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. 2022 Oct 31;12(11):e1091. doi: 10.1002/ctm2.1091

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© 2022 The Authors. Clinical and Translational Medicine published by John Wiley & Sons Australia, Ltd on behalf of Shanghai Institute of Clinical Bioinformatics.

This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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ERK signalling and surface expression of GPCRs in the presence of MRAPs. (A–D) Western blot for ERK1/2 and pERK1/2, and Tubulin was used as reference control. The samples order from left to right were: GPCR only (with 10^‐7 M agonist), GPCR+MRAP1 (with 10^‐7 M agonist), GPCR+MRAP2 (with 10^‐7 M agonist), GPCR only (with 10^‐9 M agonist), GPCR+MRAP1 (with 10^‐9 M agonist), GPCR+MRAP2 (with 10^‐9 M agonist). (E–L) Surface expression of selected GPCRs in HEK293 cells transfected with empty vector, MRAP1 or MRAP2 at 1:3 and 1:6 ratio using cell ELISA assays. One‐way ANOVA with post hoc Turkey test. ns, no significant change; *p < .05, **p < .01, ***p < .001, ****p < .0001. ELISA results of other GPCRs are shown in Figure S9. Each data column represents the mean ± SEM of three replicates (n = 3).