Evidence map›Paper›PMID 30674664›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Thermodynamic phase diagram of amyloid-β (16-22) peptide.

Yiming Wang, Samuel J Bunce, Sheena E Radford, Andrew J Wilson, Stefan Auer, Carol K Hall

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
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

30 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Nonparametric Determination of the Committor in Multimolecular Systems.Journal of chemical theory and computation · 2025
    Article
  5. Physics of Protein Aggregation in Normal and Accelerated Brain Aging.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Mapping the configurational landscape and aggregation phase behavior of the tau protein fragment PHF6.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Nucleation and Growth of Amyloid Fibrils.The journal of physical chemistry. B · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Defining the Neuropathological Aggresome acrossThe journal of physical chemistry. B · 2021
    Review
  19. Article
  20. 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 at 2 institutions in 2 countries.

Yiming WangDepartment of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905.ORCID 0000-0003-3657-6100
Samuel J BunceAstbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, United Kingdom.
Sheena E RadfordAstbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, United Kingdom.
Andrew J WilsonAstbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, United Kingdom.ORCID 0000-0001-9852-6366
Stefan AuerSchool of Chemistry, University of Leeds, LS2 9JT Leeds, United Kingdom.
Carol K HallDepartment of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905; hall@ncsu.edu.
University of Leeds · GBNorth Carolina State University · US

Funding

Biotechnology Research Partnerships Renewal: Aggregation of Therapeutic ProteinsR01EB006006 · NIBIB · UNIVERSITY OF COLORADO · PI RANDOLPH, THEODORE W · 2006 to 2017
$7.2M
Biotechnology and Biological Sciences Research Council BB/J014443/1NIBIB NIH HHS R01 EB006006Wellcome TrustWellcome Trust 090932/Z/09/Z
6 · The paper itself

Abstract

The aggregation of monomeric amyloid β protein (Aβ) peptide into oligomers and amyloid fibrils in the mammalian brain is associated with Alzheimer's disease. Insight into the thermodynamic stability of the Aβ peptide in different polymeric states is fundamental to defining and predicting the aggregation process. Experimental determination of Aβ thermodynamic behavior is challenging due to the transient nature of Aβ oligomers and the low peptide solubility. Furthermore, quantitative calculation of a thermodynamic phase diagram for a specific peptide requires extremely long computational times. Here, using a coarse-grained protein model, molecular dynamics (MD) simulations are performed to determine an equilibrium concentration and temperature phase diagram for the amyloidogenic peptide fragment Aβ

Indexed as

ThermodynamicsAmyloidAmyloid beta-PeptidesPeptide FragmentsProtein AggregatesProtein BindingProtein ConformationProtein MultimerizationSolubilityAmyloidAmyloid beta-PeptidesPeptide FragmentsProtein Aggregatesamyloidcoarse-grained simulationphase diagramprotein aggregationsolubility

Identifiers

PMID30674664
PMCPMC6369758
OpenAlexW2912172518

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.