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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:

Isomerization of Asp7 in Beta-Amyloid Enhances Inhibition of the α7 Nicotinic Receptor and Promotes Neurotoxicity
Evgeny P. Barykin, Aleksandra Garifulina, Elena V. Kruykova, et al.
Cells (2019) Vol. 8, Iss. 8, pp. 771-771
Open Access | Times Cited: 31

Showing 1-25 of 31 citing articles:

The Toxicity and Polymorphism of β-Amyloid Oligomers
Yaru Huang, Rui‐tian Liu
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 12, pp. 4477-4477
Open Access | Times Cited: 118
Cholinergic Modulation of Neuroinflammation: Focus on α7 Nicotinic Receptor
Roberta Piovesana, Michael Sebastian Salazar Intriago, Luciana Dini, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 9, pp. 4912-4912
Open Access | Times Cited: 72
An Overview on the Effect of Neonicotinoid Insecticides on Mammalian Cholinergic Functions through the Activation of Neuronal Nicotinic Acetylcholine Receptors
Jean‐Noël Houchat, Alison Cartereau, Anaïs Le Mauff, et al.
International Journal of Environmental Research and Public Health (2020) Vol. 17, Iss. 9, pp. 3222-3222
Open Access | Times Cited: 56
Phosphorylation of the Amyloid-Beta Peptide Inhibits Zinc-Dependent Aggregation, Prevents Na,K-ATPase Inhibition, and Reduces Cerebral Plaque Deposition
Evgeny P. Barykin, Irina Yu. Petrushanko, Sergey A. Kozin, et al.
Frontiers in Molecular Neuroscience (2018) Vol. 11
Open Access | Times Cited: 42
Activation of α7 Nicotinic Acetylcholine Receptor Upregulates HLA-DR and Macrophage Receptors: Potential Role in Adaptive Immunity and in Preventing Immunosuppression
Andrei E. Siniavin, Maria A. Streltsova, Denis S. Kudryavtsev, et al.
Biomolecules (2020) Vol. 10, Iss. 4, pp. 507-507
Open Access | Times Cited: 34
Docking and Molecular Dynamics-Based Identification of Interaction between Various Beta-Amyloid Isoforms and RAGE Receptor
Anna P. Tolstova, Alexei A. Adzhubei, Vladimir A. Mitkevich, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 19, pp. 11816-11816
Open Access | Times Cited: 18
Pharmacokinetics and Molecular Modeling Indicate nAChRα4-Derived Peptide HAEE Goes through the Blood–Brain Barrier
Yu. A. Zolotarev, Vladimir A. Mitkevich, С. И. Шрам, et al.
Biomolecules (2021) Vol. 11, Iss. 6, pp. 909-909
Open Access | Times Cited: 22
Effect of β-amyloid on blood-brain barrier properties and function
Irina Yu. Petrushanko, Vladimir A. Mitkevich, Alexander А. Makarov
Biophysical Reviews (2023) Vol. 15, Iss. 2, pp. 183-197
Open Access | Times Cited: 8
Structure Comparison of Beta Amyloid Peptide Aβ 1–42 Isoforms. Molecular Dynamics Modeling
Anna P. Tolstova, Alexander А. Makarov, Alexei A. Adzhubei
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 3, pp. 918-932
Closed Access | Times Cited: 3
Recent progress in the analysis of protein deamidation using mass spectrometry
Yujia Ying, Huilin Li
Methods (2020) Vol. 200, pp. 42-57
Closed Access | Times Cited: 20
The Hidden Role of Non-Canonical Amyloid β Isoforms in Alzheimer’s Disease
Lukas Busch, Simone Eggert, Kristina Endres, et al.
Cells (2022) Vol. 11, Iss. 21, pp. 3421-3421
Open Access | Times Cited: 10
Distinct Effects of Beta-Amyloid, Its Isomerized and Phosphorylated Forms on the Redox Status and Mitochondrial Functioning of the Blood–Brain Barrier Endothelium
Aleksandra Petrovskaya, Artem M. Tverskoi, Evgeny P. Barykin, et al.
International Journal of Molecular Sciences (2022) Vol. 24, Iss. 1, pp. 183-183
Open Access | Times Cited: 10
The Membrane Axis of Alzheimer's Nanomedicine
Yuhuan Li, Huayuan Tang, Nikolaos K. Andrikopoulos, et al.
Advanced NanoBiomed Research (2020) Vol. 1, Iss. 1
Open Access | Times Cited: 14
Synthetic, Cell-Derived, Brain-Derived, and Recombinant β-Amyloid: Modelling Alzheimer’s Disease for Research and Drug Development
Kseniya B. Varshavskaya, Vladimir A. Mitkevich, Alexander А. Makarov, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 23, pp. 15036-15036
Open Access | Times Cited: 8
Post-translational modifications of beta-amyloid alter its transport in the blood-brain barrier in vitro model
Kseniya B. Varshavskaya, Irina Yu. Petrushanko, Vladimir A. Mitkevich, et al.
Frontiers in Molecular Neuroscience (2024) Vol. 17
Open Access | Times Cited: 1
β-Amyloids and Immune Responses Associated with Alzheimer’s Disease
Elizaveta A Kolobova, Irina Yu. Petrushanko, Vladimir A. Mitkevich, et al.
Cells (2024) Vol. 13, Iss. 19, pp. 1624-1624
Open Access | Times Cited: 1
Beta-Amyloid and Its Asp7 Isoform: Morphological and Aggregation Properties and Effects of Intracerebroventricular Administration
Valeria Ushakova, Yana Zorkina, Olga Abramova, et al.
Brain Sciences (2024) Vol. 14, Iss. 10, pp. 1042-1042
Open Access | Times Cited: 1
N-Terminal Modified Aβ Variants Enable Modulations to the Structures and Cytotoxicity Levels of Wild-Type Aβ Fibrils through Cross-Seeding
Zhiwen Hu, Dan Fai Au, Letticia Cruceta, et al.
ACS Chemical Neuroscience (2020) Vol. 11, Iss. 14, pp. 2058-2065
Open Access | Times Cited: 11
The Dynamics of β-Amyloid Proteoforms Accumulation in the Brain of a 5xFAD Mouse Model of Alzheimer’s Disease
Anna E. Bugrova, Polina A. Strelnikova, Maria I. Indeykina, et al.
International Journal of Molecular Sciences (2021) Vol. 23, Iss. 1, pp. 27-27
Open Access | Times Cited: 10
Tetrapeptide Ac-HAEE-NH2 Protects α4β2 nAChR from Inhibition by Aβ
Evgeny P. Barykin, Aleksandra Garifulina, Anna P. Tolstova, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 17, pp. 6272-6272
Open Access | Times Cited: 10
Amyloid Beta Peptide (Aβ1-42) Reverses the Cholinergic Control of Monocytic IL-1β Release
Katrin Richter, Raymond Ogiemwonyi‐Schaefer, Sigrid Wilker, et al.
Journal of Clinical Medicine (2020) Vol. 9, Iss. 9, pp. 2887-2887
Open Access | Times Cited: 10
Interaction Interface of Aβ42 with Human Na,K-ATPase Studied by MD and ITC and Inhibitor Screening by MD
Alexei A. Adzhubei, Anna P. Tolstova, Maria A. Strelkova, et al.
Biomedicines (2022) Vol. 10, Iss. 7, pp. 1663-1663
Open Access | Times Cited: 6
Zn-dependent β-amyloid Aggregation and its Reversal by the Tetrapeptide HAEE
Vladimir A. Mitkevich, Evgeny P. Barykin, S. Yu. Eremina, et al.
Aging and Disease (2022)
Open Access | Times Cited: 6
Application of electrochemical method to a comparative study of spontaneous aggregation of amyloid-β isoforms
Elena V. Suprun, Sergey P. Radko, Sergey A. Kozin, et al.
Journal of Electroanalytical Chemistry (2020) Vol. 861, pp. 113938-113938
Closed Access | Times Cited: 8
β-amyloid’s neurotoxic mechanisms as defined by in vitro microelectrode arrays: a review
Aoife O'connell, Leo R. Quinlan, Andrea Kwakowsky
Pharmacological Research (2024) Vol. 209, pp. 107436-107436
Open Access
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