Evidence map›Paper›PMID 23442919›Full record

ArticleBiophysical journal2013

Computational assembly of polymorphic amyloid fibrils reveals stable aggregates.

Mohamed Raef Smaoui, Frédéric Poitevin, Marc Delarue, Patrice Koehl, Henri Orland, Jérôme Waldispühl

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
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  7. Diabetes Drug Discovery: hIAPPMolecules (Basel, Switzerland) · 2018
    Article
  8. Review
  9. Article
  10. Molecular docking as a popular tool in drug design, an in silico travel.Advances and applications in bioinformatics and chemistry : AABC · 2016
    Review
  11. Article
  12. On the lack of polymorphism in Aβ-peptide aggregates derived from patient brains.Protein science : a publication of the Protein Society · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. 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

6 authors at 5 institutions in 3 countries.

Mohamed Raef SmaouiSchool of Computer Science, McGill University, Montreal, Canada.
Frédéric Poitevin
Marc Delarue
Patrice Koehl
Henri Orland
Jérôme Waldispühl
McGill University · CACentre National de la Recherche Scientifique · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInstitut Pasteur · FRUniversity of California, Davis · US

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Amyloid proteins aggregate into polymorphic fibrils that damage tissues of the brain, nerves, and heart. Experimental and computational studies have examined the structural basis and the nucleation of short fibrils, but the ability to predict and precisely quantify the stability of larger aggregates has remained elusive. We established a complete classification of fibril shapes and developed a tool called CreateFibril to build such complex, polymorphic, modular structures automatically. We applied stability landscapes, a technique we developed to reveal reliable fibril structural parameters, to assess fibril stability. CreateFibril constructed HET-s, Aβ, and amylin fibrils up to 17 nm in length, and utilized a novel dipolar solvent model that captured the effect of dipole-dipole interactions between water and very large molecular systems to assess their aqueous stability. Our results validate experimental data for HET-s and Aβ, and suggest novel (to our knowledge) findings for amylin. In particular, we predicted the correct structural parameters (rotation angles, packing distances, hydrogen bond lengths, and helical pitches) for the one and three predominant HET-s protofilaments. We reveal and structurally characterize all known Aβ polymorphic fibrils, including structures recently classified as wrapped fibrils. Finally, we elucidate the predominant amylin fibrils and assert that native amylin is more stable than its amyloid form. CreateFibril and a database of all stable polymorphic fibril models we tested, along with their structural energy landscapes, are available at http://amyloid.cs.mcgill.ca.

Indexed as

Protein MultimerizationSoftwareAmino Acid SequenceAmyloidAnimalsHumansIslet Amyloid PolypeptideMolecular Sequence DataProtein ConformationProtein StabilityProtein SubunitsWaterAmyloidIslet Amyloid PolypeptideProtein SubunitsWater

Identifiers

PMID23442919
PMCPMC3566450
OpenAlexW2050891813

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.