Evidence map›Paper›PMID 29239603›Full record

ArticleACS chemical neuroscience2018

Thermodynamics of Amyloid-β Fibril Elongation: Atomistic Details of the Transition State.

Roberto A Rodriguez, Liao Y Chen, Germán Plascencia-Villa, George Perry

Abstract read
In one paragraph

Article in ACS chemical neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
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  12. Review
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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

4 authors.

Roberto A RodriguezDepartment of Physics and Astronomy , University of Texas at San Antonio , San Antonio , Texas 78249 , United States.ORCID 0000-0002-3303-9564
Liao Y ChenDepartment of Physics and Astronomy , University of Texas at San Antonio , San Antonio , Texas 78249 , United States.
Germán Plascencia-VillaDepartment of Physics and Astronomy , University of Texas at San Antonio , San Antonio , Texas 78249 , United States.
George PerryDepartment of Biology and Neurosciences Institute , University of Texas at San Antonio , San Antonio , Texas 78249 , United States.

Funding

Quantitatively predictive biology of aquaporins 1, 5, and GlpFSC1GM121275 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI CHEN, LIAO Y · 2017 to 2020
$1.4M
NIGMS NIH HHS SC1 GM121275
6 · The paper itself

Abstract

Amyloid-β (Aβ) fibrils and plaques are one of the hallmarks of Alzheimer's disease. While the kinetics of fibrillar growth of Aβ have been extensively studied, several vital questions remain. In particular, the atomistic origins of the Arrhenius barrier observed in experiments have not been elucidated. Employing the familiar thermodynamic integration method, we have directly simulated the dissociation of an Aβ

Indexed as

ThermodynamicsAlzheimer DiseaseAmyloidAmyloid beta-PeptidesHumansKineticsMolecular Dynamics SimulationPeptide FragmentsAmyloidAmyloid beta-PeptidesPeptide FragmentsAmyloid-betafibril elongationhydrophobic contactsmolecular dynamicsprotein interactionstransition state

Identifiers

PMID29239603
PMCPMC5911799

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.