Open Access Helper

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:

GPCR kinase knockout cells reveal the impact of individual GRKs on arrestin binding and GPCR regulation
Julia Drube, Raphael S. Haider, Edda S. F. Matthees, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 87

Showing 1-25 of 87 citing articles:

Plasma membrane preassociation drives β-arrestin coupling to receptors and activation
Jak Grimes, Zsombor Kőszegi, Yann Lanoiselée, et al.
Cell (2023) Vol. 186, Iss. 10, pp. 2238-2255.e20
Open Access | Times Cited: 42
The Role of G Protein–Coupled Receptors and Receptor Kinases in Pancreaticβ-Cell Function and Diabetes
Matthew J. Varney, Jeffrey Benovic
Pharmacological Reviews (2024) Vol. 76, Iss. 2, pp. 267-299
Open Access | Times Cited: 19
Arrestin‐independent internalization of the GLP‐1 receptor is facilitated by a GRK, clathrin, and caveolae‐dependent mechanism
Ee Von Moo, Thor C. Møller, Flemming Brandt Sørensen, et al.
FEBS Journal (2025)
Open Access | Times Cited: 2
How phosphorylation impacts intrinsically disordered proteins and their function
Estella A. Newcombe, Elise Delaforge, Rasmus Hartmann‐Petersen, et al.
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 901-913
Open Access | Times Cited: 49
β-arrestin1 and 2 exhibit distinct phosphorylation-dependent conformations when coupling to the same GPCR in living cells
Raphael S. Haider, Edda S. F. Matthees, Julia Drube, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 43
β-Arrestin-independent endosomal cAMP signaling by a polypeptide hormone GPCR
Emily E. Blythe, Mark von Zastrow
Nature Chemical Biology (2023)
Open Access | Times Cited: 24
GPCR signaling bias: an emerging framework for opioid drug development
Ryoji Kise, Asuka Inoue
The Journal of Biochemistry (2024) Vol. 175, Iss. 4, pp. 367-376
Open Access | Times Cited: 10
The role of G protein-coupled receptor kinases in GLP-1R β-arrestin recruitment and internalisation
Samantha M. McNeill, Jessica Bo Li Lu, Carlo Marion C. Carino, et al.
Biochemical Pharmacology (2024) Vol. 222, pp. 116119-116119
Open Access | Times Cited: 10
GPCR kinases differentially modulate biased signaling downstream of CXCR3 depending on their subcellular localization
Julia Gardner, Dylan Scott Eiger, Chloe Hicks, et al.
Science Signaling (2024) Vol. 17, Iss. 823
Open Access | Times Cited: 9
Know your molecule: pharmacological characterization of drug candidates to enhance efficacy and reduce late-stage attrition
Terry Kenakin
Nature Reviews Drug Discovery (2024) Vol. 23, Iss. 8, pp. 626-644
Closed Access | Times Cited: 8
Differential Regulation of GPCRs—Are GRK Expression Levels the Key?
Edda S. F. Matthees, Raphael S. Haider, Carsten Hoffmann, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 46
How Carvedilol activates β2-adrenoceptors
Tobias Benkel, Mirjam Zimmermann, Julian Zeiner, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 33
Atypical Chemokine Receptor 3 “Senses” CXC Chemokine Receptor 4 Activation Through GPCR Kinase Phosphorylation
Christopher T. Schafer, Qiuyan Chen, J.J.G. Tesmer, et al.
Molecular Pharmacology (2023) Vol. 104, Iss. 4, pp. 174-186
Open Access | Times Cited: 19
Bias translation: The final frontier?
Terry Kenakin
British Journal of Pharmacology (2024) Vol. 181, Iss. 9, pp. 1345-1360
Open Access | Times Cited: 8
Unraveling allostery within the angiotensin II type 1 receptor for Gα q and β-arrestin coupling
Yubo Cao, Wijnand J. C. van der Velden, Yoon Namkung, et al.
Science Signaling (2023) Vol. 16, Iss. 797
Open Access | Times Cited: 16
Structural biology of complement receptors
Jorge Arturo Santos-López, Karla de la Paz, Francisco J. Fernández, et al.
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 13
Arrestin‐centred interactions at the membrane and their conformational determinants
Owen Underwood, Raphael S. Haider, Julie Sanchez, et al.
British Journal of Pharmacology (2024)
Open Access | Times Cited: 5
Regulation of the pro‐inflammatory G protein‐coupled receptor GPR84
Sara Marsango, Graeme Milligan
British Journal of Pharmacology (2023) Vol. 181, Iss. 10, pp. 1500-1508
Open Access | Times Cited: 11
GRK specificity and Gβγ dependency determines the potential of a GPCR for arrestin-biased agonism
Edda S. F. Matthees, Jenny C. Filor, Natasha Jaiswal, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 4
Key phosphorylation sites for robust β-arrestin2 binding at the MOR revisited
Owen Underwood, Sebastian Fritzwanker, Jaqueline Glenn, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 4
Enhanced Production and Functional Characterization of Recombinant Equine Chorionic Gonadotropin (rec-eCG) in CHO-DG44 Cells
Munkhzaya Byambaragchaa, Sei Hyen Park, Myung-Hum Park, et al.
Biomolecules (2025) Vol. 15, Iss. 2, pp. 289-289
Open Access
Distinct Membrane Binding Properties of the Two Non-visual Arrestins
Thomas D. Killeen, Katelyn R. Tepper, Kyle W. Miller, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access
Intersection of GPCR trafficking and cAMP signaling at endomembranes
Léa Ripoll, Mark von Zastrow, Emily E. Blythe
The Journal of Cell Biology (2025) Vol. 224, Iss. 4
Closed Access
Signal termination of the chemokine receptor CCR9 is governed by an arrestin-independent phosphorylation mechanism
Thomas D. Lamme, Martine J. Smit, Christopher T. Schafer
Journal of Biological Chemistry (2025), pp. 108462-108462
Open Access
Page 1 - Next Page

Scroll to top