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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Wild-type α-synuclein inherits the structure and exacerbated neuropathology of E46K mutant fibril strain by cross-seeding
Houfang Long, W. Sharon Zheng, Yang Liu, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 20
Open Access | Times Cited: 42

Showing 1-25 of 42 citing articles:

Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Sjors H. W. Scheres, Benjamin Falcon, Michel Goedert
Nature (2023) Vol. 621, Iss. 7980, pp. 701-710
Closed Access | Times Cited: 110
Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases
Dan Li, Cong Liu
Nature reviews. Neuroscience (2022) Vol. 23, Iss. 9, pp. 523-534
Closed Access | Times Cited: 75
Structure of alpha-synuclein fibrils derived from human Lewy body dementia tissue
Dhruva Dhavale, Alexander M. Barclay, Collin G. Borcik, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 28
Aspirin inhibits proteasomal degradation and promotes α-synuclein aggregate clearance through K63 ubiquitination
Jing Gao, Yan Liu, Chenfang Si, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 3
Conformational Dynamics of an α-Synuclein Fibril upon Receptor Binding Revealed by Insensitive Nuclei Enhanced by Polarization Transfer-Based Solid-State Nuclear Magnetic Resonance and Cryo-Electron Microscopy
Shengnan Zhang, Juan Li, Qianhui Xu, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 8, pp. 4473-4484
Closed Access | Times Cited: 29
Protein amyloid aggregate: Structure and function
Qianhui Xu, Yeyang Ma, Yunpeng Sun, et al.
Aggregate (2023) Vol. 4, Iss. 4
Open Access | Times Cited: 29
Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments
Yulong Bai, Shengnan Zhang, Hui Dong, et al.
Chemical Reviews (2023) Vol. 123, Iss. 21, pp. 12254-12311
Closed Access | Times Cited: 26
A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity
Senthil T. Kumar, Anne‐Laure Mahul‐Mellier, Ramanath Narayana Hegde, et al.
Science Advances (2022) Vol. 8, Iss. 17
Open Access | Times Cited: 30
Distinct Effects of Familial Parkinson’s Disease-Associated Mutations on α-Synuclein Phase Separation and Amyloid Aggregation
Bingkuan Xu, Fengshuo Fan, Yunpeng Liu, et al.
Biomolecules (2023) Vol. 13, Iss. 5, pp. 726-726
Open Access | Times Cited: 21
α-Synuclein Strains and Their Relevance to Parkinson’s Disease, Multiple System Atrophy, and Dementia with Lewy Bodies
Noah J. Graves, Yann Gambin, Emma Sierecki
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 15, pp. 12134-12134
Open Access | Times Cited: 17
On the pH-dependence of α-synuclein amyloid polymorphism and the role of secondary nucleation in seed-based amyloid propagation
Lukas Frey, Dhiman Ghosh, Bilal M. Qureshi, et al.
eLife (2024) Vol. 12
Open Access | Times Cited: 8
Cyclic Ion Mobility-Mass Spectrometry and Tandem Collision Induced Unfolding for Quantification of Elusive Protein Biomarkers
Devin M. Makey, Varun V. Gadkari, Robert T. Kennedy, et al.
Analytical Chemistry (2024) Vol. 96, Iss. 15, pp. 6021-6029
Open Access | Times Cited: 6
Consequences of variability in α-synuclein fibril structure on strain biology
Sara A. M. Holec, Samantha L Liu, Amanda L. Woerman
Acta Neuropathologica (2022) Vol. 143, Iss. 3, pp. 311-330
Closed Access | Times Cited: 26
Real-Time Fast Amyloid Seeding and Translocation of α-Synuclein with a Nanopipette
Nathan Meyer, Jean‐Marc Janot, Joan Torrent, et al.
ACS Central Science (2022) Vol. 8, Iss. 4, pp. 441-448
Open Access | Times Cited: 26
Molecular rules governing the structural polymorphism of amyloid fibrils in neurodegenerative diseases
Dan Li, Cong Liu
Structure (2023) Vol. 31, Iss. 11, pp. 1335-1347
Closed Access | Times Cited: 13
Multiple system atrophy prions transmit neurological disease to mice expressing wild-type human α-synuclein
Sara A. M. Holec, Jisoo Lee, Abby Oehler, et al.
Acta Neuropathologica (2022) Vol. 144, Iss. 4, pp. 677-690
Open Access | Times Cited: 20
Protein Aggregation and its Affecting Mechanisms in Neurodegenerative Diseases.
Junyun Wu, Jianan Wu, Tao Chen, et al.
Neurochemistry International (2024) Vol. 180, pp. 105880-105880
Closed Access | Times Cited: 4
Drosophila aux orchestrates the phosphorylation-dependent assembly of the lysosomal V-ATPase in glia and contributes to SNCA/α-synuclein degradation
Shiping Zhang, Linfang Wang, Shuanglong Yi, et al.
Autophagy (2025), pp. 1-20
Open Access
Binding adaptability of chemical ligands to polymorphic α-synuclein amyloid fibrils
Kaien Liu, Youqi Tao, Qinyue Zhao, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 35
Closed Access | Times Cited: 3
Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases
Arpine Sokratian, Ye Zhou, Meltem Tatlı, et al.
Science Advances (2024) Vol. 10, Iss. 44
Open Access | Times Cited: 3
Physiological and pathological effects of phase separation in the central nervous system
Jiaxin Wang, Hongrui Zhu, Ruijia Tian, et al.
Journal of Molecular Medicine (2024) Vol. 102, Iss. 5, pp. 599-615
Open Access | Times Cited: 2
Exogenous Amyloid Fibrils Can Cause Significant Upregulation of Neurodegenerative Disease Proteins
Xihua Liu, Wenzhe Jia, Yapeng Fang, et al.
ACS Chemical Neuroscience (2024)
Closed Access | Times Cited: 2
The E46K mutation modulates α-synuclein prion replication in transgenic mice
Sara A. M. Holec, Jisoo Lee, Abby Oehler, et al.
PLoS Pathogens (2022) Vol. 18, Iss. 12, pp. e1010956-e1010956
Open Access | Times Cited: 10
Structure of alpha-synuclein fibrils derived from human Lewy body dementia tissue
Dhruva Dhavale, Alexander M. Barclay, Collin G. Borcik, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6
Chemical probes for investigating protein liquid-liquid phase separation and aggregation
Rui Sun, Shenqing Zhang, Yu Liu, et al.
Current Opinion in Chemical Biology (2023) Vol. 74, pp. 102291-102291
Closed Access | Times Cited: 6
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