Evidence map›Paper›PMID 28272542›Full record

ArticleScientific reports2017

Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives.

V Castelletto, P Ryumin, R Cramer, I W Hamley, M Taylor, D Allsop, M Reza, J Ruokolainen, T Arnold, D Hermida-Merino and 3 more

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Self-Assembly of Peptides and Biomolecular Systems Into Functional Nanomaterials.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Review
  2. Article
  3. Chemistry of materials : a publication of the American Chemical Society · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Self-Assembly of Block Heterochiral Peptides into Helical Tapes.Journal of the American Chemical Society · 2020
    Article
  15. Article
  16. Article
  17. Review
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

13 authors.

V CastellettoSchool of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading RG6 6AD, UK.
P RyuminSchool of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading RG6 6AD, UK.
R CramerSchool of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading RG6 6AD, UK.
I W HamleySchool of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading RG6 6AD, UK.
M TaylorDivision of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK.
D AllsopDivision of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK.
M RezaDepartment of Applied Physics, Aalto University School of Science, Aalto FI-00076, Finland.
J RuokolainenDepartment of Applied Physics, Aalto University School of Science, Aalto FI-00076, Finland.
T ArnoldDiamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.
D Hermida-MerinoEuropean Synchrotron Radiation Facility, ESRF, 71 avenue des Martyrs, 38000 Grenoble, France.
C I GarciaFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina.
M C LealFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina.
E CastañoFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH

Indexed as

Protein AggregatesAmino Acid SequenceAmyloid beta-PeptidesAmyloidosisAnimalsCell SurvivalMolecular StructureNeuronsPeptide FragmentsProtein Aggregation, PathologicalProtein Structure, SecondaryRatsSpectrometry, Mass, Electrospray IonizationSpectroscopy, Fourier Transform InfraredX-Ray DiffractionAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (16-20)Peptide FragmentsProtein Aggregates

Identifiers

PMID28272542
PMCPMC5341572

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.