OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Activation of the A2A adenosine G-protein-coupled receptor by conformational selection
Libin Ye, Ned Van Eps, Marco Zimmer, et al.
Nature (2016) Vol. 533, Iss. 7602, pp. 265-268
Closed Access | Times Cited: 344

Showing 1-25 of 344 citing articles:

The Molecular Basis of G Protein–Coupled Receptor Activation
William I. Weis, Brian K. Kobilka
Annual Review of Biochemistry (2018) Vol. 87, Iss. 1, pp. 897-919
Open Access | Times Cited: 983

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: 797

GPCR Dynamics: Structures in Motion
Naomi R. Latorraca, AJ Venkatakrishnan, Ron O. Dror
Chemical Reviews (2016) Vol. 117, Iss. 1, pp. 139-155
Open Access | Times Cited: 677

Pharmacology of Adenosine Receptors: The State of the Art
Pier Andrea Borea, Stefania Gessi, Stefania Merighi, et al.
Physiological Reviews (2018) Vol. 98, Iss. 3, pp. 1591-1625
Open Access | Times Cited: 621

Common activation mechanism of class A GPCRs
Qingtong Zhou, Dehua Yang, Meng Wu, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 526

Structure of the adenosine A2A receptor bound to an engineered G protein
Byron Carpenter, Rony Nehmé, Tony Warne, et al.
Nature (2016) Vol. 536, Iss. 7614, pp. 104-107
Open Access | Times Cited: 426

Structural insights into G-protein-coupled receptor allostery
David M. Thal, Alisa Glukhova, Patrick M. Sexton, et al.
Nature (2018) Vol. 559, Iss. 7712, pp. 45-53
Closed Access | Times Cited: 303

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

A nontoxic pain killer designed by modeling of pathological receptor conformations
Viola Spahn, Giovanna Del Vecchio, Dominika Łabuz, et al.
Science (2017) Vol. 355, Iss. 6328, pp. 966-969
Closed Access | Times Cited: 209

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

The role of dimer asymmetry and protomer dynamics in enzyme catalysis
Tae Hun Kim, P. Mehrabi, Zhong Ren, et al.
Science (2017) Vol. 355, Iss. 6322
Closed Access | Times Cited: 187

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

Activation pathway of a G protein-coupled receptor uncovers conformational intermediates as targets for allosteric drug design
Shaoyong Lu, Xinheng He, Zhao Yang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 166

Lipid-Dependent Regulation of Ion Channels and G Protein–Coupled Receptors: Insights from Structures and Simulations
Anna L. Duncan, Wanling Song, Mark S.P. Sansom
The Annual Review of Pharmacology and Toxicology (2019) Vol. 60, Iss. 1, pp. 31-50
Open Access | Times Cited: 147

Delineating the conformational landscape of the adenosine A2A receptor during G protein coupling
Shuya Kate Huang, Aditya Pandey, Duy Phuoc Tran, et al.
Cell (2021) Vol. 184, Iss. 7, pp. 1884-1894.e14
Open Access | Times Cited: 127

In-Cell Structural Biology by NMR: The Benefits of the Atomic Scale
François‐Xavier Theillet
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9497-9570
Open Access | Times Cited: 80

Anionic phospholipids control mechanisms of GPCR-G protein recognition
Naveen Thakur, Arka Prabha Ray, Liam Sharp, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 55

Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery
Paolo Conflitti, Edward Lyman, Mark S.P. Sansom, et al.
Nature Reviews Drug Discovery (2025)
Closed Access | Times Cited: 2

Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations
Libin Ye, Chris Neale, Adnan Sljoka, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 147

Structural Basis for G Protein–Coupled Receptor Signaling
Sarah C. Erlandson, Conor McMahon, Andrew C. Kruse
Annual Review of Biophysics (2018) Vol. 47, Iss. 1, pp. 1-18
Open Access | Times Cited: 131

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

An online resource for GPCR structure determination and analysis
Christian Munk, Eshita Mutt, Vignir Ísberg, et al.
Nature Methods (2019) Vol. 16, Iss. 2, pp. 151-162
Open Access | Times Cited: 126

Selective Radical Trifluoromethylation of Native Residues in Proteins
Mateusz Imiołek, Gogulan Karunanithy, Wai‐Lung Ng, et al.
Journal of the American Chemical Society (2018) Vol. 140, Iss. 5, pp. 1568-1571
Open Access | Times Cited: 120

Page 1 - Next Page

Scroll to top