Evidence map›Paper›PMID 31660732›Full record

ArticleACS chemical neuroscience2019

Molecular Mechanism and Kinetics of Amyloid-β

Viet Hoang Man, Xibing He, Beihong Ji, Shuhan Liu, Xiang-Qun Xie, Junmei Wang

Abstract read
In one paragraph

Article in ACS chemical neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Phosphorylation at Ser289 Enhances the Oligomerization of Tau Repeat R2.Journal of chemical information and modeling · 2023
    Article
  10. Stable Cavitation Interferes with AβJournal of chemical information and modeling · 2022
    Article
  11. Review
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

6 authors.

Viet Hoang ManDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy , University of Pittsburgh , Pittsburgh , Pennsylvania 15261 , United States.ORCID 0000-0002-8907-6479
Xibing HeDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy , University of Pittsburgh , Pittsburgh , Pennsylvania 15261 , United States.
Beihong JiDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy , University of Pittsburgh , Pittsburgh , Pennsylvania 15261 , United States.
Shuhan LiuDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy , University of Pittsburgh , Pittsburgh , Pennsylvania 15261 , United States.
Xiang-Qun XieDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy , University of Pittsburgh , Pittsburgh , Pennsylvania 15261 , United States.ORCID 0000-0002-6881-6175
Junmei WangDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy , University of Pittsburgh , Pittsburgh , Pennsylvania 15261 , United States.ORCID 0000-0002-9607-8229

Funding

NIDA Center of Excellence OF Computational Drug Abuse Research (CDAR)P30DA035778 · NIDA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BAHAR, IVET, XIE, XIANG-QUN · 2014 to 2018
$5.4M
AMBER force field consortium: a coherent biomolecular simulation platformR01GM079383 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CIEPLAK, PIOTR, DUAN, YONG · 2007 to 2017
$4.7M
Protein Design Using Physical Scoring Functions integrated with Site CouplingsR21GM097617 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI WANG, JUNMEI · 2011 to 2012
$397k
NIDA NIH HHS P30 DA035778NIGMS NIH HHS R01 GM079383NIGMS NIH HHS R21 GM097617
6 · The paper itself

Abstract

As an important neuropathological hallmark of Alzheimer's disease (AD), the oligomerization of amyloid-β (Aβ) peptides has been intensively investigated in both theoretical and experimental studies. However, the oligomerization space in terms of the kinetics, molecular mechanism, and oligomer structures remains mysterious to us. An equation that can quantitatively describe the time it takes for Aβ oligomers to appear in the human brain at a given Aβ monomer concentration is extremely vital for us to understand the development and disease progression of AD. In this study, we utilized molecular dynamics (MD) simulations to investigate the oligomerization of Aβ

Indexed as

Models, MolecularMolecular Dynamics SimulationProtein AggregatesAmyloid beta-PeptidesPeptide FragmentsProtein Structure, SecondaryAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide FragmentsProtein AggregatesAlzheimer’s diseaseamyloid-betaconcentrationequationoligomerizationoligomers

Identifiers

PMID31660732
PMCPMC7336531

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.