Sarah Hennebry completed her Ph.D. in December 2007. The subject of her thesis was 'The evolution of the structure and function of transthyretin-like proteins'. Sarah's research has involved the integration of a number of techniques, including protein structure determination, recombinant protein generation and functional characterization, gene expression, microbiology and phylogenetic analysis of protein evolution. In early 2008, Sarah commenced employment in the Human Neurotransmitters and Hypertension & Kidney Disease Laboratories at the Baker IDI Heart and Diabetes Institute, where she was commissioned to cement the molecular biology research division of the group with a particular focus on the establishment of a translational research programme into the role of novel proteins in human health and disease. Sarah's recent research has been focused on elucidating the function of a novel monoamine oxidase, renalase. Renalase is hypothesized to act as the soluble counterpart to monoamine oxidases and may play an important role in the regulation of blood pressure. At the recent Annual Scientific Meeting for the High Blood Pressure Research Council of Australia, Sarah presented data demonstrating the wide-spread distribution of renalase in human tissues, despite previous reports of the protein being largely restricted to renal and cardiac tissues. Sarah has identified several splice variants of the renalase gene and will use a number of cell culture models recently established by herself and colleagues to determine whether there is tissue-specific regulation of renalase function.