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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:

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

Showing 23 citing articles:

Bibliometric Review of the Literature on Cone Snail Peptide Toxins from 2000 to 2022
Linh T. T. Nguyen, David J. Craik, Quentin Kaas
Marine Drugs (2023) Vol. 21, Iss. 3, pp. 154-154
Open Access | Times Cited: 14
Advances in Biosensors for the Rapid Detection of Marine Biotoxins: Current Status and Future Perspectives
Xiangwei Zhu, Yufa Zhao, Long Wu, et al.
Biosensors (2024) Vol. 14, Iss. 4, pp. 203-203
Open Access | Times Cited: 5
Selective Inhibition of Rat α7 Nicotinic Acetylcholine Receptors by LvID, a Newly Characterized α4/7-Conotoxin from Conus lividus
Man Guo, Xiaopeng Zhu, Tao Ma, et al.
Journal of Medicinal Chemistry (2025)
Closed Access
Structural and Functional Analyses of Cone Snail Toxins
Harry Morales Duque, Simoni Campos Dias, Octávio Luiz Franco
Marine Drugs (2019) Vol. 17, Iss. 6, pp. 370-370
Open Access | Times Cited: 31
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
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
Historical Perspective of the Characterization of Conotoxins Targeting Voltage-Gated Sodium Channels
James R. Groome
Marine Drugs (2023) Vol. 21, Iss. 4, pp. 209-209
Open Access | Times Cited: 7
Rational Design of α-Conotoxin RegIIA Analogues Selectively Inhibiting the Human α3β2 Nicotinic Acetylcholine Receptor through Computational Scanning
Qingliang Xu, Han‐Shen Tae, Zihao Wang, et al.
ACS Chemical Neuroscience (2020) Vol. 11, Iss. 18, pp. 2804-2811
Closed Access | Times Cited: 19
PeIA-5466: A Novel Peptide Antagonist Containing Non-natural Amino Acids That Selectively Targets α3β2 Nicotinic Acetylcholine Receptors
Arik J. Hone, F. Fisher, Sean Christensen, et al.
Journal of Medicinal Chemistry (2019) Vol. 62, Iss. 13, pp. 6262-6275
Open Access | Times Cited: 18
Structure-Function Elucidation of a New α-Conotoxin, MilIA, from Conus milneedwardsi
Steve Peigneur, Prabha Devi, Andrea Seldeslachts, et al.
Marine Drugs (2019) Vol. 17, Iss. 9, pp. 535-535
Open Access | Times Cited: 14
Characterisation of Elevenin-Vc1 from the Venom of Conus victoriae: A Structural Analogue of α-Conotoxins
Bankala Krishnarjuna, Punnepalli Sunanda, Jeffrey Seow, et al.
Marine Drugs (2023) Vol. 21, Iss. 2, pp. 81-81
Open Access | Times Cited: 4
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
In Silico Modeling of the α7 Nicotinic Acetylcholine Receptor: New Pharmacological Challenges Associated with Multiple Modes of Signaling
Alican Gulsevin, Roger L. Papke, Nicole A. Horenstein
Mini-Reviews in Medicinal Chemistry (2020) Vol. 20, Iss. 10, pp. 841-864
Open Access | Times Cited: 8
Structural and Functional Characterization of Conotoxins from Conus achatinus Targeting NMDAR
Xiujie Liu, Ge Yao, Kang Wang, et al.
Marine Drugs (2020) Vol. 18, Iss. 3, pp. 135-135
Open Access | Times Cited: 8
Targeting Alpha7 Nicotinic Acetylcholine Receptors in Lung Cancer: Insights, Challenges, and Therapeutic Strategies
Kuntarat Arunrungvichian, Opa Vajragupta, Yoshihiro Hayakawa, et al.
ACS Pharmacology & Translational Science (2023)
Closed Access | Times Cited: 2
Characterization of an α 4/7-Conotoxin LvIF from Conus lividus That Selectively Blocks α3β2 Nicotinic Acetylcholine Receptor
Man Guo, Jinpeng Yu, Xiaopeng Zhu, et al.
Marine Drugs (2021) Vol. 19, Iss. 7, pp. 398-398
Open Access | Times Cited: 5
Synthesis and characterization of αM-conotoxin SIIID, a reversible human α7 nicotinic acetylcholine receptor antagonist
Hongxing Wang, Yubin Li, Manyi Yang, et al.
Toxicon (2022) Vol. 210, pp. 141-147
Closed Access | Times Cited: 3
Single Amino Acid Substitution in Loop1 Switches the Selectivity of α-Conotoxin RegIIA towards the α7 Nicotinic Acetylcholine Receptor
Jinpeng Yu, Junjie Xie, Yuting Ma, et al.
Marine Drugs (2024) Vol. 22, Iss. 9, pp. 390-390
Open Access
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
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
Marine-derived nicotinic receptor antagonist toxins: Pinnatoxins and alpha conotoxins
Shane D. Hellyer
Advances in neurotoxicology (2021), pp. 105-191
Closed Access | Times Cited: 2
The 3/4- and 3/6-Subfamily Variants of α-Conotoxins GI and MI Exhibit Potent Inhibitory Activity against Muscular Nicotinic Acetylcholine Receptors
Xiaoli Ma, Qiuyuan Huang, Shuo Yu, et al.
Marine Drugs (2021) Vol. 19, Iss. 12, pp. 705-705
Open Access | Times Cited: 2
Toxinology of Marine Venomous Snails
Gholam Hossein Mohebbi, Iraj Nabipour
Iranian South Medical Journal (2021) Vol. 24, Iss. 5, pp. 505-581
Open Access
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