Evidence map›Paper›PMID 19164927›Full record

ReviewPrion

Computational simulations of the early steps of protein aggregation.

Guanghong Wei, Normand Mousseau, Philippe Derreumaux

Abstract readReview
In one paragraph

Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
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  5. Review
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  10. Review
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  12. The power of coarse graining in biomolecular simulations.Wiley interdisciplinary reviews. Computational molecular science · 2014
    Article
  13. Article
  14. Side-chain hydrophobicity and the stability of Aβ₁₆₋₂₂ aggregates.Protein science : a publication of the Protein Society · 2012
    Article
  15. Review
  16. 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

3 authors.

Guanghong WeiDepartment of Physics, Fudan University, Shanghai, China.
Normand Mousseau
Philippe Derreumaux

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is strong evidence that the oligomers of key proteins, formed during the early steps of aggregation, could be the primary toxic species associated with human neuro-degenerative diseases, such as Alzheimer's and prion diseases. Here, we review recent progress in the development of computational approaches in order to understand the structures, dynamics and free energy surfaces of oligomers. We also discuss possible research directions for the coming years.

Indexed as

Protein FoldingAlzheimer DiseaseAnimalsComputational BiologyHumansPrion DiseasesPrionsProtein Structure, QuaternaryPrions

Identifiers

PMID19164927
PMCPMC2633700

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.