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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:

Decreasing amyloid toxicity through an increased rate of aggregation
Silvia Sonzini, Helen F. Stanyon, Oren A. Scherman
Physical Chemistry Chemical Physics (2016) Vol. 19, Iss. 2, pp. 1458-1465
Open Access | Times Cited: 26

Showing 1-25 of 26 citing articles:

Unconjugated PLGA nanoparticles attenuate temperature-dependent β-amyloid aggregation and protect neurons against toxicity: implications for Alzheimer’s disease pathology
Pallabi Sil Paul, Jae‐Young Cho, Qi Wu, et al.
Journal of Nanobiotechnology (2022) Vol. 20, Iss. 1
Open Access | Times Cited: 29
Cucurbit[8]uril Binds Nonterminal Dipeptide Sites with High Affinity and Induces a Type II β-Turn
Paolo Suating, Lauren B. Kimberly, Marc B. Ewe, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 11, pp. 7649-7657
Closed Access | Times Cited: 7
Modulating the aggregation of amyloid proteins by macrocycles
Li Gao, Yanmei Li
Aggregate (2022) Vol. 3, Iss. 2
Open Access | Times Cited: 26
Small-Molecule Inhibitors of Amyloid Beta: Insights from Molecular Dynamics—Part A: Endogenous Compounds and Repurposed Drugs
Mariyana Atanasova
Pharmaceuticals (2025) Vol. 18, Iss. 3, pp. 306-306
Open Access
What Is the “Relevant” Amyloid β42 Concentration?
Jevgenij A. Raskatov
ChemBioChem (2019) Vol. 20, Iss. 13, pp. 1725-1726
Open Access | Times Cited: 30
Mimosine functionalized gold nanoparticles (Mimo-AuNPs) suppress β-amyloid aggregation and neuronal toxicity
Bibin G. Anand, Qi Wu, Govindarajan Karthivashan, et al.
Bioactive Materials (2021) Vol. 6, Iss. 12, pp. 4491-4505
Open Access | Times Cited: 26
Molecular recognition of peptides and proteins by cucurbit[n]urils: systems and applications
Lyle Armstrong, Sarah L. Chang, Nia Clements, et al.
Chemical Society Reviews (2024)
Open Access | Times Cited: 3
From structure to application: Progress and opportunities in peptide materials development
Tania L. Lopez-Silva, Joel P. Schneider
Current Opinion in Chemical Biology (2021) Vol. 64, pp. 131-144
Open Access | Times Cited: 22
Constraints on the Structure of Fibrils Formed by a Racemic Mixture of Amyloid-β Peptides from Solid-State NMR, Electron Microscopy, and Theory
Jevgenij A. Raskatov, Alejandro R. Foley, John M. Louis, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 33, pp. 13299-13313
Open Access | Times Cited: 22
Tau Derived Hexapeptide AcPHF6 Promotes Beta-Amyloid (Aβ) Fibrillogenesis
Tarek Mohamed, Sarbjeet Singh Gujral, Praveen P. N. Rao
ACS Chemical Neuroscience (2017) Vol. 9, Iss. 4, pp. 773-782
Closed Access | Times Cited: 22
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease
Tatsuya Ikenoue, Francesco A. Aprile, Pietro Sormanni, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 18
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: 6
Differential Modulation of the Aggregation of N‐Terminal Truncated Aβ using Cucurbiturils
Li Gao, Wuyue Yang, Yufen Zhao, et al.
Chemistry - A European Journal (2018) Vol. 24, Iss. 51, pp. 13647-13653
Closed Access | Times Cited: 19
Cucurbituril-Oriented Nanoplatforms in Biomedical Applications
Guowang Cheng, Jingshan Luo, Yao Liu, et al.
ACS Applied Bio Materials (2020) Vol. 3, Iss. 12, pp. 8211-8240
Closed Access | Times Cited: 17
Small Molecules N-Phenylbenzofuran-2-carboxamide and N-Phenylbenzo[b]thiophene-2-carboxamide Promote Beta-Amyloid (Aβ42) Aggregation and Mitigate Neurotoxicity
Yusheng Zhao, Praveen P. N. Rao
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 23, pp. 4185-4198
Closed Access | Times Cited: 5
Molecular Dynamics Studies of Atomistically Determined Fibrillar Assemblies: Comparison of the Rippled β-Sheet, Pleated β-Sheet, and Herringbone Structures
Hyeonju Lee, Moon Young Yang, Jevgenij A. Raskatov, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 17, pp. 4568-4574
Closed Access | Times Cited: 1
Rationally Designed Peptoid Inhibitors of Amyloid‐β Oligomerization
Mihyun Lim Waugh, Lauren M. Wolf, Kelly A. Moore, et al.
ChemBioChem (2024) Vol. 25, Iss. 13
Open Access | Times Cited: 1
A role of sea buckthorn on Alzheimer’s disease
Ke Dong, Warnakulasuriya Mary Ann Dipika Binosha Fernando, Rosalie J Durham, et al.
International Journal of Food Science & Technology (2020) Vol. 55, Iss. 9, pp. 3073-3081
Closed Access | Times Cited: 12
Improved Physical Stability of an Antibody–Drug Conjugate Using Host–Guest Chemistry
Silvia Sonzini, Maria Laura Greco, Thaïs Cailleau, et al.
Bioconjugate Chemistry (2019) Vol. 31, Iss. 1, pp. 123-129
Closed Access | Times Cited: 8
Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar Structures
Tatsuya Ikenoue, Francesco A. Aprile, Pietro Sormanni, et al.
Frontiers in Neuroscience (2021) Vol. 15
Open Access | Times Cited: 7
Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up?
Yong Xu, Roberto Maya‐Martinez, Sheena E. Radford
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 959-975
Open Access | Times Cited: 4
Insights into β-amyloid transition prevention by cucurbit[7]uril from molecular modeling
Osmair Vital de Oliveira, Arlan da Silva Gonçalves, Natália E. C. de Almeida
Journal of Biomolecular Structure and Dynamics (2021) Vol. 40, Iss. 20, pp. 9602-9612
Closed Access | Times Cited: 5
Cucurbituril-functionalized Supramolecular Assemblies: Gateways to Diverse Applications
Jyotirmayee Mohanty, Raman Khurana, N. Barooah, et al.
The Royal Society of Chemistry eBooks (2019), pp. 235-257
Closed Access | Times Cited: 3
Molecular Recognition of Proteins by Cucurbiturils
Pim J. de Vink, Luc Brunsveld
The Royal Society of Chemistry eBooks (2019), pp. 464-482
Closed Access | Times Cited: 2
Thermo-Responsive self-assembly of a dual glucagon-like peptide and glucagon receptor agonist
Sonja Kinna, Myriam Ouberaï, Silvia Sonzini, et al.
International Journal of Pharmaceutics (2021) Vol. 604, pp. 120719-120719
Closed Access | Times Cited: 2
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