My lab studies programmed cell death, a process crucial for tissue development and keeping us healthy.
We use protein crystallography to visualise molecules in atomic detail. This is providing insights into the proteins that regulate programmed cell death and guiding the development of drugs that can target these proteins in diseased cells.
Co-awardee with Prof David Huang, Assoc Prof Guillaume Lessene and Prof Andrew Roberts, Eureka Prize for Innovation in Medical Research, Awarded by the Australian Museum,
Gottschalk Medal, Awarded by the Australian Academy of Science,
Co-awardee with Assoc Prof Guilluame Lessene, Burnet Prize, Awarded by Walter and Eliza Hall Institute,
Available for supervision
Our lab is working towards understanding how cell death is controlled at the molecular level.
Our main interests are:
- Control of apoptosis by the Bcl-2 family of proteins.
- Designing therapeutics to target Bcl-2 protein family regulated cell death.
- Understanding how the MLKL protein regulates necroptotic cell death.
We use structural biology, in particular protein crystallography supported by biochemical and biological analyses, to decipher these pathways. These tools allow us to observe the atomic details of cell death proteins, providing key insights into how they function at the molecular level and informing the development of therapeutic compounds capable of modulating their activity.
We also use protein crystallography to study other proteins important to human health, including:
- CLEC9A, a dendritic cell receptor that recognises dead and dying cells
-Malarial proteins involved in parasite invasion of red blood cells.