The Relaxin Receptor (RXFP1) Utilizes Hydrophobic Moieties on a Signaling Surface of Its N-terminal Low Density Lipoprotein Class A Module to Mediate Receptor Activation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
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1. Characterization of a new potent and long-lasting single chain peptide agonist of RXFP1 in cells and in vivo translational models;Scientific Reports;2022-11-28
2. Expression and Characterization of Relaxin Family Peptide Receptor 1 Variants;Frontiers in Pharmacology;2022-01-28
3. Structural Insights into the Unique Modes of Relaxin-Binding and Tethered-Agonist Mediated Activation of RXFP1 and RXFP2;Journal of Molecular Biology;2021-10
4. Structural insights into the modes of relaxin-binding and tethered-agonist activation of RXFP1 and RXFP2;2021-06-07
5. Using the novel HiBiT tag to label cell surface relaxin receptors for BRET proximity analysis;Pharmacology Research & Perspectives;2019-07-30
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