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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:

Visualizing and trapping transient oligomers in amyloid assembly pathways
Emma E. Cawood, Theodoros K. Karamanos, Andrew J. Wilson, et al.
Biophysical Chemistry (2020) Vol. 268, pp. 106505-106505
Open Access | Times Cited: 116

Showing 1-25 of 116 citing articles:

Protein–Small Molecule Interactions in Native Mass Spectrometry
Jack L. Bennett, Giang Nguyen, William A. Donald
Chemical Reviews (2021) Vol. 122, Iss. 8, pp. 7327-7385
Closed Access | Times Cited: 104
Energy Landscapes of Protein Aggregation and Conformation Switching in Intrinsically Disordered Proteins
Birgit Strodel
Journal of Molecular Biology (2021) Vol. 433, Iss. 20, pp. 167182-167182
Closed Access | Times Cited: 88
Drug delivery of memantine with carbon dots for Alzheimer’s disease: blood–brain barrier penetration and inhibition of tau aggregation
Wei Zhang, Nabin Kandel, Yiqun Zhou, et al.
Journal of Colloid and Interface Science (2022) Vol. 617, pp. 20-31
Open Access | Times Cited: 66
Molecular insights into the phase transition of lysozyme into amyloid nanostructures: Implications of therapeutic strategies in diverse pathological conditions
Sindhujit Roy, Venkat Ramanan Srinivasan, Subash Arunagiri, et al.
Advances in Colloid and Interface Science (2024) Vol. 331, pp. 103205-103205
Closed Access | Times Cited: 10
A brief history of amyloid aggregation simulations
Hebah Fatafta, Mohammed Khaled, Batuhan Kav, et al.
Wiley Interdisciplinary Reviews Computational Molecular Science (2024) Vol. 14, Iss. 1
Closed Access | Times Cited: 9
The folding and misfolding of multidomain proteins
Stefano Gianni, Maurizio Brunori
Molecular Aspects of Medicine (2025) Vol. 101, pp. 101337-101337
Closed Access | Times Cited: 1
Rapid discovery of cyclic peptide protein aggregation inhibitors by continuous selection
Linwei Yang, Jingwei Zhang, James S. Andon, et al.
Nature Chemical Biology (2025)
Closed Access | Times Cited: 1
Molecular insight into cross-interaction between amyloid β isoforms and its effect on aggregation pathways
Li Wang, Sanghwan Park, Jae Hong Choi, et al.
Journal of Biomolecular Structure and Dynamics (2025), pp. 1-11
Closed Access | Times Cited: 1
A mechanistic survey of Alzheimer's disease
Yijing Tang, Dong Zhang, Xiong Gong, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106735-106735
Open Access | Times Cited: 45
Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein
Sabine M. Ulamec, Roberto Maya‐Martinez, Emily J. Byrd, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 37
Lipids uniquely alter rates of insulin aggregation and lower toxicity of amyloid aggregates
Mikhail Matveyenka, Stanislav Rizevsky, Jean‐Philippe Pellois, et al.
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (2022) Vol. 1868, Iss. 1, pp. 159247-159247
Open Access | Times Cited: 35
Taking Charge: Metal Ions Accelerate Amyloid Aggregation in Sequence Variants of α-Synuclein
Emily J. Byrd, Martin Wilkinson, Sheena E. Radford, et al.
Journal of the American Society for Mass Spectrometry (2023) Vol. 34, Iss. 3, pp. 493-504
Open Access | Times Cited: 17
Mechanism of Protein Aggregation Inhibition by Arginine: Blockage of Anionic Side Chains Favors Unproductive Encounter Complexes
Yuen Ki Ng, Lars Konermann
Journal of the American Chemical Society (2024) Vol. 146, Iss. 12, pp. 8394-8406
Closed Access | Times Cited: 8
Kinetics theories to understand the mechanism of aggregation of a protein and to design strategies for its inhibition
Shilpa Sharma, Priya Modi, Gargi Sharma, et al.
Biophysical Chemistry (2021) Vol. 278, pp. 106665-106665
Closed Access | Times Cited: 39
A Comprehensive Insight into the Mechanisms of Dopamine in Disrupting Aβ Protofibrils and Inhibiting Aβ Aggregation
Yujie Chen, Xuhua Li, Chendi Zhan, et al.
ACS Chemical Neuroscience (2021) Vol. 12, Iss. 21, pp. 4007-4019
Closed Access | Times Cited: 39
Direct observation of protein structural transitions through entire amyloid aggregation processes in water using 2D-IR spectroscopy
So Yeon Chun, Myung Kook Son, Chae Ri Park, et al.
Chemical Science (2022) Vol. 13, Iss. 16, pp. 4482-4489
Open Access | Times Cited: 24
Decoding the Roles of Amyloid-β (1–42)’s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors
Dongjoon Im, Soohyeong Kim, Gyusub Yoon, et al.
JACS Au (2023) Vol. 3, Iss. 4, pp. 1065-1075
Open Access | Times Cited: 16
Disease-relevant β2-microglobulin variants share a common amyloid fold
Martin Wilkinson, Rodrigo Gallardo, Roberto Maya‐Martinez, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15
Protein Oligomer Engineering: A New Frontier for Studying Protein Structure, Function, and Toxicity
Chang Liu, Jinghui Luo
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 23
Open Access | Times Cited: 15
Are fibrinaloid microclots a cause of autoimmunity in Long Covid and other post-infection diseases?
Douglas B. Kell, Etheresia Pretorius
Biochemical Journal (2023) Vol. 480, Iss. 15, pp. 1217-1240
Open Access | Times Cited: 15
Fibrinaloid Microclots and Atrial Fibrillation
Douglas B. Kell, Gregory Y.H. Lip, Etheresia Pretorius
Biomedicines (2024) Vol. 12, Iss. 4, pp. 891-891
Open Access | Times Cited: 5
Characterizing Prion‐Like Protein Aggregation: Emerging Nanopore‐Based Approaches
Nathan Meyer, Joan Torrent, Sébastien Balme
Small Methods (2024)
Open Access | Times Cited: 5
Molecular insights into the primary nucleation of polymorphic amyloid β dimers in DOPC lipid bilayer membrane
Olga Press‐Sandler, Yifat Miller
Protein Science (2022) Vol. 31, Iss. 5
Open Access | Times Cited: 19
Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases
R. Loch, Hongzhi Wang, Alex Perálvarez‐Marín, et al.
Computational and Structural Biotechnology Journal (2023) Vol. 21, pp. 1189-1204
Open Access | Times Cited: 12
Structural Dynamics of Amyloid-β Protofibrils and Actions of Anti-Amyloid-β Antibodies as Observed by High-Speed Atomic Force Microscopy
Takahiro Watanabe‐Nakayama, Mayumi Tsuji, Kenichi Umeda, et al.
Nano Letters (2023) Vol. 23, Iss. 13, pp. 6259-6268
Closed Access | Times Cited: 12
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