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:

Structures of the glucocorticoid-bound adhesion receptor GPR97–Go complex
Yu-Qi Ping, Chunyou Mao, Peng Xiao, et al.
Nature (2021) Vol. 589, Iss. 7843, pp. 620-626
Open Access | Times Cited: 134

Showing 1-25 of 134 citing articles:

Sampling alternative conformational states of transporters and receptors with AlphaFold2
Diego del Alamo, Davide Sala, Hassane S. Mchaourab, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 342

Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1
Qiuyan Chen, Manolo Plasencia, Zhuang Li, et al.
Nature (2021) Vol. 595, Iss. 7868, pp. 600-605
Open Access | Times Cited: 119

The tethered peptide activation mechanism of adhesion GPCRs
Ximena Barros-Álvarez, Robert M. Nwokonko, Alexander Vizurraga, et al.
Nature (2022) Vol. 604, Iss. 7907, pp. 757-762
Open Access | Times Cited: 102

Tethered peptide activation mechanism of the adhesion GPCRs ADGRG2 and ADGRG4
Peng Xiao, Shengchao Guo, Xin Wen, et al.
Nature (2022) Vol. 604, Iss. 7907, pp. 771-778
Closed Access | Times Cited: 100

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

Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1
Xiangli Qu, Na Qiu, Mu Wang, et al.
Nature (2022) Vol. 604, Iss. 7907, pp. 779-785
Open Access | Times Cited: 86

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 for strychnine activation of human bitter taste receptor TAS2R46
Weixiu Xu, Lijie Wu, Shenhui Liu, et al.
Science (2022) Vol. 377, Iss. 6612, pp. 1298-1304
Closed Access | Times Cited: 73

Gut microbial metabolite facilitates colorectal cancer development via ferroptosis inhibition
Weiwei Cui, Meng Guo, Dong Liu, et al.
Nature Cell Biology (2024) Vol. 26, Iss. 1, pp. 124-137
Closed Access | Times Cited: 66

G protein-coupled receptors in neurodegenerative diseases and psychiatric disorders
Thian‐Sze Wong, Guangzhi Li, Shiliang Li, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 62

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: 47

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 pharmacology of human itch receptor complexes
Fan Yang, Lulu Guo, Yu Li, et al.
Nature (2021) Vol. 600, Iss. 7887, pp. 164-169
Closed Access | Times Cited: 102

Structure determination of GPCRs: cryo-EM compared with X-ray crystallography
Javier García‐Nafría, Christopher G. Tate
Biochemical Society Transactions (2021) Vol. 49, Iss. 5, pp. 2345-2355
Open Access | Times Cited: 84

Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition
Yuan Yuan, Guowen Jia, Chao Wu, et al.
Cell Research (2021) Vol. 31, Iss. 12, pp. 1263-1274
Open Access | Times Cited: 71

S-nitrosylation-mediated coupling of G-protein alpha-2 with CXCR5 induces Hippo/YAP-dependent diabetes-accelerated atherosclerosis
Meng‐Lin Chao, Shanshan Luo, Chao Zhang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 57

G protein-coupled receptor signaling: transducers and effectors
Haoran Jiang, Daniella Galtes, Jialu Wang, et al.
AJP Cell Physiology (2022) Vol. 323, Iss. 3, pp. C731-C748
Open Access | Times Cited: 51

Pituitary hormone α-MSH promotes tumor-induced myelopoiesis and immunosuppression
Yueli Xu, Jiaxian Yan, Ye Tao, et al.
Science (2022) Vol. 377, Iss. 6610, pp. 1085-1091
Closed Access | Times Cited: 50

Adhesion G protein-coupled receptors: structure, signaling, physiology, and pathophysiology
Trisha Lala, Randy A. Hall
Physiological Reviews (2022) Vol. 102, Iss. 4, pp. 1587-1624
Open Access | Times Cited: 43

ZDHHC5-mediated NLRP3 palmitoylation promotes NLRP3-NEK7 interaction and inflammasome activation
Sihao Zheng, Xiangyong Que, Shuxian Wang, et al.
Molecular Cell (2023) Vol. 83, Iss. 24, pp. 4570-4585.e7
Open Access | Times Cited: 41

The cancer-immune dialogue in the context of stress
Yuting Ma, Guido Kroemer
Nature reviews. Immunology (2023) Vol. 24, Iss. 4, pp. 264-281
Closed Access | Times Cited: 34

Ligand recognition and G-protein coupling of trace amine receptor TAAR1
Zheng Xu, Lulu Guo, Jingjing Yu, et al.
Nature (2023) Vol. 624, Iss. 7992, pp. 672-681
Closed Access | Times Cited: 33

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: 32

Polycystin Channel Complexes
Orhi Esarte Palomero, Megan Larmore, Paul G. DeCaen
Annual Review of Physiology (2023) Vol. 85, Iss. 1, pp. 425-448
Open Access | Times Cited: 29

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: 28

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