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For: Ping YQ, Mao C, Xiao P, Zhao RJ, Jiang Y, Yang Z, An WT, Shen DD, Yang F, Zhang H, Qu C, Shen Q, Tian C, Li ZJ, Li S, Wang GY, Tao X, Wen X, Zhong YN, Yang J, Yi F, Yu X, Xu HE, Zhang Y, Sun JP. Structures of the glucocorticoid-bound adhesion receptor GPR97-Go complex. Nature 2021;589:620-6. [PMID: 33408414 DOI: 10.1038/s41586-020-03083-w] [Cited by in Crossref: 12] [Cited by in F6Publishing: 11] [Article Influence: 12.0] [Reference Citation Analysis]
Number Citing Articles
1 Yuan Y, Jia G, Wu C, Wang W, Cheng L, Li Q, Li Z, Luo K, Yang S, Yan W, Su Z, Shao Z. Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition. Cell Res 2021. [PMID: 34526663 DOI: 10.1038/s41422-021-00566-x] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
2 Chen Q, Plasencia M, Li Z, Mukherjee S, Patra D, Chen CL, Klose T, Yao XQ, Kossiakoff AA, Chang L, Andrews PC, Tesmer JJG. Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1. Nature 2021;595:600-5. [PMID: 34262173 DOI: 10.1038/s41586-021-03721-x] [Cited by in Crossref: 8] [Cited by in F6Publishing: 3] [Article Influence: 8.0] [Reference Citation Analysis]
3 Jiang H. Cryo-EM structure determination captures new chemical modification of protein. Sci China Life Sci 2021;64:1781-3. [PMID: 33471275 DOI: 10.1007/s11427-021-1886-8] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
4 Boucard AA. Self-activated adhesion receptor proteins visualized. Nature 2022. [PMID: 35418555 DOI: 10.1038/d41586-022-00972-0] [Reference Citation Analysis]
5 Barros-Álvarez X, Nwokonko RM, Vizurraga A, Matzov D, He F, Papasergi-Scott MM, Robertson MJ, Panova O, Yardeni EH, Seven AB, Kwarcinski FE, Su H, Peroto MC, Meyerowitz JG, Shalev-Benami M, Tall GG, Skiniotis G. The tethered peptide activation mechanism of adhesion GPCRs. Nature 2022. [PMID: 35418682 DOI: 10.1038/s41586-022-04575-7] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 3.0] [Reference Citation Analysis]
6 Qu X, Qiu N, Wang M, Zhang B, Du J, Zhong Z, Xu W, Chu X, Ma L, Yi C, Han S, Shui W, Zhao Q, Wu B. Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1. Nature 2022. [PMID: 35418679 DOI: 10.1038/s41586-022-04580-w] [Cited by in Crossref: 4] [Cited by in F6Publishing: 1] [Article Influence: 4.0] [Reference Citation Analysis]
7 García-Nafría J, Tate CG. Structure determination of GPCRs: cryo-EM compared with X-ray crystallography. Biochem Soc Trans 2021;49:2345-55. [PMID: 34581758 DOI: 10.1042/BST20210431] [Reference Citation Analysis]
8 Liebscher I, Cevheroğlu O, Hsiao CC, Maia AF, Schihada H, Scholz N, Soave M, Spiess K, Trajković K, Kosloff M, Prömel S. A guide to adhesion GPCR research. FEBS J 2021. [PMID: 34729908 DOI: 10.1111/febs.16258] [Reference Citation Analysis]
9 Wittlake A, Prömel S, Schöneberg T. The Evolutionary History of Vertebrate Adhesion GPCRs and Its Implication on Their Classification. Int J Mol Sci 2021;22:11803. [PMID: 34769233 DOI: 10.3390/ijms222111803] [Reference Citation Analysis]
10 Yang F, Guo L, Li Y, Wang G, Wang J, Zhang C, Fang GX, Chen X, Liu L, Yan X, Liu Q, Qu C, Xu Y, Xiao P, Zhu Z, Li Z, Zhou J, Yu X, Gao N, Sun JP. Structure, function and pharmacology of human itch receptor complexes. Nature 2021;600:164-9. [PMID: 34789875 DOI: 10.1038/s41586-021-04077-y] [Reference Citation Analysis]
11 Qin J, Cai Y, Xu Z, Ming Q, Ji SY, Wu C, Zhang H, Mao C, Shen DD, Hirata K, Ma Y, Yan W, Zhang Y, Shao Z. Molecular mechanism of agonism and inverse agonism in ghrelin receptor. Nat Commun 2022;13:300. [PMID: 35027551 DOI: 10.1038/s41467-022-27975-9] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
12 [DOI: 10.1101/2021.04.01.438115] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
13 Harada N, Arahori Y, Okuyama M, Luis PB, Joseph AI, Kitakaze T, Goshima N, Schneider C, Inui H, Yamaji R. Curcumin activates G protein-coupled receptor 97 (GPR97) in a manner different from glucocorticoid. Biochemical and Biophysical Research Communications 2022;595:41-6. [DOI: 10.1016/j.bbrc.2022.01.075] [Reference Citation Analysis]
14 Baxendale S, Asad A, Shahidan NO, Wiggin GR, Whitfield TT. The adhesion GPCR Adgrg6 (Gpr126): Insights from the zebrafish model. Genesis 2021;59:e23417. [PMID: 33735533 DOI: 10.1002/dvg.23417] [Reference Citation Analysis]
15 Torrens-Fontanals M, Stepniewski TM, Gloriam DE, Selent J. Structural dynamics bridge the gap between the genetic and functional levels of GPCRs. Curr Opin Struct Biol 2021;69:150-9. [PMID: 34052782 DOI: 10.1016/j.sbi.2021.04.005] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
16 Xiao P, Guo S, Wen X, He QT, Lin H, Huang SM, Gou L, Zhang C, Yang Z, Zhong YN, Yang CC, Li Y, Gong Z, Tao XN, Yang ZS, Lu Y, Li SL, He JY, Wang C, Zhang L, Kong L, Sun JP, Yu X. Tethered peptide activation mechanism of the adhesion GPCRs ADGRG2 and ADGRG4. Nature 2022. [PMID: 35418677 DOI: 10.1038/s41586-022-04590-8] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 4.0] [Reference Citation Analysis]
17 Pawnikar S, Magenheimer BS, Munoz EN, Maser RL, Miao Y. Mechanism of tethered agonist-mediated signaling by polycystin-1. Proc Natl Acad Sci U S A 2022;119:e2113786119. [PMID: 35522707 DOI: 10.1073/pnas.2113786119] [Reference Citation Analysis]
18 Bueschbell B, Manga P, Schiedel AC. The Many Faces of G Protein-Coupled Receptor 143, an Atypical Intracellular Receptor. Front Mol Biosci 2022;9:873777. [DOI: 10.3389/fmolb.2022.873777] [Reference Citation Analysis]
19 Rosa M, Noel T, Harris M, Ladds G. Emerging roles of adhesion G protein-coupled receptors. Biochem Soc Trans 2021:BST20201144. [PMID: 34282836 DOI: 10.1042/BST20201144] [Reference Citation Analysis]
20 Poll BG, Chen L, Chou CL, Raghuram V, Knepper MA. Landscape of GPCR expression along the mouse nephron. Am J Physiol Renal Physiol 2021;321:F50-68. [PMID: 34029142 DOI: 10.1152/ajprenal.00077.2021] [Reference Citation Analysis]
21 Kaczmarek I, Suchý T, Prömel S, Schöneberg T, Liebscher I, Thor D. The relevance of adhesion G protein-coupled receptors in metabolic functions. Biol Chem 2021. [PMID: 34218541 DOI: 10.1515/hsz-2021-0146] [Reference Citation Analysis]
22 An W, Lin H, Ma L, Zhang C, Zheng Y, Cheng Q, Ma C, Wu X, Zhang Z, Zhong Y, Wang M, He D, Yang Z, Du L, Feng S, Wang C, Yang F, Xiao P, Zhang P, Yu X, Sun JP. Progesterone activates GPR126 to promote breast cancer development via the Gi pathway. Proc Natl Acad Sci U S A 2022;119:e2117004119. [PMID: 35394864 DOI: 10.1073/pnas.2117004119] [Reference Citation Analysis]
23 Wang MW, Yang Z, Chen X, Zhou SH, Huang GL, Sun JN, Jiang H, Xu WM, Lin HC, Yu X, Sun JP. Activation of PTH1R alleviates epididymitis and orchitis through Gq and β-arrestin-1 pathways. Proc Natl Acad Sci U S A 2021;118:e2107363118. [PMID: 34740971 DOI: 10.1073/pnas.2107363118] [Reference Citation Analysis]
24 Lin JY, Yang Z, Yang C, Du JX, Yang F, Cheng J, Pan W, Zhang SJ, Yan X, Wang J, Wang J, Tie L, Yu X, Chen X, Sun JP. An ionic lock and a hydrophobic zipper mediate the coupling between an insect pheromone receptor BmOR3 and downstream effectors. J Biol Chem 2021;297:101160. [PMID: 34480896 DOI: 10.1016/j.jbc.2021.101160] [Reference Citation Analysis]
25 Ping YQ, Xiao P, Yang F, Zhao RJ, Guo SC, Yan X, Wu X, Zhang C, Lu Y, Zhao F, Zhou F, Xi YT, Yin W, Liu FZ, He DF, Zhang DL, Zhu ZL, Jiang Y, Du L, Feng SQ, Schöneberg T, Liebscher I, Xu HE, Sun JP. Structural basis for the tethered peptide activation of adhesion GPCRs. Nature 2022. [PMID: 35418678 DOI: 10.1038/s41586-022-04619-y] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 3.0] [Reference Citation Analysis]
26 Chao ML, Luo S, Zhang C, Zhou X, Zhou M, Wang J, Kong C, Chen J, Lin Z, Tang X, Sun S, Tang X, Chen H, Wang H, Wang D, Sun JP, Han Y, Xie L, Ji Y. S-nitrosylation-mediated coupling of G-protein alpha-2 with CXCR5 induces Hippo/YAP-dependent diabetes-accelerated atherosclerosis. Nat Commun 2021;12:4452. [PMID: 34294713 DOI: 10.1038/s41467-021-24736-y] [Reference Citation Analysis]