Evidence map›Paper›PMID 37964757›Full record

ArticlePhysical chemistry chemical physics : PCCP2023

Co-aggregation of α-synuclein with amyloid-β stabilizes β-sheet-rich oligomers and enhances the formation of β-barrels.

Fengjuan Huang, Yuying Liu, Ying Wang, Jia Xu, Jiangfang Lian, Yu Zou, Chuang Wang, Feng Ding, Yunxiang Sun

Open access · greenAbstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.1field-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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Effect of high hydrostatic pressure onFrontiers in nutrition · 2026
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  6. Polyoxometalates bind multiple targets involved in Alzheimer's disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  7. Computational insights into the aggregation mechanism of human calcitonin.International journal of biological macromolecules · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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 at 4 institutions in 2 countries.

Fengjuan HuangNingbo Institute of Innovation for Combined Medicine and Engineering (NIIME), Ningbo Medical Center Lihuili Hospital, Ningbo 315211, China.
Yuying LiuSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China. sunyunxiang@nbu.edu.cn.
Ying WangSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China. sunyunxiang@nbu.edu.cn.
Jia XuSchool of Medicine, Ningbo University, Ningbo 315211, China. wangchuang@nbu.edu.cn.
Jiangfang LianNingbo Institute of Innovation for Combined Medicine and Engineering (NIIME), Ningbo Medical Center Lihuili Hospital, Ningbo 315211, China.
Yu ZouDepartment of Sport and Exercise Science, Zhejiang University, Hangzhou 310058, China.ORCID http://orcid.org/0000-0001-5699-5869
Chuang WangSchool of Medicine, Ningbo University, Ningbo 315211, China. wangchuang@nbu.edu.cn.
Feng DingDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA. fding@clemson.edu.ORCID http://orcid.org/0000-0003-1850-6336
Yunxiang SunSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China. sunyunxiang@nbu.edu.cn.ORCID http://orcid.org/0000-0001-9799-7131
Ningbo University · CNNingbo Medical Center Lihuili Hospital · CNClemson University · USZhejiang University · 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

Alzheimer's disease (AD) and Parkinson's disease (PD) are the two most common neurodegenerative diseases with markedly different pathological features of β-amyloid (Aβ) plaques and α-synuclein (αS) Lewy bodies (LBs), respectively. However, clinical overlaps in symptoms and pathologies between AD and PD are commonly observed caused by the cross-interaction between Aβ and αS. To uncover the molecular mechanisms behind their overlapping symptoms and pathologies, we computationally investigated the impact of αS on an Aβ monomer and dimerization using atomistic discrete molecular dynamics simulations (DMD). Our results revealed that αS could directly interact with Aβ monomers and dimers, thus forming β-sheet-rich oligomers, including potentially toxic β-barrel intermediates. The binding hotspot involved the second half of the N-terminal domain and NAC region in αS, along with residues 10-21 and 31-42 in Aβ. In their hetero-complex, the binding hotspot primarily assumed a β-sheet core buried inside, which was dynamically shielded by the highly charged, amyloid-resistant C-terminus of αS. Because the amyloid prion region was the same as the binding hotspot being buried, their fibrillization may be delayed, causing the toxic oligomers to increase. This study sheds light on the intricate relationship between Aβ and αS and provides insights into the overlapping pathology of AD and PD.

Indexed as

Alzheimer DiseaseParkinson Diseasealpha-SynucleinAmyloid beta-PeptidesHumansProtein Conformation, beta-Strandalpha-SynucleinAmyloid beta-Peptides

Identifiers

PMID37964757
PMCPMC10704842
OpenAlexW4388153824

What Socratic 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 Socratic graph.