Evidence map›Paper›PMID 39226847›Full record

ArticleColloids and surfaces. B, Biointerfaces2024

Computational insights into the aggregation mechanism and amyloidogenic core of aortic amyloid medin polypeptide.

Fengjuan Huang, Jiajia Yan, Xiaohan Zhang, Huan Xu, Jiangfang Lian, Xi Yang, Chuang Wang, Feng Ding, Yunxiang Sun

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Colloids and surfaces. B, Biointerfaces, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. The Glycine-Rich Region as a Flexible Molecular Glue Promoting hPrPJournal of chemical information and modeling · 2025
    Article
  3. Article
  4. Article
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

9 authors.

Fengjuan HuangNingbo Institute of Innovation for Combined Medicine and Engineering (NIIME), Ningbo Medical Center Lihuili Hospital, Ningbo 315211, China.
Jiajia YanSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China.
Xiaohan ZhangSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China.
Huan XuSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China.
Jiangfang LianNingbo Institute of Innovation for Combined Medicine and Engineering (NIIME), Ningbo Medical Center Lihuili Hospital, Ningbo 315211, China.
Xi YangNingbo Institute of Innovation for Combined Medicine and Engineering (NIIME), Ningbo Medical Center Lihuili Hospital, Ningbo 315211, China.
Chuang WangSchool of Medicine, Ningbo University, Ningbo 315211, China. Electronic address: wangchuang@nbu.edu.cn.
Feng DingDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, United States. Electronic address: fding@clemson.edu.
Yunxiang SunSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China; Department of Physics and Astronomy, Clemson University, Clemson, SC 29634, United States. Electronic address: sunyunxiang@nbu.edu.cn.

Funding

Tissue Structural and Neural Remodeling in Human Sacroiliac JointP20GM121342 · NIGMS · CLEMSON UNIVERSITY · PI Jeryl Jones · 2018 to 2026
$24.7M
Inhibition of Human Islet Amyloid Polypeptide AggregationR35GM145409 · NIGMS · CLEMSON UNIVERSITY · PI Feng Ding · 2022 to 2026
$2.0M
NIGMS NIH HHS P20 GM121342NIGMS NIH HHS R35 GM145409
6 · The paper itself

Abstract

Medin amyloid, prevalent in the vessel walls of 97 % of individuals over 50, contributes to arterial stiffening and cerebrovascular dysfunction, yet our understanding of its aggregation mechanism remains limited. Dividing the full-length 50-amino-acid medin peptide into five 10-residue segments, we conducted individual investigations on each segment's self-assembly dynamics via microsecond-timescale atomistic discrete molecular dynamics (DMD) simulations. Our findings showed that medin

Indexed as

AmyloidMolecular Dynamics SimulationAmino Acid SequenceAntigens, SurfaceAortaHumansMilk ProteinsPeptidesProtein AggregatesProtein Conformation, beta-StrandAmyloidAntigens, SurfaceMFGE8 protein, humanMilk ProteinsPeptidesProtein AggregatesAggregation mechanismAmyloid-aggregationAmyloidogenic coreComputational simulationMedin

Identifiers

PMID39226847
PMCPMC11588409

What Socratic holds

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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 Socratic graph.