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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:

Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies
Michael J. Morten, Liina Sirvio, Huzefa Rupawala, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 41
Open Access | Times Cited: 28

Showing 1-25 of 28 citing articles:

Mechanisms and pathology of protein misfolding and aggregation
Nikolaos Louros, Joost Schymkowitz, Frédéric Rousseau
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 12, pp. 912-933
Closed Access | Times Cited: 105
Synucleins: New Data on Misfolding, Aggregation and Role in Diseases
Andrei Surguchov, Alexei Surguchev
Biomedicines (2022) Vol. 10, Iss. 12, pp. 3241-3241
Open Access | Times Cited: 46
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: 25
Single-Molecule Spectroscopy and Super-Resolution Mapping of Physicochemical Parameters in Living Cells
Megan A. Steves, Changdong He, Ke Xu
Annual Review of Physical Chemistry (2024) Vol. 75, Iss. 1, pp. 163-183
Closed Access | Times Cited: 11
Current trends in basic research on Parkinson’s disease: from mitochondria, lysosome to α-synuclein
Hideaki Matsui, Ryōsuke Takahashi
Journal of Neural Transmission (2024) Vol. 131, Iss. 6, pp. 663-674
Open Access | Times Cited: 8
Beyond DNA: new probes for PAINT super-resolution microscopy
Marrit M. E. Tholen, Roderick P. Tas, Yuyang Wang, et al.
Chemical Communications (2023) Vol. 59, Iss. 54, pp. 8332-8342
Open Access | Times Cited: 16
Automated microscopic measurement of fibrinaloid microclots and their degradation by nattokinase, the main natto protease
Justine M. Grixti, Chrispian W. Theron, J. Enrique Salcedo-Sora, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6
Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates
Alexandre Chappard, Craig Leighton, Rebecca S. Saleeb, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 15
Open Access | Times Cited: 14
Multicolor single-molecule localization microscopy: review and prospect
Xi Chen, Xiangyu Wang, Fang Huang, et al.
PhotoniX (2024) Vol. 5, Iss. 1
Open Access | Times Cited: 4
Molecular Determinants of Protein Pathogenicity at the Single‐Aggregate Level
Agnieszka Urbanek, Emily M. Garland, Emily E. Prescott, et al.
Advanced Science (2025)
Open Access
Super-resolution microscopy as drug discovery tool
Lauren Toms, Louis J Fitzpatrick, Philip Auckland
SLAS DISCOVERY (2025) Vol. 31, pp. 100209-100209
Open Access
Recent advances in dynamic single-molecule analysis platforms for diagnostics: advantages over bulk assays and miniaturization approaches
Dang Du Nguyen, Fedor A. Shuklin, Elena Barulina, et al.
Biosensors and Bioelectronics (2025) Vol. 278, pp. 117361-117361
Closed Access
Advancing Biosensing through Super-Resolution Fluorescence Microscopy
Ga‐eun Go, Doory Kim
Biosensors and Bioelectronics (2025), pp. 117374-117374
Closed Access
Two-color coincidence single-molecule pulldown for the specific detection of disease-associated protein aggregates
Rebecca S. Saleeb, Craig Leighton, Ji‐Eun Lee, et al.
Science Advances (2023) Vol. 9, Iss. 46
Open Access | Times Cited: 9
Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics
Elad Arad, Kasper B. Pedersen, Orit Malka, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9
Formation of amyloid fibrils by the regulatory 14-3-3 ζ protein
Darius Šulskis, Mantas Žiaunys, Andrius Sakalauskas, et al.
Open Biology (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 2
Blinking fluorescent probes for single-molecule localization-based super-resolution imaging
Hua Liu, Zhongju Ye, Yanan Deng, et al.
TrAC Trends in Analytical Chemistry (2023) Vol. 169, pp. 117359-117359
Closed Access | Times Cited: 6
Beyond Strains: Molecular Diversity in Alpha-Synuclein at the Center of Disease Heterogeneity
Marcelina J. Wojewska, Maria Otero‐Jimenez, José Guijarro-Nuez, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 17, pp. 13199-13199
Open Access | Times Cited: 5
Transmembrane β-Barrel Models of α-Synuclein Oligomers
Manuela Maurer, Themis Lazaridis
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 22, pp. 7171-7179
Closed Access | Times Cited: 4
Visualizing Amyloid Assembly at the Nanoscale: Insights from Super‐Resolution Imaging
Kaustubh R. Bhuskute, Kai Kikuchi, Zijie Luo, et al.
Analysis & Sensing (2024) Vol. 4, Iss. 4
Open Access | Times Cited: 1
Catalytic physiological amyloids
Elad Arad, Raz Jelinek
Methods in enzymology on CD-ROM/Methods in enzymology (2024), pp. 77-112
Closed Access | Times Cited: 1
Associations of amyloid-β oligomers and plaques with neuropathology in the AppNL-G-F mouse
Jiabin Tang, Helen Huang, Robert C. J. Muirhead, et al.
Brain Communications (2024) Vol. 6, Iss. 4
Open Access | Times Cited: 1
Coiled double amyloid-like fibrils allosterically catalyze hydrolysis of beta-lactam antibiotics
Raz Jelinek, sisira Mambram Kunnath, Elad Arad, et al.
(2024)
Open Access | Times Cited: 1
A glimpse into the structural properties of α‐synuclein oligomers
Jaime Santos, Irantzu Pallarès, Salvador Ventura
BioFactors (2023) Vol. 50, Iss. 3, pp. 439-449
Open Access | Times Cited: 3
Molecular determinants of protein pathogenicity at the single-aggregate level
Agnieszka Urbanek, Emily M. Garland, Emily E. Prescott, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
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