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:

Structural mechanism of muscle nicotinic receptor desensitization and block by curare
MD Rahman, Tamara Basta, Jinfeng Teng, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 4, pp. 386-394
Open Access | Times Cited: 62

Showing 1-25 of 62 citing articles:

Clinical and Pathologic Features of Congenital Myasthenic Syndromes Caused by 35 Genes—A Comprehensive Review
Kinji Ohno, Bisei Ohkawara, Xin‐Ming Shen, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 4, pp. 3730-3730
Open Access | Times Cited: 66

Lipid nanodisc scaffold and size alter the structure of a pentameric ligand-gated ion channel
Vikram L. Dalal, Mark J. Arcario, John T. Petroff, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 34

Structural mechanisms of α7 nicotinic receptor allosteric modulation and activation
Sean M. Burke, Mariia Avstrikova, Colleen Noviello, et al.
Cell (2024) Vol. 187, Iss. 5, pp. 1160-1176.e21
Open Access | Times Cited: 17

Structural insights into opposing actions of neurosteroids on GABAA receptors
Dagimhiwat Legesse, Chen Fan, Jinfeng Teng, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 41

Recent advances in membrane mimetics for membrane protein research
John William Young
Biochemical Society Transactions (2023) Vol. 51, Iss. 3, pp. 1405-1416
Open Access | Times Cited: 27

Conformational transitions and allosteric modulation in a heteromeric glycine receptor
Eric Gibbs, Emily Klemm, David Seiferth, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 24

The Nicotinic Acetylcholine Receptor and Its Pentameric Homologs: Toward an Allosteric Mechanism of Signal Transduction at the Atomic Level
Marco Cecchini, Pierre‐Jean Corringer, Jean‐Pierre Changeux
Annual Review of Biochemistry (2024) Vol. 93, Iss. 1, pp. 339-366
Closed Access | Times Cited: 9

A release of local subunit conformational heterogeneity underlies gating in a muscle nicotinic acetylcholine receptor
Mackenzie J. Thompson, Farid Mansoub Bekarkhanechi, Anna Ananchenko, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 9

Structural basis of sensory receptor evolution in octopus
Corey AH Allard, Guipeun Kang, Jeong Joo Kim, et al.
Nature (2023) Vol. 616, Iss. 7956, pp. 373-377
Closed Access | Times Cited: 22

Structural switch in acetylcholine receptors in developing muscle
Huanhuan Li, Jinfeng Teng, Ryan Hibbs
Nature (2024) Vol. 632, Iss. 8027, pp. 1174-1180
Closed Access | Times Cited: 7

Modulation of a rapid neurotransmitter receptor-ion channel by membrane lipids
Francisco J. Barrantes
Frontiers in Cell and Developmental Biology (2024) Vol. 11
Open Access | Times Cited: 6

Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation
John T. Petroff, Noah M. Dietzen, Ezry Santiago-McRae, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 27

Advances of computer-aided drug design (CADD) in the development of anti-Azheimer’s-disease drugs
Yuzhen Niu, Ping Lin
Drug Discovery Today (2023) Vol. 28, Iss. 8, pp. 103665-103665
Closed Access | Times Cited: 16

Structure and function meet at the nicotinic acetylcholine receptor-lipid interface
Francisco J. Barrantes
Pharmacological Research (2023) Vol. 190, pp. 106729-106729
Open Access | Times Cited: 15

Cryo-EM structures of prokaryotic ligand-gated ion channel GLIC provide insights into gating in a lipid environment
Nikhil Bharambe, Zhuowen Li, David Seiferth, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5

Influence of lipid bilayer on the structure of the muscle-type nicotinic acetylcholine receptor
Nigel Unwin
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 19
Open Access | Times Cited: 5

Illumination of a progressive allosteric mechanism mediating the glycine receptor activation
Sophie Shi, S. Lefebvre, Laurie Peverini, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 12

The modes of action of ion-channel-targeting neurotoxic insecticides: lessons from structural biology
Tobias Raisch, Stefan Raunser
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 10, pp. 1411-1427
Closed Access | Times Cited: 12

In silico approaches for developing sesquiterpene derivatives as antagonists of human nicotinic acetylcholine receptors (nAChRs) for nicotine addiction treatment
Taufik Muhammad Fakih, Aden Dhana Rizkita, Sintia Ayu Dewi, et al.
Current Research in Structural Biology (2025) Vol. 9, pp. 100162-100162
Closed Access

Structural insights into the activation mechanism of the human zinc-activated channel
Xuhang Lu, Dongmei Li, Yaojie Wang, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Identification of Bioactive Metabolites of Capirona macrophylla by Metabolomic Analysis, Molecular Docking, and In Vitro Antiparasitic Assays
Joseph Albert Medeiros Evaristo, Estella Aparecida De Laia, Bruna de Souza Tavares, et al.
Metabolites (2025) Vol. 15, Iss. 3, pp. 157-157
Open Access

Deterministic principles underlying nicotinic receptor protein function
Ewa Nurowska, Krzysztof A. Meissner
International Journal of Biological Macromolecules (2025), pp. 142769-142769
Closed Access

Structures of the human adult muscle-type nicotinic receptor in resting and desensitized states
Anna Li, A.C.W. Pike, Richard Webster, et al.
Cell Reports (2025) Vol. 44, Iss. 5, pp. 115581-115581
Closed Access

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