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:

Scorpion toxins interact with nicotinic acetylcholine receptors
Igor E. Kasheverov, Peter B. Oparin, М. Н. Жмак, et al.
FEBS Letters (2019) Vol. 593, Iss. 19, pp. 2779-2789
Open Access | Times Cited: 14

Showing 14 citing articles:

Nicotinic acetylcholine receptors in cancer: Limitations and prospects
Tanja Bele, Tom Turk, Igor Križaj
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2023) Vol. 1870, Iss. 1, pp. 166875-166875
Open Access | Times Cited: 12

A Taxon-Specific and High-Throughput Method for Measuring Ligand Binding to Nicotinic Acetylcholine Receptors
Christina N. Zdenek, Richard J. Harris, Sanjaya Kuruppu, et al.
Toxins (2019) Vol. 11, Iss. 10, pp. 600-600
Open Access | Times Cited: 35

Multi-targeting sodium and calcium channels using venom peptides for the treatment of complex ion channels-related diseases
Fernanda C. Cardoso
Biochemical Pharmacology (2020) Vol. 181, pp. 114107-114107
Closed Access | Times Cited: 29

α-Conotoxin RgIA and oligoarginine R8 in the mice model alleviate long-term oxaliplatin induced neuropathy
I. A. Dyachenko, Yu. A. Palikova, В. А. Паликов, et al.
Biochimie (2022) Vol. 194, pp. 127-136
Closed Access | Times Cited: 17

Advances in small molecule selective ligands for heteromeric nicotinic acetylcholine receptors
Carlo Matera, Claudio Papotto, Clelia Dallanoce, et al.
Pharmacological Research (2023) Vol. 194, pp. 106813-106813
Open Access | Times Cited: 10

Characterization of Sodium Channel Peptides Obtained from the Venom of the Scorpion Centruroides bonito
Rita Restano‐Cassulini, Timoteo Olamendi‐Portugal, Lidia Riaño‐Umbarila, et al.
Toxins (2024) Vol. 16, Iss. 3, pp. 125-125
Open Access | Times Cited: 3

Venom-Derived Neurotoxins Targeting Nicotinic Acetylcholine Receptors
Ayaulym Bekbossynova, Albina Zharylgap, Olena Filchakova
Molecules (2021) Vol. 26, Iss. 11, pp. 3373-3373
Open Access | Times Cited: 19

Venom-derived modulators of epilepsy-related ion channels
Chun Yuen Chow, Nathan L. Absalom, Kimberley A. Biggs, et al.
Biochemical Pharmacology (2020) Vol. 181, pp. 114043-114043
Open Access | Times Cited: 20

Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone Heteractis magnifica
Rimma Kalina, Igor E. Kasheverov, Sergey G. Koshelev, et al.
Toxins (2022) Vol. 14, Iss. 10, pp. 697-697
Open Access | Times Cited: 10

Peptides from the Sea Anemone Metridium senile with Modified Inhibitor Cystine Knot (ICK) Fold Inhibit Nicotinic Acetylcholine Receptors
Igor E. Kasheverov, Yulia A. Logashina, Fedor Kornilov, et al.
Toxins (2022) Vol. 15, Iss. 1, pp. 28-28
Open Access | Times Cited: 10

Effect of animal venom toxins on the main links of the homeostasis of mammals (Review)
Ruzhena Matkivska, Inha Samborska, Oleksandr Maievskyi
Biomedical Reports (2023) Vol. 20, Iss. 2
Open Access | Times Cited: 5

Complex approach for analysis of snake venom α-neurotoxins binding to HAP, the high-affinity peptide
Denis S. Kudryavtsev, Valentin М. Tabakmakher, Gleb S. Budylin, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 13

Fifty Years of Animal Toxin Research at the Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry RAS
Victor I. Tsetlin, Irina Shelukhina, Sergey A. Kozlov, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 18, pp. 13884-13884
Open Access | Times Cited: 2

Artificial pore blocker acts specifically on voltage-gated potassium channel isoform KV1.6
Andrei M. Gigolaev, Владислав А. Лушпа, Ernesto Lopes Pinheiro-Júnior, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 11, pp. 102467-102467
Open Access | Times Cited: 3

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