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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:

High-Throughput Screening at the Membrane Interface Reveals Inhibitors of Amyloid-β
Sarah J. Cox, Brian Lam, Ajay Prasad, et al.
Biochemistry (2020) Vol. 59, Iss. 24, pp. 2249-2258
Open Access | Times Cited: 44

Showing 1-25 of 44 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: 545
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
Mechanistic Insight into the Design of Chemical Tools to Control Multiple Pathogenic Features in Alzheimer’s Disease
Jiyeon Han, Cheng‐Feng Du, Mi Hee Lim
Accounts of Chemical Research (2021) Vol. 54, Iss. 20, pp. 3930-3940
Closed Access | Times Cited: 52
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: 40
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
Early stage β-amyloid-membrane interactions modulate lipid dynamics and influence structural interfaces and fibrillation
June M. Kenyaga, Qinghui Cheng, Wei Qiang
Journal of Biological Chemistry (2022) Vol. 298, Iss. 10, pp. 102491-102491
Open Access | Times Cited: 23
Metal-Complexes Bearing Releasable CO Differently Modulate Amyloid Aggregation
Sara La Manna, Valentina Roviello, Fabiana Napolitano, et al.
Inorganic Chemistry (2023) Vol. 62, Iss. 26, pp. 10470-10480
Open Access | Times Cited: 12
Alleviating the unwanted effects of oxidative stress on Aβ clearance: a review of related concepts and strategies for the development of computational modelling
Sarawoot Somin, Don Kulasiri, Sandhya Samarasinghe
Translational Neurodegeneration (2023) Vol. 12, Iss. 1
Open Access | Times Cited: 11
Molecular Mechanism in the Disruption of Chronic Traumatic Encephalopathy-Related R3–R4 Tau Protofibril by Quercetin and Gallic Acid: Similarities and Differences
Jiaxing Tang, Yu Zou, Yehong Gong, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 5, pp. 897-908
Closed Access | Times Cited: 10
Recent developments in the chemical biology of amyloid-β oligomer targeting
Yalin Wang, Jiefang Chen, Furong Gao, et al.
Organic & Biomolecular Chemistry (2023) Vol. 21, Iss. 22, pp. 4540-4552
Closed Access | Times Cited: 10
The Effects of Naturally Occurring Phenols on Amyloid Fibrils from Insulin in the Liquid Phase Using Atomic Force Microscopy
Divya B. Dasani, Tyler P. Nghiem, Katherine A. Facteau, et al.
Natural Product Communications (2025) Vol. 20, Iss. 2
Open Access
Green tea extract EGCG plays a dual role in Aβ42 protofibril disruption and membrane protection: A molecular dynamic study
Xuewei Dong, Yiming Tang, Chendi Zhan, et al.
Chemistry and Physics of Lipids (2020) Vol. 234, pp. 105024-105024
Closed Access | Times Cited: 27
Nanomaterial synthesis, an enabler of amyloidosis inhibition against human diseases
Nikolaos K. Andrikopoulos, Yuhuan Li, Luca Cecchetto, et al.
Nanoscale (2020) Vol. 12, Iss. 27, pp. 14422-14440
Closed Access | Times Cited: 24
The interplay between lipid and Aβ amyloid homeostasis in Alzheimer’s Disease: risk factors and therapeutic opportunities
Sara García‐Viñuales, Michele F. M. Sciacca, Valeria Lanza, et al.
Chemistry and Physics of Lipids (2021) Vol. 236, pp. 105072-105072
Closed Access | Times Cited: 22
Experimental approaches for altering the expression of Abeta‐degrading enzymes
David A. Loeffler
Journal of Neurochemistry (2023) Vol. 164, Iss. 6, pp. 725-763
Open Access | Times Cited: 9
Inhibition of Aβ16–22 Peptide Aggregation by Small Molecules and Their Permeation through POPC Lipid Bilayer: Insight from Molecular Dynamics Simulation Study
Rabindranath Paul, Siddhartha Bera, Madhusmita Devi, et al.
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 21, pp. 5193-5207
Closed Access | Times Cited: 14
Five similar anthocyanidin molecules display distinct disruptive effects and mechanisms of action on Aβ1–42 protofibril: A molecular dynamic simulation study
Yujie Chen, Chendi Zhan, Xuhua Li, et al.
International Journal of Biological Macromolecules (2023) Vol. 256, pp. 128467-128467
Closed Access | Times Cited: 8
Novel Peptide-Calix[4]arene Conjugate Inhibits Aβ Aggregation and Rescues Neurons from Aβ’s Oligomers Cytotoxicity In Vitro
Grazia M. L. Consoli, Rita Tosto, Ausilia Baglieri, et al.
ACS Chemical Neuroscience (2021) Vol. 12, Iss. 8, pp. 1449-1462
Open Access | Times Cited: 17
KLVFF oligopeptide-decorated amphiphilic cyclodextrin nanomagnets for selective amyloid beta recognition and fishing
Antonino Mazzaglia, Giuseppe Di Natale, Rita Tosto, et al.
Journal of Colloid and Interface Science (2022) Vol. 613, pp. 814-826
Closed Access | Times Cited: 12
Recent advances in the modulation of amyloid protein aggregation using the supramolecular host-guest approaches
Debabrata Maity
Biophysical Chemistry (2023) Vol. 297, pp. 107022-107022
Closed Access | Times Cited: 7
Extracellular vesicles: the key to unlocking mechanisms of age-related vascular disease?
Meredith Whitehead, Marco Antonazzi, Catherine M. Shanahan
The Journal of Cardiovascular Aging (2024) Vol. 4, Iss. 1
Open Access | Times Cited: 2
Effect of tert-alcohol functional imidazolium salts on oligomerization and fibrillization of amyloid β (1–42) peptide
Madhukar S. Said, Govinda R. Navale, Ashok Yadav, et al.
Biophysical Chemistry (2020) Vol. 267, pp. 106480-106480
Closed Access | Times Cited: 18
Cholesterol Molecules Alter the Energy Landscape of Small Aβ1–42 Oligomers
Sơn Tùng Ngô, Phuong H. Nguyen, Philippe Derreumaux
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 9, pp. 2299-2307
Open Access | Times Cited: 16
Noncanonical protein kinase A activation by oligomerization of regulatory subunits as revealed by inherited Carney complex mutations
Naeimeh Jafari, Jason C. Del Rio, Madoka Akimoto, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 21
Open Access | Times Cited: 15
Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics
Debabrata Maity
ChemMedChem (2022) Vol. 18, Iss. 2
Closed Access | Times Cited: 11
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