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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-Affinity α-Conotoxin PnIA Analogs Designed on the Basis of the Protein Surface Topography Method
Igor E. Kasheverov, Anton O. Chugunov, Denis S. Kudryavtsev, et al.
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 26

Showing 1-25 of 26 citing articles:

Nicotinic acetylcholine receptor inhibitors derived from snake and snail venoms
Sébastien Dutertre, Annette Nicke, Victor I. Tsetlin
Neuropharmacology (2017) Vol. 127, pp. 196-223
Closed Access | Times Cited: 70
α7- and α9-Containing Nicotinic Acetylcholine Receptors in the Functioning of Immune System and in Pain
Irina Shelukhina, Andrei E. Siniavin, Igor E. Kasheverov, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 7, pp. 6524-6524
Open Access | Times Cited: 18
Discovery of peptide ligands through docking and virtual screening at nicotinic acetylcholine receptor homology models
Abba E. Leffler, Alexander Kuryatov, Henry Zebroski, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 38
Open Access | Times Cited: 60
High Selectivity of an α-Conotoxin LvIA Analogue for α3β2 Nicotinic Acetylcholine Receptors Is Mediated by β2 Functionally Important Residues
Xiaopeng Zhu, Si Pan, Man‐Yu Xu, et al.
Journal of Medicinal Chemistry (2020) Vol. 63, Iss. 22, pp. 13656-13668
Closed Access | Times Cited: 28
Snails In Silico: A Review of Computational Studies on the Conopeptides
Rachael A. Mansbach, Timothy Travers, Benjamin H. McMahon, et al.
Marine Drugs (2019) Vol. 17, Iss. 3, pp. 145-145
Open Access | Times Cited: 25
Mutagenesis of α-Conotoxins for Enhancing Activity and Selectivity for Nicotinic Acetylcholine Receptors
Matthew Turner, Leanna A. Marquart, Paul D. Phillips, et al.
Toxins (2019) Vol. 11, Iss. 2, pp. 113-113
Open Access | Times Cited: 23
Novel long-chain neurotoxins from Bungarus candidus distinguish the two binding sites in muscle-type nicotinic acetylcholine receptors
Yuri N. Utkin, Ulrich Kuch, Igor E. Kasheverov, et al.
Biochemical Journal (2019) Vol. 476, Iss. 8, pp. 1285-1302
Open Access | Times Cited: 21
Oligoarginine Peptides, a New Family of Nicotinic Acetylcholine Receptor Inhibitors
Д. С. Лебедев, Elena V. Kryukova, Igor A. Ivanov, et al.
Molecular Pharmacology (2019) Vol. 96, Iss. 5, pp. 664-673
Open Access | Times Cited: 20
Fluorescent α-Conotoxin [Q1G, ΔR14]LvIB Identifies the Distribution of α7 Nicotinic Acetylcholine Receptor in the Rat Brain
Hongyu Shan, Nan Wang, Xinyu Gao, et al.
Marine Drugs (2024) Vol. 22, Iss. 5, pp. 200-200
Open Access | Times Cited: 2
Labelled animal toxins as selective molecular markers of ion channels: Applications in neurobiology and beyond
Alexey I. Kuzmenkov, Alexander A. Vassilevski
Neuroscience Letters (2017) Vol. 679, pp. 15-23
Closed Access | Times Cited: 20
Orthosteric and/or Allosteric Binding of α-Conotoxins to Nicotinic Acetylcholine Receptors and Their Models
Elena V. Kryukova, Igor A. Ivanov, Д. С. Лебедев, et al.
Marine Drugs (2018) Vol. 16, Iss. 12, pp. 460-460
Open Access | Times Cited: 18
Modelling the interactions between animal venom peptides and membrane proteins
Andrew Hung, Serdar Kuyucak, Christina I. Schroeder, et al.
Neuropharmacology (2017) Vol. 127, pp. 20-31
Closed Access | Times Cited: 16
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
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
Effects of C-Terminal Carboxylation on α-Conotoxin LsIA Interactions with Human α7 Nicotinic Acetylcholine Receptor: Molecular Simulation Studies
Jierong Wen, Andrew Hung
Marine Drugs (2019) Vol. 17, Iss. 4, pp. 206-206
Open Access | Times Cited: 8
Qualitative Assay to Detect Dopamine Release by Ligand Action on Nicotinic Acetylcholine Receptors
Leanna A. Marquart, Matthew Turner, Owen M. McDougal
Toxins (2019) Vol. 11, Iss. 12, pp. 682-682
Open Access | Times Cited: 8
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
Graph-Directed Approach for Downselecting Toxins for Experimental Structure Determination
Rachael A. Mansbach, Srirupa Chakraborty, Timothy Travers, et al.
Marine Drugs (2020) Vol. 18, Iss. 5, pp. 256-256
Open Access | Times Cited: 5
Potassium channel blocker crafted by α-hairpinin scaffold engineering
Valentin М. Tabakmakher, Andrei M. Gigolaev, Steve Peigneur, et al.
Biophysical Journal (2021) Vol. 120, Iss. 12, pp. 2471-2481
Open Access | Times Cited: 5
Posttranslational modifications of α-conotoxins: sulfotyrosine and C-terminal amidation stabilise structures and increase acetylcholine receptor binding
Thao N. T. Ho, Han Siean Lee, Shilpa Swaminathan, et al.
RSC Medicinal Chemistry (2021) Vol. 12, Iss. 9, pp. 1574-1584
Open Access | Times Cited: 5
In Silico Conotoxin Studies: Progress and Prospects
Ruihan Li, Md. Mahadhi Hasan, Dan Wang
Molecules (2024) Vol. 29, Iss. 24, pp. 6061-6061
Open Access
From Peptides to Receptors
Victor I. Tsetlin
Russian Journal of Bioorganic Chemistry (2023) Vol. 49, Iss. 3, pp. 417-421
Open Access | Times Cited: 1
From Peptides to Receptors
Victor I. Tsetlin
Биоорганическая химия (2023) Vol. 49, Iss. 3, pp. 224-228
Closed Access | Times Cited: 1
Polyarginine Peptides As a New Class of Ligands of Nicotinic Acetylcholine Receptors
Elena V. Kryukova, Igor A. Ivanov, Д. С. Лебедев, et al.
Doklady Biochemistry and Biophysics (2018) Vol. 483, Iss. 1, pp. 313-315
Closed Access | Times Cited: 2
Ribbon α-Conotoxin KTM Exhibits Potent Inhibition of Nicotinic Acetylcholine Receptors
Leanna A. Marquart, Matthew Turner, Lisa Warner, et al.
Marine Drugs (2019) Vol. 17, Iss. 12, pp. 669-669
Open Access | Times Cited: 2
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