina TheisenSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Milena W FowlerSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Youssra Al-HilalySchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Lenzie FordSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
György KemenesSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Iain J DaySchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Kevin StarasSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
Louise C SerpellSchool of Life Sciences, University of Sussex, Falmer, BN1 9QG, UK.
University of Sussex · GBMustansiriyah University · IQ

Funding

Biotechnology and Biological Sciences Research Council BB/E009042/1Medical Research Council MR/K022105/1
6 · The paper itself

Abstract

Amyloid β1-42 (Aβ1-42) plays a central role in Alzheimer's disease. The link between structure, assembly and neuronal toxicity of this peptide is of major current interest but still poorly defined. Here, we explored this relationship by rationally designing a variant form of Aβ1-42 (vAβ1-42) differing in only two amino acids. Unlike Aβ1-42, we found that the variant does not self-assemble, nor is it toxic to neuronal cells. Moreover, while Aβ1-42 oligomers impact on synaptic function, vAβ1-42 does not. In a living animal model system we demonstrate that only Aβ1-42 leads to memory deficits. Our findings underline a key role for peptide sequence in the ability to assemble and form toxic structures. Furthermore, our non-toxic variant satisfies an unmet demand for a closely related control peptide for Aβ1-42 cellular studies of disease pathology, offering a new opportunity to decipher the mechanisms that accompany Aβ1-42-induced toxicity leading to neurodegeneration.

Indexed as

Alzheimer DiseaseAmino Acid SequenceAmyloid beta-PeptidesAmyloidogenic ProteinsAmyloidosisAnimalsCell LineDisease Models, AnimalHumansMemory DisordersNeurodegenerative DiseasesNeuronsPeptide FragmentsRatsAmyloid beta-PeptidesAmyloidogenic ProteinsPeptide Fragments

Identifiers

PMID27443509
PMCPMC4957119
OpenAlexW2486642379

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.