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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:

Multiple ligand-specific conformations of the β2-adrenergic receptor
Alem W. Kahsai, Kunhong Xiao, Sudarshan Rajagopal, et al.
Nature Chemical Biology (2011) Vol. 7, Iss. 10, pp. 692-700
Open Access | Times Cited: 247

Showing 1-25 of 247 citing articles:

Molecular Docking and Structure-Based Drug Design Strategies
Leonardo L. G. Ferreira, Ricardo Nascimento dos Santos, Glaucius Oliva, et al.
Molecules (2015) Vol. 20, Iss. 7, pp. 13384-13421
Open Access | Times Cited: 1880
Molecular signatures of G-protein-coupled receptors
AJ Venkatakrishnan, Xavier Deupí, Guillaume Lebon, et al.
Nature (2013) Vol. 494, Iss. 7436, pp. 185-194
Closed Access | Times Cited: 1426
The Dynamic Process of β2-Adrenergic Receptor Activation
Rie Nygaard, Yaozhong Zou, Ron O. Dror, et al.
Cell (2013) Vol. 152, Iss. 3, pp. 532-542
Open Access | Times Cited: 762
Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR
Jeffrey J. Liu, Reto Horst, Vsevolod Katritch, et al.
Science (2012) Vol. 335, Iss. 6072, pp. 1106-1110
Open Access | Times Cited: 677
Biased signalling: from simple switches to allosteric microprocessors
Jeffrey S. Smith, Robert J. Lefkowitz, Sudarshan Rajagopal
Nature Reviews Drug Discovery (2018) Vol. 17, Iss. 4, pp. 243-260
Open Access | Times Cited: 643
Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors
Éric Reiter, Seungkirl Ahn, Arun K. Shukla, et al.
The Annual Review of Pharmacology and Toxicology (2011) Vol. 52, Iss. 1, pp. 179-197
Open Access | Times Cited: 545
Copper is required for oncogenic BRAF signalling and tumorigenesis
Donita C. Brady, Matthew S. Crowe, Michelle L. Turski, et al.
Nature (2014) Vol. 509, Iss. 7501, pp. 492-496
Open Access | Times Cited: 512
Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation
Dean P. Staus, Ryan T. Strachan, Aashish Manglik, et al.
Nature (2016) Vol. 535, Iss. 7612, pp. 448-452
Open Access | Times Cited: 322
The role of kinetic context in apparent biased agonism at GPCRs
Carmen Klein Herenbrink, David A. Sykes, Prashant Donthamsetti, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 312
GPCR desensitization: Acute and prolonged phases
Sudarshan Rajagopal, Sudha K. Shenoy
Cellular Signalling (2017) Vol. 41, pp. 9-16
Open Access | Times Cited: 289
Recent developments in biased agonism
James W. Wisler, Kunhong Xiao, A. Thomsen, et al.
Current Opinion in Cell Biology (2013) Vol. 27, pp. 18-24
Open Access | Times Cited: 272
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
Biased agonism: An emerging paradigm in GPCR drug discovery
Zoran Ranković, Tarsis F. Brust, Laura Bohn
Bioorganic & Medicinal Chemistry Letters (2015) Vol. 26, Iss. 2, pp. 241-250
Open Access | Times Cited: 248
G-Protein–Coupled Receptors in Heart Disease
Jialu Wang, Clarice Gareri, Howard A. Rockman
Circulation Research (2018) Vol. 123, Iss. 6, pp. 716-735
Open Access | Times Cited: 245
Nanobodies to Study G Protein–Coupled Receptor Structure and Function
Aashish Manglik, Brian K. Kobilka, Jan Steyaert
The Annual Review of Pharmacology and Toxicology (2016) Vol. 57, Iss. 1, pp. 19-37
Open Access | Times Cited: 244
The role of protein dynamics in GPCR function: insights from the β2AR and rhodopsin
Aashish Manglik, Brian K. Kobilka
Current Opinion in Cell Biology (2014) Vol. 27, pp. 136-143
Open Access | Times Cited: 218
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: 217
New Insights into Modes of GPCR Activation
Wenjing Wang, Yuhui Qiao, Zijian Li
Trends in Pharmacological Sciences (2018) Vol. 39, Iss. 4, pp. 367-386
Closed Access | Times Cited: 202
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and 19F-NMR
Fan Yang, Xiao Yu, Chuan Liu, et al.
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 186
A new era of GPCR structural and chemical biology
Sébastien Granier, Brian K. Kobilka
Nature Chemical Biology (2012) Vol. 8, Iss. 8, pp. 670-673
Open Access | Times Cited: 201
Efficacy of the β2-adrenergic receptor is determined by conformational equilibrium in the transmembrane region
Yutaka Kofuku, Takumi Ueda, Junya Okude, et al.
Nature Communications (2012) Vol. 3, Iss. 1
Open Access | Times Cited: 191
Biased and G Protein-Independent Signaling of Chemokine Receptors
Anne Steen, Olav Larsen, Stefanie Thiele, et al.
Frontiers in Immunology (2014) Vol. 5
Open Access | Times Cited: 169
A kinetic view of GPCR allostery and biased agonism
J. Robert Lane, Lauren T. May, Robert G. Parton, et al.
Nature Chemical Biology (2017) Vol. 13, Iss. 9, pp. 929-937
Open Access | Times Cited: 160
Functional competence of a partially engaged GPCR–β-arrestin complex
Punita Kumari, Ashish Srivastava, Ramanuj Banerjee, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 159
The Dynamic Process of b 2 -Adrenergic Receptor Activation
Rie Nygaard, Yaozhong Zou, Ron O. Dror, et al.
(2013)
Closed Access | Times Cited: 157
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