Multi-Component Mechanism of H2 Relaxin Binding to RXFP1 through NanoBRET Kinetic Analysis-Reference-Cited by-同舟云学术

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Multi-Component Mechanism of H2 Relaxin Binding to RXFP1 through NanoBRET Kinetic Analysis

Published:2019-01 Issue: Volume:11 Page:93-113
ISSN:2589-0042
Container-title:iScience
language:en
Short-container-title:iScience

Author:

Hoare Bradley L.,Bruell Shoni,Sethi Ashish,Gooley Paul R.,Lew Michael J.,Hossain Mohammed A.,Inoue Asuka,Scott Daniel J.,Bathgate Ross A.D.

Funder

National Health and Medical Research Council

Victorian Government Operational Infrastructure Support Program

Japan Agency for Medical Research and Development

Japan Society for the Promotion of Science

Publisher

Elsevier BV

Subject

Multidisciplinary

Reference47 articles.

1. International Union of Pharmacology LVII: recommendations for the nomenclature of receptors for relaxin family peptides;Bathgate;Pharmacol. Rev.,2006

2. Chimeric RXFP1 and RXFP2 receptors highlight the similar mechanism of activation utilizing their N-terminal low-density lipoprotein class A modules;Bruell;Front. Endocrinol.,2013

3. Distinct activation modes of the Relaxin Family Peptide Receptor 2 in response to insulin-like peptide 3 and relaxin;Bruell;Sci. Rep.,2017

4. The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7;Bullesbach;J. Biol. Chem.,2005

5. Prolonged RXFP1 and RXFP2 signaling can be explained by poor internalization and a lack of β-arrestin recruitment;Callander;Am. J. Physiol. Cell Physiol.,2009

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