ArticleMolecular simulation2011
Internal and environmental effects on folding and dimerization of the Alzheimer's β amyloid peptide.
Article in Molecular simulation, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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.
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.
Who cites it
3 citing papers in PubMed.
- Side-chain hydrophobicity and the stability of Aβ₁₆₋₂₂ aggregates.Protein science : a publication of the Protein Society · 2012Article
- Structure and dynamics of amyloid-β segmental polymorphisms.PloS one · 2012Article
- Replica exchange molecular dynamics of the thermodynamics of fibril growth of Alzheimer's Aβ42 peptide.The Journal of chemical physics · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Amyloid deposits are a hallmark of many diseases. In the case of Alzheimer's disease a turn between 21Ala and 30Ala, stabilized by a salt bridge between 22Glu/23Asp and 28Lys, may nucleate folding and aggregation of the Aβ peptide. In the present paper we test this hypothesis by studying how salt bridge and turn formation vary with intrinsic and environmental changes, and how these changes effect folding and aggregation of the Aβ peptide.
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What OpenQuestion holds
Registered trials
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.