Evidence map›Paper›PMID 31476124›Full record

ArticleJournal of chemical theory and computation2019

Modulation of Amyloid-β42 Conformation by Small Molecules Through Nonspecific Binding.

Chungwen Liang, Sergey N Savinov, Jasna Fejzo, Stephen J Eyles, Jianhan Chen

Abstract read
In one paragraph

Article in Journal of chemical theory and computation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

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  14. Molecular Basis of Small-Molecule Binding to α-Synuclein.Journal of the American Chemical Society · 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

5 authors.

Chungwen LiangComputational Modeling Core Facility, Institute for Applied Life Sciences (IALS) , University of Massachusetts Amherst , Amherst , Massachusetts 01003 , United States.ORCID http://orcid.org/0000-0001-9721-6411
Sergey N SavinovComputational Modeling Core Facility, Institute for Applied Life Sciences (IALS) , University of Massachusetts Amherst , Amherst , Massachusetts 01003 , United States.
Jasna FejzoBiomolecular NMR Core Facility, Institute for Applied Life Sciences (IALS) , University of Massachusetts Amherst , Amherst , Massachusetts 01003 , United States.
Stephen J EylesMass Spectrometry Core Facility, Institute for Applied Life Sciences (IALS) , University of Massachusetts Amherst , Amherst , Massachusetts 01003 , United States.
Jianhan ChenDepartment of Biochemistry and Molecular Biology , University of Massachusetts Amherst , Amherst , Massachusetts 01003 , United States.ORCID http://orcid.org/0000-0002-5281-1150

Funding

Multi-scale enhanced sampling of disordered proteins: Admin Supplement InstrumentationR01GM114300 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHEN, JIANHAN · 2016 to 2020
$1.5M
NIGMS NIH HHS R01 GM114300
6 · The paper itself

Abstract

Aggregation of amyloid-β (Aβ) peptides is a crucial step in the progression of Alzheimer's disease (AD). Identifying aggregation inhibitors against AD has been a great challenge. We report an atomistic simulation study of the inhibition mechanism of two small molecules, homotaurine and

Indexed as

Amyloid beta-PeptidesBinding SitesHumansMolecular Dynamics SimulationProtein AggregatesProtein BindingProtein ConformationSmall Molecule LibrariesAmyloid beta-PeptidesProtein AggregatesSmall Molecule Libraries

Identifiers

PMID31476124
PMCPMC6783347

What OpenQuestion holds

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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.