Evidence map›Paper›PMID 29550287›Full record

ArticleBiochimica et biophysica acta. Biomembranes2018

Structures and dynamics of β-barrel oligomer intermediates of amyloid-beta16-22 aggregation.

Xinwei Ge, Yunxiang Sun, Feng Ding

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  7. Computer Simulations Aimed at Exploring Protein Aggregation and Dissociation.Methods in molecular biology (Clifton, N.J.) · 2022
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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.

Xinwei GeDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, United States.
Yunxiang SunDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, United States.
Feng DingDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, United States. Electronic address: fding@clemson.edu.

Funding

Inhibition of Human Islet Amyloid Polypeptide AggregationR35GM119691 · NIGMS · CLEMSON UNIVERSITY · PI DING, FENG · 2016 to 2020
$1.9M
NIGMS NIH HHS R35 GM119691
6 · The paper itself

Abstract

Accumulating evidence suggests that soluble oligomers are more toxic than final fibrils of amyloid aggregations. Among the mixture of inter-converting intermediates with continuous distribution of sizes and secondary structures, oligomers in the β-barrel conformation - a common class of protein folds with a closed β-sheet - have been postulated as the toxic species with well-defined three-dimensional structures to perform pathological functions. A common mechanism for amyloid toxicity, therefore, implies that all amyloid peptides should be able to form β-barrel oligomers as the aggregation intermediates. Here, we applied all-atom discrete molecular dynamics (DMD) simulations to evaluate the formation of β-barrel oligomers and characterize their structures and dynamics in the aggregation of a seven-residue amyloid peptide, corresponding to the amyloid core of amyloid-β with a sequence of

Indexed as

Aggregation oligomerAmyloid aggregationAmyloid-betaMolecular dynamicsβ-barrel

Identifiers

PMID29550287
PMCPMC6145138

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.