ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2016
Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Article
- Engineering of antimicrobial peptide fibrils with feedback degradation of bacterial-secreted enzymes.Chemical science · 2023Article
- Single-molecule visualization determines conformational substate ensembles in β-sheet-rich peptide fibrils.Science advances · 2023Article
- A swarm of slippery micropropellers penetrates the vitreous body of the eye.Science advances · 2018Article
- CDtoolX, a downloadable software package for processing and analyses of circular dichroism spectroscopic data.Protein science : a publication of the Protein Society · 2018Article
- Nano-assembly of amyloid β peptide: role of the hairpin fold.Scientific reports · 2017Article
- Nanoscale studies link amyloid maturity with polyglutamine diseases onset.Scientific reports · 2016Article
- Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity. In this work, the early Aβ
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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.