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Characterisation of the signalling pathways of the relaxin family peptpide receptors, RXFP1 and RXFP2

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Version 2 2022-11-07, 05:51
Version 1 2021-07-13, 03:39
thesis
posted on 2022-11-07, 05:51 authored by Michelle Louise Halls.

Winner of the Mollie Holman Doctoral Medal for Excellence.


Two orphan leucine-rich repeat-containing G protein-coupled receptors were recently identified as targets for the relaxin family peptides relaxin and insulin-like peptide (INSL) 3. Relaxin is the cognate ligand for relaxin family peptide receptor (RXFP) 1, whereas INSL3 is the ligand

for RXFP2. This study sought to characterise the pharmacological binding properties and signalling pathways of both RXFP1 and RXFP2.


This thesis was scanned from the print manuscript for digital preservation and is copyright the author. 


Author requested conversion to open access 27 Oct 2022



History

Principal supervisor

Roger J. Summers

Additional supervisor 1

Ross A.D. Bathgate

Year of Award

2007

Department, School or Centre

Biomedical Sciences (Monash Biomedicine Discovery Institute)

Additional Institution or Organisation

Pharmacology

Campus location

Australia

Course

Doctor of Philosophy

Degree Type

DOCTORATE

Faculty

Faculty of Medicine, Nursing and Health Sciences

File Name

Halls-33168027190160

Author converted thesis to Open Access

2022-10-27