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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:

A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
Rodrigo Cataldi, Sean Chia, Katarina Pisani, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 34

Showing 1-25 of 34 citing articles:

Polyphenols: Secondary Metabolites with a Biological Impression
Ecem Bolat, Sümeyye Sarıtaş, Hatice Duman, et al.
Nutrients (2024) Vol. 16, Iss. 15, pp. 2550-2550
Open Access | Times Cited: 19
Resveratrol and neuroprotection: an insight into prospective therapeutic approaches against Alzheimer’s disease from bench to bedside
Fahadul Islam, Mohamed H. Nafady, Md. Rezaul Islam, et al.
Molecular Neurobiology (2022) Vol. 59, Iss. 7, pp. 4384-4404
Closed Access | Times Cited: 57
Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1–42 aggregates
Kiryl Zhaliazka, Mikhail Matveyenka, Dmitry Kurouski
FEBS Journal (2023) Vol. 290, Iss. 12, pp. 3203-3220
Open Access | Times Cited: 37
The Role of Catecholamines in the Pathogenesis of Diseases and the Modified Electrodes for Electrochemical Detection of Catecholamines: A Review
Meng Zhang, Yimeng Wang, Jie Jiang, et al.
Critical Reviews in Analytical Chemistry (2024), pp. 1-22
Closed Access | Times Cited: 8
The degree of unsaturation of fatty acids in phosphatidylserine alters the rate of insulin aggregation and the structure and toxicity of amyloid aggregates
Mikhail Matveyenka, Stanislav Rizevsky, Dmitry Kurouski
FEBS Letters (2022) Vol. 596, Iss. 11, pp. 1424-1433
Open Access | Times Cited: 33
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: 33
Amyloid aggregates exert cell toxicity causing irreversible damages in the endoplasmic reticulum
Mikhail Matveyenka, Stanislav Rizevsky, Dmitry Kurouski
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2022) Vol. 1868, Iss. 11, pp. 166485-166485
Open Access | Times Cited: 32
Nanoscale Characterization of Parallel and Antiparallel β-Sheet Amyloid Beta 1–42 Aggregates
Kiryl Zhaliazka, Dmitry Kurouski
ACS Chemical Neuroscience (2022) Vol. 13, Iss. 19, pp. 2813-2820
Open Access | Times Cited: 29
Lipids uniquely alter secondary structure and toxicity of lysozyme aggregates
Mikhail Matveyenka, Kiryl Zhaliazka, Stanislav Rizevsky, et al.
The FASEB Journal (2022) Vol. 36, Iss. 10
Open Access | Times Cited: 28
The dopaminergic system promotes neprilysin-mediated degradation of amyloid-β in the brain
Naoto Watamura, Naomasa Kakiya, Ryo Fujioka, et al.
Science Signaling (2024) Vol. 17, Iss. 848
Closed Access | Times Cited: 6
Elucidation of Secondary Structure and Toxicity of α-Synuclein Oligomers and Fibrils Grown in the Presence of Phosphatidylcholine and Phosphatidylserine
Tianyi Dou, Mikhail Matveyenka, Dmitry Kurouski
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 17, pp. 3183-3191
Open Access | Times Cited: 14
Electrochemical biosensors for early detection of Alzheimer’s disease
Sanoeva Matlyuba Jakhonkulovna, Gulnoz Bahodirova Kamolovna, Muzaffar Zokirov, et al.
Clinica Chimica Acta (2025), pp. 120278-120278
Closed Access
Charge of Phospholipids Determines the Rate of Lysozyme Aggregation but Not the Structure and Toxicity of Amyloid Aggregates
Kiryl Zhaliazka, Stanislav Rizevsky, Mikhail Matveyenka, et al.
The Journal of Physical Chemistry Letters (2022) Vol. 13, Iss. 38, pp. 8833-8839
Open Access | Times Cited: 19
Transition metal ions and neurotransmitters: coordination chemistry and implications for neurodegeneration
Jeasang Yoo, Jiyeon Han, Mi Hee Lim
RSC Chemical Biology (2023) Vol. 4, Iss. 8, pp. 548-563
Open Access | Times Cited: 12
Modulatory role of copper on hIAPP aggregation and toxicity in presence of insulin
Dipanwita Roy, Narayan Chandra Maity, Sourav Kumar, et al.
International Journal of Biological Macromolecules (2023) Vol. 241, pp. 124470-124470
Closed Access | Times Cited: 11
The coherence between PSMC6 and α-ring in the 26S proteasome is associated with Alzheimer’s disease
Jing Xiong, Xinping Pang, Xianghu Song, et al.
Frontiers in Molecular Neuroscience (2024) Vol. 16
Open Access | Times Cited: 4
Elucidation of the Effect of Phospholipid Charge on the Rate of Insulin Aggregation and Structure and Toxicity of Amyloid Fibrils
Mikhail Matveyenka, Stanislav Rizevsky, Dmitry Kurouski
ACS Omega (2023) Vol. 8, Iss. 13, pp. 12379-12386
Open Access | Times Cited: 10
Serum metabolomics combined with gut microbiota reveals the effects of Polygala tenuifolia polysaccharide on the metabolic and microbial profiles in SAMP8 mouse
Zheng Li, Yuanyuan Li, Jin Zhang, et al.
Journal of Pharmaceutical and Biomedical Analysis (2024) Vol. 251, pp. 116442-116442
Closed Access | Times Cited: 3
Lipids reverse supramolecular chirality and reduce toxicity of amyloid fibrils
Stanislav Rizevsky, Kiryl Zhaliazka, Mikhail Matveyenka, et al.
FEBS Journal (2022) Vol. 289, Iss. 23, pp. 7537-7544
Closed Access | Times Cited: 14
Protein-to-lipid ratio uniquely changes the rate of lysozyme aggregation but does not significantly alter toxicity of mature protein aggregates
Kiryl Zhaliazka, Valeryia Serada, Mikhail Matveyenka, et al.
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (2023) Vol. 1868, Iss. 5, pp. 159305-159305
Open Access | Times Cited: 8
Elucidation of molecular mechanisms by which amyloid β1–42 fibrils exert cell toxicity
Kiryl Zhaliazka, Dmitry Kurouski
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (2024) Vol. 1869, Iss. 6, pp. 159510-159510
Closed Access | Times Cited: 2
Preparation and Characterization of Zn(II)-Stabilized Aβ42 Oligomers
Alicia González Díaz, Rodrigo Cataldi, Benedetta Mannini, et al.
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 14, pp. 2586-2599
Open Access | Times Cited: 2
The dopamine analogue CA140 alleviates AD pathology, neuroinflammation, and rescues synaptic/cognitive functions by modulating DRD1 signaling or directly binding to Abeta
Sehyun Chae, Hyunju Lee, Ha-Eun Lee, et al.
Journal of Neuroinflammation (2024) Vol. 21, Iss. 1
Open Access | Times Cited: 2
Effects of Striatal Amyloidosis on the Dopaminergic System and Behavior: A Comparative Study in Male and Female 5XFAD Mice
Theresa A. Lansdell, Hui Xu, James J. Galligan, et al.
Journal of Alzheimer s Disease (2023) Vol. 94, Iss. 4, pp. 1361-1375
Closed Access | Times Cited: 6
Neuropathology of the Brainstem to Mechanistically Understand and to Treat Alzheimer’s Disease
Ágoston Patthy, János Murai, János Hanics, et al.
Journal of Clinical Medicine (2021) Vol. 10, Iss. 8, pp. 1555-1555
Open Access | Times Cited: 13
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