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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:

Cryo-EM structure of an activated GPCR–G protein complex in lipid nanodiscs
Meng Zhang, Miao Gui, Zifu Wang, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 3, pp. 258-267
Open Access | Times Cited: 93

Showing 1-25 of 93 citing articles:

Protein Design: From the Aspect of Water Solubility and Stability
Rui Qing, Shilei Hao, Eva Smorodina, et al.
Chemical Reviews (2022) Vol. 122, Iss. 18, pp. 14085-14179
Open Access | Times Cited: 148
Time-resolved cryo-EM of G-protein activation by a GPCR
Makaía M. Papasergi-Scott, Guillermo Pérez‐Hernández, Hossein Batebi, et al.
Nature (2024) Vol. 629, Iss. 8014, pp. 1182-1191
Open Access | Times Cited: 43
Structure-based design of non-hypertrophic apelin receptor modulator
Weiwei Wang, Su‐Yu Ji, W. Zhang, et al.
Cell (2024) Vol. 187, Iss. 6, pp. 1460-1475.e20
Closed Access | Times Cited: 17
Capturing a rhodopsin receptor signalling cascade across a native membrane
Siyun Chen, Tamar Getter, David Salom, et al.
Nature (2022) Vol. 604, Iss. 7905, pp. 384-390
Open Access | Times Cited: 57
Lipid–Protein Interactions in Plasma Membrane Organization and Function
Taras Sych, Kandice R. Levental, Erdinç Sezgin
Annual Review of Biophysics (2022) Vol. 51, Iss. 1, pp. 135-156
Open Access | Times Cited: 46
Structural basis of neuropeptide Y signaling through Y1 receptor
Chaehee Park, Jinuk Kim, Seung-Bum Ko, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 42
Dynamic spatiotemporal determinants modulate GPCR:G protein coupling selectivity and promiscuity
Manbir Sandhu, Aaron Cho, Ning Ma, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 41
Structural and dynamic insights into supra-physiological activation and allosteric modulation of a muscarinic acetylcholine receptor
Jun Xu, Qinggong Wang, Harald Hübner, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 28
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
Molecular architecture of the Gαi-bound TRPC5 ion channel
Jongdae Won, Jinsung Kim, Hyeongseop Jeong, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 23
Role of Protonation States in the Stability of Molecular Dynamics Simulations of High-Resolution Membrane Protein Structures
Jonathan Lasham, Amina Djurabekova, Volker Zickermann, et al.
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 10, pp. 2304-2316
Open Access | Times Cited: 9
Structure and Dynamics of GPCRs in Lipid Membranes: Physical Principles and Experimental Approaches
Andrew J. Y. Jones, Florian Gabriel, Aditi Tandale, et al.
Molecules (2020) Vol. 25, Iss. 20, pp. 4729-4729
Open Access | Times Cited: 55
Membrane protein production and formulation for drug discovery
Ellen Gulezian, Christina Crivello, Janna Bednenko, et al.
Trends in Pharmacological Sciences (2021) Vol. 42, Iss. 8, pp. 657-674
Closed Access | Times Cited: 47
Angiotensin II receptor type 1 – An update on structure, expression and pathology
Robert Eckenstaler, Jana Sandori, Michael Gekle, et al.
Biochemical Pharmacology (2021) Vol. 192, pp. 114673-114673
Closed Access | Times Cited: 46
Lipid Nanodiscs for High-Resolution NMR Studies of Membrane Proteins
Umut Günsel, Franz Hagn
Chemical Reviews (2021) Vol. 122, Iss. 10, pp. 9395-9421
Closed Access | Times Cited: 44
Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment
Bankala Krishnarjuna, Ayyalusamy Ramamoorthy
Biomolecules (2022) Vol. 12, Iss. 8, pp. 1076-1076
Open Access | Times Cited: 36
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
Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering
Willem J. de Grip, Srividya Ganapathy
Frontiers in Chemistry (2022) Vol. 10
Open Access | Times Cited: 28
Allosteric modulation of ghrelin receptor signaling by lipids
Marjorie Damian, Maxime Louet, Antoniel Augusto Severo Gomes, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 38
Time-resolved cryo-EM of G protein activation by a GPCR
Makaía M. Papasergi-Scott, Guillermo Pérez‐Hernández, Hossein Batebi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 13
Mapping the conformational landscape of the stimulatory heterotrimeric G protein
Shuya Kate Huang, Louis-Philippe Picard, Rima Rahmatullah, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 4, pp. 502-511
Closed Access | Times Cited: 13
Cryo-EM structure of cell-free synthesized human histamine 2 receptor/Gs complex in nanodisc environment
Zoe Köck, Kilian Schnelle, Margherita Persechino, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Selective targeting of ligand-dependent and -independent signaling by GPCR conformation-specific anti-US28 intrabodies
Timo W. M. De Groof, Nick D. Bergkamp, Raimond Heukers, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 30
Tissue-specific mechanisms of fat metabolism that focus on insulin actions
Shusong Wu, Jijun Tan, Hongfu Zhang, et al.
Journal of Advanced Research (2022) Vol. 53, pp. 187-198
Open Access | Times Cited: 19
How Ligands Achieve Biased Signaling toward Arrestins
Qianru Jiang, Tao Che
Biochemistry (2025)
Closed Access
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