Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators
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DOI: 10.1038/nature22378
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Cited by:
- Fenghui Zhao & Qingtong Zhou & Zhaotong Cong & Kaini Hang & Xinyu Zou & Chao Zhang & Yan Chen & Antao Dai & Anyi Liang & Qianqian Ming & Mu Wang & Li-Nan Chen & Peiyu Xu & Rulve Chang & Wenbo Feng & T, 2022. "Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
- Janik B. Hedderich & Margherita Persechino & Katharina Becker & Franziska M. Heydenreich & Torben Gutermuth & Michel Bouvier & Moritz Bünemann & Peter Kolb, 2022. "The pocketome of G-protein-coupled receptors reveals previously untargeted allosteric sites," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
- Xueqian Peng & Linlin Yang & Zixuan Liu & Siyi Lou & Shiliu Mei & Meiling Li & Zhong Chen & Haitao Zhang, 2022. "Structural basis for recognition of antihistamine drug by human histamine receptor," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
- Shane C. Wright & Aikaterini Motso & Stefania Koutsilieri & Christian M. Beusch & Pierre Sabatier & Alessandro Berghella & Élodie Blondel-Tepaz & Kimberley Mangenot & Ioannis Pittarokoilis & Despoina-, 2023. "GLP-1R signaling neighborhoods associate with the susceptibility to adverse drug reactions of incretin mimetics," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
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