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:

Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
Arvind Kumar, Sandip Basak, Shanlin Rao, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 95

Showing 1-25 of 95 citing articles:

Structure and gating mechanism of the α7 nicotinic acetylcholine receptor
Colleen Noviello, Anant Gharpure, Nuriya Mukhtasimova, et al.
Cell (2021) Vol. 184, Iss. 8, pp. 2121-2134.e13
Open Access | Times Cited: 207

Understanding the invisible hands of sample preparation for cryo-EM
Giulia Weissenberger, René Henderikx, Peter J. Peters
Nature Methods (2021) Vol. 18, Iss. 5, pp. 463-471
Open Access | Times Cited: 135

Mechanism of gating and partial agonist action in the glycine receptor
Jie Yu, Hongtao Zhu, Remigijus Lapė, et al.
Cell (2021) Vol. 184, Iss. 4, pp. 957-968.e21
Open Access | Times Cited: 115

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

Direct Structural Insights into GABAA Receptor Pharmacology
Jeong Joo Kim, Ryan Hibbs
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 6, pp. 502-517
Open Access | Times Cited: 95

Architecture and assembly mechanism of native glycine receptors
Hongtao Zhu, Eric Gouaux
Nature (2021) Vol. 599, Iss. 7885, pp. 513-517
Open Access | Times Cited: 64

Conformational transitions and ligand-binding to a muscle-type nicotinic acetylcholine receptor
Eleftherios Zarkadas, Eva Pebay‐Peyroula, Mackenzie J. Thompson, et al.
Neuron (2022) Vol. 110, Iss. 8, pp. 1358-1370.e5
Open Access | Times Cited: 62

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

Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins
Saman Majeed, Akram Ahmad, Ujala Sehar, et al.
Membranes (2021) Vol. 11, Iss. 9, pp. 685-685
Open Access | Times Cited: 56

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

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

Characterization of the subunit composition and structure of adult human glycine receptors
Hailong Yu, Xiao‐chen Bai, Weiwei Wang
Neuron (2021) Vol. 109, Iss. 17, pp. 2707-2716.e6
Open Access | Times Cited: 47

Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM
Sarah Piper, Rachel M. Johnson, Denise Wootten, et al.
Chemical Reviews (2022) Vol. 122, Iss. 17, pp. 13989-14017
Open Access | Times Cited: 33

Tuning phenylalanine fluorination to assess aromatic contributions to protein function and stability in cells
Grace D. Galles, Daniel T. Infield, Colin J. Clark, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 20

Using a Dynamic Hydrophilization Strategy to Achieve Nanodispersion, Full Wetting, and Precise Delivery of Hydrophobic Pesticide
Kefei Zhao, Guangchun Xu, Leng Wang, et al.
ACS Applied Materials & Interfaces (2023) Vol. 15, Iss. 30, pp. 37093-37106
Closed Access | Times Cited: 17

Structural basis for partial agonism in 5-HT3A receptors
Kevin Felt, Madeleine Stauffer, Leslie Salas-Estrada, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 4, pp. 598-609
Closed Access | Times Cited: 6

Elephants in the Dark: Insights and Incongruities in Pentameric Ligand-gated Ion Channel Models
Rebecca J. Howard
Journal of Molecular Biology (2021) Vol. 433, Iss. 17, pp. 167128-167128
Open Access | Times Cited: 40

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

Structure and dynamics of differential ligand binding in the human ρ-type GABAA receptor
John Cowgill, Chen Fan, Nandan Haloi, et al.
Neuron (2023) Vol. 111, Iss. 21, pp. 3450-3464.e5
Open Access | Times Cited: 16

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

The desensitization pathway of GABAA receptors, one subunit at a time
Marc Gielen, Nathalie Barilone, Pierre‐Jean Corringer
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 37

Cyclodextrins increase membrane tension and are universal activators of mechanosensitive channels
Charles D. Cox, Yixiao Zhang, Zijing Zhou, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 36
Open Access | Times Cited: 31

Molecular Simulations of Hydrophobic Gating of Pentameric Ligand Gated Ion Channels: Insights into Water and Ions
Shanlin Rao, Gianni Klesse, Charlotte I. Lynch, et al.
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 4, pp. 981-994
Open Access | Times Cited: 28

Druggable Lipid Binding Sites in Pentameric Ligand-Gated Ion Channels and Transient Receptor Potential Channels
Wayland W.L. Cheng, Mark J. Arcario, John T. Petroff
Frontiers in Physiology (2022) Vol. 12
Open Access | Times Cited: 19

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