Evidence map›Paper›PMID 33356290›Full record

ArticleThe journal of physical chemistry letters2021

Amyloid Aggregation under the Lens of Liquid-Liquid Phase Separation.

Yanting Xing, Aparna Nandakumar, Aleksandr Kakinen, Yunxiang Sun, Thomas P Davis, Pu Chun Ke, Feng Ding

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 76 citations in OpenAlex.

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  6. Chemistry of materials : a publication of the American Chemical Society · 2025
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  14. RNA tailing machinery drives amyloidogenic phase transition.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

7 authors at 4 institutions in 3 countries.

Yanting XingDepartment of Physics and Astronomy, Clemson University, Clemson 29634, South Carolina, United States.
Aparna NandakumarARC Centre of Excellence in Convergent Bio-Nano Science and Technology, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville 3052, VIC, Australia.
Aleksandr KakinenARC Centre of Excellence in Convergent Bio-Nano Science and Technology, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville 3052, VIC, Australia.
Yunxiang SunDepartment of Physics and Astronomy, Clemson University, Clemson 29634, South Carolina, United States.ORCID http://orcid.org/0000-0001-9799-7131
Thomas P DavisARC Centre of Excellence in Convergent Bio-Nano Science and Technology, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville 3052, VIC, Australia.ORCID http://orcid.org/0000-0003-2581-4986
Pu Chun KeARC Centre of Excellence in Convergent Bio-Nano Science and Technology, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville 3052, VIC, Australia.ORCID http://orcid.org/0000-0003-2134-0859
Feng DingDepartment of Physics and Astronomy, Clemson University, Clemson 29634, South Carolina, United States.ORCID http://orcid.org/0000-0003-1850-6336
The University of Queensland · AUMonash University · AUClemson University · USNingbo University · CN

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

Increasing experiments suggest that amyloid peptides can undergo liquid-liquid phase separation (LLPS) before the formation of amyloid fibrils. However, the exact role of LLPS in amyloid aggregation at the molecular level remains elusive. Here, we investigated the LLPS and amyloid fibrillization of a coarse-grained peptide, capable of capturing fundamental properties of amyloid aggregation over a wide range of concentrations in molecular dynamics simulations. On the basis of the Flory-Huggins theory of polymer solutions, we determined the binodal and spinodal concentrations of LLPS in the low-concentration regime, ϕ

Indexed as

Molecular Dynamics SimulationProtein AggregatesAmyloidPeptidesProtein ConformationAmyloidPeptidesProtein Aggregates

Identifiers

PMID33356290
PMCPMC7855599
OpenAlexW3115955672

What OpenQuestion 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 OpenQuestion graph.