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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:

Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β 40 (Aβ 40 ) by the peptide fragment Aβ 16–22
Samuel J. Bunce, Yiming Wang, Katie L. Stewart, et al.
Science Advances (2019) Vol. 5, Iss. 6
Open Access | Times Cited: 71

Showing 1-25 of 71 citing articles:

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Phuong H. Nguyen, Ayyalusamy Ramamoorthy, Bikash R. Sahoo, et al.
Chemical Reviews (2021) Vol. 121, Iss. 4, pp. 2545-2647
Open Access | Times Cited: 539
Amyloid structures: much more than just a cross-β fold
Rodrigo Gallardo, Neil A. Ranson, Sheena E. Radford
Current Opinion in Structural Biology (2019) Vol. 60, pp. 7-16
Open Access | Times Cited: 180
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
Recent Advances in Coarse-Grained Models for Biomolecules and Their Applications
Nidhi Singh, Wenjin Li
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 15, pp. 3774-3774
Open Access | Times Cited: 99
Structures of the intrinsically disordered Aβ, tau and α-synuclein proteins in aqueous solution from computer simulations
Hoang-Phuong Nguyen, Philippe Derreumaux
Biophysical Chemistry (2020) Vol. 264, pp. 106421-106421
Closed Access | Times Cited: 91
General Principles Underpinning Amyloid Structure
Taylor AIP, Rosemary A. Staniforth
Frontiers in Neuroscience (2022) Vol. 16
Open Access | Times Cited: 39
Structural evolution of fibril polymorphs during amyloid assembly
Martin Wilkinson, Yong Xu, Dev Thacker, et al.
Cell (2023) Vol. 186, Iss. 26, pp. 5798-5811.e26
Open Access | Times Cited: 36
Direct observation of secondary nucleation along the fibril surface of the amyloid β 42 peptide
Dev Thacker, Mohammad Barghouth, Mara Bless, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 25
Open Access | Times Cited: 24
Controlled Noncovalent Synthesis of Secondary Supramolecular Polymers
Souvik Sarkar, Raju Laishram, Darshana Deb, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 40, pp. 22009-22018
Closed Access | Times Cited: 24
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
Molecular Insights into the Misfolding and Dimerization Dynamics of the Full-Length α-Synuclein from Atomistic Discrete Molecular Dynamics Simulations
Yu Zhang, Ying Wang, Yuying Liu, et al.
ACS Chemical Neuroscience (2022) Vol. 13, Iss. 21, pp. 3126-3137
Open Access | Times Cited: 34
Challenges in studying the liquid-to-solid phase transitions of proteins using computer simulations
Beata Szała-Mendyk, Tien M. Phan, Priyesh Mohanty, et al.
Current Opinion in Chemical Biology (2023) Vol. 75, pp. 102333-102333
Open Access | Times Cited: 17
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
Ultrasmall Molybdenum Disulfide Quantum Dots Cage Alzheimer’s Amyloid Beta to Restore Membrane Fluidity
Yuhuan Li, Huayuan Tang, Houjuan Zhu, et al.
ACS Applied Materials & Interfaces (2021) Vol. 13, Iss. 25, pp. 29936-29948
Open Access | Times Cited: 34
Molecular Scale Structure and Kinetics of Layer-by-Layer Peptide Self-Organization at Atomically Flat Solid Surfaces
Ayhan Yurtsever, Linhao Sun, Kaito Hirata, et al.
ACS Nano (2023) Vol. 17, Iss. 8, pp. 7311-7325
Closed Access | Times Cited: 16
SEVI Inhibits Aβ Amyloid Aggregation by Capping the β-Sheet Elongation Edges
Ying Wang, Jia Xu, Fengjuan Huang, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 11, pp. 3567-3578
Open Access | Times Cited: 15
Spike Protein Fragments Promote Alzheimer’s Amyloidogenesis
Sujian Cao, Zhiyuan Song, Jinyu Rong, et al.
ACS Applied Materials & Interfaces (2023) Vol. 15, Iss. 34, pp. 40317-40329
Open Access | Times Cited: 15
The Double-Layered Structure of Amyloid-β Assemblage on GM1-Containing Membranes Catalytically Promotes Fibrillization
Maho Yagi‐Utsumi, Satoru Itoh, Hisashi Okumura, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 15, pp. 2648-2657
Open Access | Times Cited: 13
Using protein engineering to understand and modulate aggregation
Jessica S. Ebo, Nicolas Guthertz, Sheena E. Radford, et al.
Current Opinion in Structural Biology (2020) Vol. 60, pp. 157-166
Open Access | Times Cited: 38
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, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 46, pp. 31604-31614
Closed Access | Times Cited: 13
Molecular Insights into the Effects of F16L and F19L Substitutions on the Conformation and Aggregation Dynamics of Human Calcitonin
Fengjuan Huang, Jiahui Huang, Jiajia Yan, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 11, pp. 4500-4510
Closed Access | Times Cited: 4
Accelerated Alzheimer’s Aβ-42 secondary nucleation chronologically visualized on fibril surfaces
Peter Niraj Nirmalraj, Shayon Bhattacharya, Damien Thompson
Science Advances (2024) Vol. 10, Iss. 43
Open Access | Times Cited: 4
Computational Exploration of the Self-Aggregation Mechanisms of Phenol-Soluble Modulins β1 and β2 in Staphylococcus aureus Biofilms
Huan Xu, Xiaohan Zhang, Zhongyue Lv, et al.
Colloids and Surfaces B Biointerfaces (2025) Vol. 248, pp. 114498-114498
Closed Access
Concentration-dependent polymorphism of insulin amyloid fibrils
Andrius Sakalauskas, Mantas Žiaunys, Vytautas Smirnovas
PeerJ (2019) Vol. 7, pp. e8208-e8208
Open Access | Times Cited: 34
Amyloid Evolution: Antiparallel Replaced by Parallel
Ali Asghar Hakami Zanjani, Nicholas P. Reynolds, Afang Zhang, et al.
Biophysical Journal (2020) Vol. 118, Iss. 10, pp. 2526-2536
Open Access | Times Cited: 32
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