Evidence map›Paper›PMID 27513605›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Gold-Induced Fibril Growth: The Mechanism of Surface-Facilitated Amyloid Aggregation.

Anika Gladytz, Bernd Abel, Herre Jelger Risselada

Open access · bronzeAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Noble Metal Nanoparticles with Nanogel Coatings: Coinage Metal Thiolate-Stabilized Glutathione Hydrogel Shells.The journal of physical chemistry. C, Nanomaterials and interfaces · 2024
    Article
  3. Article
  4. Article
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  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Inhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles.Chemistry of materials : a publication of the American Chemical Society · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition.Small (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  19. Mitigation of Amyloidosis with Nanomaterials.Advanced materials (Deerfield Beach, Fla.) · 2020
    Review
  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

3 authors at 3 institutions in 1 country.

Anika GladytzChemistry Department, Leibniz Institute of Surface Modification (IOM) Leipzig e.V., Permoserstrasse 15, 04318, Leipzig, Germany.
Bernd AbelChemistry Department, Leibniz Institute of Surface Modification (IOM) Leipzig e.V., Permoserstrasse 15, 04318, Leipzig, Germany. bernd.abel@iom-leipzig.de.
Herre Jelger RisseladaChemistry Department, Leibniz Institute of Surface Modification (IOM) Leipzig e.V., Permoserstrasse 15, 04318, Leipzig, Germany. hrissel@gwdg.de.
Leibniz Institute of Surface Engineering · DELeipzig University · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The question of how amyloid fibril formation is influenced by surfaces is crucial for a detailed understanding of the process in vivo. We applied a combination of kinetic experiments and molecular dynamics simulations to elucidate how (model) surfaces influence fibril formation of the amyloid-forming sequences of prion protein SUP35 and human islet amyloid polypeptide. The kinetic data suggest that structural reorganization of the initial peptide corona around colloidal gold nanoparticles is the rate-limiting step. The molecular dynamics simulations reveal that partial physisorption to the surface results in the formation of aligned monolayers, which stimulate the formation of parallel, critical oligomers. The general mechanism implies that the competition between the underlying peptide-peptide and peptide-surface interactions must strike a balance to accelerate fibril formation.

Indexed as

GoldHumansIslet Amyloid PolypeptideKineticsMetal NanoparticlesMolecular Dynamics SimulationPrion ProteinsProtein AggregatesSurface PropertiesGoldIslet Amyloid PolypeptidePrion ProteinsProtein Aggregatescitrate-covered gold nanoparticleshIAPPmolecular dynamics simulationsRamachandran plotsSUP35

Identifiers

PMID27513605
PMCPMC5113782
OpenAlexW2509997327

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.