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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:

Identification of a Conformational Equilibrium That Determines the Efficacy and Functional Selectivity of the μ‐Opioid Receptor
Junya Okude, Takumi Ueda, Yutaka Kofuku, et al.
Angewandte Chemie International Edition (2015) Vol. 54, Iss. 52, pp. 15771-15776
Open Access | Times Cited: 125

Showing 1-25 of 125 citing articles:

Structure and dynamics of GPCR signaling complexes
Daniel Hilger, Matthieu Masureel, Brian K. Kobilka
Nature Structural & Molecular Biology (2017) Vol. 25, Iss. 1, pp. 4-12
Open Access | Times Cited: 796
Structure of the µ-opioid receptor–Gi protein complex
Antoine Koehl, Hongli Hu, Shoji Maeda, et al.
Nature (2018) Vol. 558, Iss. 7711, pp. 547-552
Open Access | Times Cited: 613
Nanodiscs in Membrane Biochemistry and Biophysics
Ilia G. Denisov, Stephen G. Sligar
Chemical Reviews (2017) Vol. 117, Iss. 6, pp. 4669-4713
Open Access | Times Cited: 446
Angiotensin Analogs with Divergent Bias Stabilize Distinct Receptor Conformations
Laura M. Wingler, Matthias Elgeti, Daniel Hilger, et al.
Cell (2019) Vol. 176, Iss. 3, pp. 468-478.e11
Open Access | Times Cited: 251
GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures
Ichio Shimada, Takumi Ueda, Yutaka Kofuku, et al.
Nature Reviews Drug Discovery (2018) Vol. 18, Iss. 1, pp. 59-82
Open Access | Times Cited: 218
Allosteric Coupling of Drug Binding and Intracellular Signaling in the A2A Adenosine Receptor
Matthew T. Eddy, Ming-Yue Lee, Zhan‐Guo Gao, et al.
Cell (2017) Vol. 172, Iss. 1-2, pp. 68-80.e12
Open Access | Times Cited: 193
Conformational Basis of G Protein-Coupled Receptor Signaling Versatility
Laura M. Wingler, Robert J. Lefkowitz
Trends in Cell Biology (2020) Vol. 30, Iss. 9, pp. 736-747
Open Access | Times Cited: 192
Structural Basis for G Protein-Coupled Receptor Activation
Aashish Manglik, Andrew C. Kruse
Biochemistry (2017) Vol. 56, Iss. 42, pp. 5628-5634
Open Access | Times Cited: 174
G Protein-Coupled Receptors: A Century of Research and Discovery
Samuel Liu, Preston J. Anderson, Sudarshan Rajagopal, et al.
Circulation Research (2024) Vol. 135, Iss. 1, pp. 174-197
Closed Access | Times Cited: 32
Ligand efficacy modulates conformational dynamics of the µ-opioid receptor
Jiawei Zhao, Matthias Elgeti, Evan S. O’Brien, et al.
Nature (2024) Vol. 629, Iss. 8011, pp. 474-480
Open Access | Times Cited: 18
Molecular Basis of Oxytocin Receptor Signalling in the Brain: What We Know and What We Need to Know
Marta Busnelli, Bice Chini
Current topics in behavioral neurosciences (2017), pp. 3-29
Closed Access | Times Cited: 130
Structural insights into differences in G protein activation by family A and family B GPCRs
Daniel Hilger, Kaavya Krishna Kumar, Hongli Hu, et al.
Science (2020) Vol. 369, Iss. 6503
Open Access | Times Cited: 128
Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems
Stefan Schütz, Remco Sprangers
Progress in Nuclear Magnetic Resonance Spectroscopy (2019) Vol. 116, pp. 56-84
Open Access | Times Cited: 126
Insight into partial agonism by observing multiple equilibria for ligand-bound and Gs-mimetic nanobody-bound β1-adrenergic receptor
Andras Solt, Mark J. Bostock, Binesh Shrestha, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 102
The role of structural dynamics in GPCR‐mediated signaling
Daniel Hilger
FEBS Journal (2021) Vol. 288, Iss. 8, pp. 2461-2489
Open Access | Times Cited: 80
G protein-coupled receptor-G protein interactions: a single-molecule perspective
Davide Calebiro, Zsombor Kőszegi, Yann Lanoiselée, et al.
Physiological Reviews (2020) Vol. 101, Iss. 3, pp. 857-906
Open Access | Times Cited: 79
Conformational Complexity and Dynamics in a Muscarinic Receptor Revealed by NMR Spectroscopy
Jun Xu, Yunfei Hu, Jonas Kaindl, et al.
Molecular Cell (2019) Vol. 75, Iss. 1, pp. 53-65.e7
Open Access | Times Cited: 78
Structural basis of sphingosine-1-phosphate receptor 1 activation and biased agonism
Zhenmei Xu, Tatsuya Ikuta, Kouki Kawakami, et al.
Nature Chemical Biology (2021) Vol. 18, Iss. 3, pp. 281-288
Closed Access | Times Cited: 68
Molecular insights into the biased signaling mechanism of the μ-opioid receptor
Xiaojing Cong, Damien Maurel, Hélène Déméné, et al.
Molecular Cell (2021) Vol. 81, Iss. 20, pp. 4165-4175.e6
Open Access | Times Cited: 60
Allosteric coupling and biased agonism in G protein‐coupled receptors
Andreas Böck, Marcel Bermúdez
FEBS Journal (2021) Vol. 288, Iss. 8, pp. 2513-2528
Open Access | Times Cited: 58
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: 27
Structural and dynamic insights into the activation of the μ-opioid receptor by an allosteric modulator
Shun Kaneko, Shunsuke Imai, Tomomi Uchikubo‐Kamo, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 8
Ligand modulation of sidechain dynamics in a wild-type human GPCR
Lindsay Clark, Igor Dikiy, Karen Chapman, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 83
Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
Yutaro Shiraishi, Mei Natsume, Yutaka Kofuku, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 72
Production of isotope-labeled proteins in insect cells for NMR
Bastian Franke, Christian Opitz, Shin Isogai, et al.
Journal of Biomolecular NMR (2018) Vol. 71, Iss. 3, pp. 173-184
Open Access | Times Cited: 60
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