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:

Structural basis for the tethered peptide activation of adhesion GPCRs
Yu-Qi Ping, Peng Xiao, Fan Yang, et al.
Nature (2022) Vol. 604, Iss. 7907, pp. 763-770
Closed Access | Times Cited: 88

Showing 1-25 of 88 citing articles:

Unsaturated bond recognition leads to biased signal in a fatty acid receptor
Chunyou Mao, Peng Xiao, Xiao-Na Tao, et al.
Science (2023) Vol. 380, Iss. 6640
Open Access | Times Cited: 76

Structural basis of amine odorant perception by a mammal olfactory receptor
Lulu Guo, Jie Cheng, Shuo Lian, et al.
Nature (2023) Vol. 618, Iss. 7963, pp. 193-200
Closed Access | Times Cited: 48

Evolutionary study and structural basis of proton sensing by Mus GPR4 and Xenopus GPR4
Xin Wen, Pan Shang, Haidi Chen, et al.
Cell (2025)
Closed Access | Times Cited: 4

Identification, structure, and agonist design of an androgen membrane receptor
Zhao Yang, Yu-Qi Ping, Ming‐Wei Wang, et al.
Cell (2025)
Closed Access | Times Cited: 3

A force-sensitive adhesion GPCR is required for equilibrioception
Zhao Yang, Shuhua Zhou, Qiyue Zhang, et al.
Cell Research (2025)
Open Access | Times Cited: 2

Structure, function and drug discovery of GPCR signaling
Lin Cheng, Fan Xia, Ziyan Li, et al.
Molecular Biomedicine (2023) Vol. 4, Iss. 1
Open Access | Times Cited: 33

Molecular sensing of mechano- and ligand-dependent adhesion GPCR dissociation
Nicole Scholz, Anne-Kristin Dahse, Marguerite Kemkemer, et al.
Nature (2023) Vol. 615, Iss. 7954, pp. 945-953
Closed Access | Times Cited: 30

A method for structure determination of GPCRs in various states
Qiong Guo, Binbin He, Yixuan Zhong, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 1, pp. 74-82
Closed Access | Times Cited: 28

Cryo-EM advances in GPCR structure determination
Wataru Shihoya, A. Iwama, Fumiya K. Sano, et al.
The Journal of Biochemistry (2024) Vol. 176, Iss. 1, pp. 1-10
Open Access | Times Cited: 15

Conformational transitions and activation of the adhesion receptor CD97
Chunyou Mao, Ru-Jia Zhao, Ying-Jun Dong, et al.
Molecular Cell (2024) Vol. 84, Iss. 3, pp. 570-583.e7
Closed Access | Times Cited: 10

Structural insights into adhesion GPCR ADGRL3 activation and Gq, Gs, Gi, and G12 coupling
Qian Yu, Zhengxiong Ma, Chunhong Liu, et al.
Molecular Cell (2022) Vol. 82, Iss. 22, pp. 4340-4352.e6
Open Access | Times Cited: 37

Structural basis of adhesion GPCR GPR110 activation by stalk peptide and G-proteins coupling
Xinyan Zhu, Qian Yu, Xiaowan Li, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 31

Structures of the ADGRG2–Gs complex in apo and ligand-bound forms
Hui Lin, Peng Xiao, Ruiqian Bu, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 11, pp. 1196-1203
Closed Access | Times Cited: 29

Constitutive activation mechanism of a class C GPCR
Jin Woo Shin, Junhyeon Park, Jieun Jeong, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 4, pp. 678-687
Closed Access | Times Cited: 7

The repertoire and structure of adhesion GPCR transcript variants assembled from publicly available deep-sequenced human samples
Christina Katharina Kuhn, Udo Stenzel, Sandra Berndt, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 7, pp. 3823-3836
Open Access | Times Cited: 7

Heterogeneity of tethered agonist signaling in adhesion G protein-coupled receptors
Andrew N. Dates, Daniel T.D. Jones, Jeffrey S. Smith, et al.
Cell chemical biology (2024) Vol. 31, Iss. 8, pp. 1542-1553.e4
Closed Access | Times Cited: 7

The dark sides of the GPCR tree ‐ research progress on understudied GPCRs
Magdalena M. Scharf, Laura J. Humphrys, Sandra Berndt, et al.
British Journal of Pharmacology (2024)
Open Access | Times Cited: 6

Stachel-mediated activation of adhesion G protein-coupled receptors: insights from cryo-EM studies
Ines Liebscher, Torsten Schöneberg, Doreen Thor
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 24

The adhesion GPCRs CELSR1–3 and LPHN3 engage G proteins via distinct activation mechanisms
Duy Lan Huong Bui, Andrew T. Roach, Jingxian Li, et al.
Cell Reports (2023) Vol. 42, Iss. 6, pp. 112552-112552
Open Access | Times Cited: 16

7TM domain structures of adhesion GPCRs: what's new and what's missing?
Florian Seufert, Yin Kwan Chung, Peter W. Hildebrand, et al.
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 8, pp. 726-739
Closed Access | Times Cited: 16

Piconewton Forces Mediate GAIN Domain Dissociation of the Latrophilin-3 Adhesion GPCR
Brian L. Zhong, Christina E. Lee, Vipul T. Vachharajani, et al.
Nano Letters (2023) Vol. 23, Iss. 20, pp. 9187-9194
Open Access | Times Cited: 14

Isoform- and ligand-specific modulation of the adhesion GPCR ADGRL3/Latrophilin3 by a synthetic binder
Szymon P. Kordon, Przemysław Dutka, Justyna M. Adamska, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 13

Exploring the constitutive activation mechanism of the class A orphan GPR20
Mingyang Zhang, Jian‐Yang Ao, Ning Liu, et al.
Acta Pharmacologica Sinica (2024)
Closed Access | Times Cited: 5

Role of Adhesion G Protein-Coupled Receptors in Immune Dysfunction and Disorder
Wen-Yi Tseng, Martin Stacey, Hsi‐Hsien Lin
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 6, pp. 5499-5499
Open Access | Times Cited: 12

Mechanosensitive GPCRs and ion channels in shear stress sensing
Rui Xiao, Jie Liu, X.Z. Shawn Xu
Current Opinion in Cell Biology (2023) Vol. 84, pp. 102216-102216
Closed Access | Times Cited: 12

Page 1 - Next Page

Scroll to top