Dr Maddalena Cross
Affiliation: Department of Medicine, University of Melbourne
Department of Medicine
The University of Melbourne
Chronic inflammatory diseases, including arthritis, represent the greatest collective burden of suffering and economic cost in the developed world, afflicting one in three people over the course of their lives, in addition to consuming tens of billions of dollars in annual health care costs.
Macrophages are the key cells of arthritic disease. Macrophages are the only cell type whose number correlates with the severity of rheumatoid arthritis lesions. Our goal is to understand the cellular signalling networks within the macrophage that are associated specifically with the CSF-1 receptor (CSF-1R) upon activation, the signalosome. The signalosome is comprised of proteins and protein complexes that interact either directly, constitutively or lie downstream of the CSF-1R. A novel enrichment strategy for the specific study of the CSF-1R signalosome has been developed. By utilising a proteomic approach, we are gaining further insight into the proteins that are involved in the CSF-1R signalosome. A greater knowledge of macrophage cell signalling will enable us to control macrophage function.
- Cross M, Csar X, Wilson NJ, Manes G, Addona TA, Whitty GA, Hamilton JA, Molecular analysis of CSF-1-induced macrophage differentiation in M1 cells: a novel 110kDa form of MysPDZ associated with signaling via tyrosine 559 in the activated CSF-1 receptor, Journal of Biological Chemistry, (2003) submitted for publication
- Maher, MJ, CrossM, WilceMCJ, GussJM, Wedd, AGMetal-Substituted Derivatives of the Rubredoxin from Clostridium pasteurianum: X-ray Crystallography’, Acta Cryst (2003) submitted for publication
- Bertini I, Luchinat C, Nerinovski K, Parigi G, Cross M, Xiao Z, Wedd AG, Hydration in a Rubredoxin Mutant protein containing a (Cys-S)3FeIII(OH) Site, Biophysical Journal, 84, 545-551 (2003)
- Cross M, Xiao Z, Maes EM, Czernuszewicz RS, Drew SC, Pilbrow JR, George GN and Wedd AG, “Mutation of the cysteine residues 9 and 42 to alanine and glycine in the rubredoxin from Clostridium pasteurianum”, J. Biol. Inorg. Chem., 7, 781–790 (2002)
- Xiao Z, Gardner AR, Cross M, Maes EA, Czernuszewicz RS, Sola M, Wedd AG, “Redox thermodynamics of mutant forms of the rubredoxin from Clostridium pasteurianum: identification of a stable FeIII(S-Cys)3(OH) centre in the C6S mutant”, J. Biol. Inorg. Chem., 6, 638-649 (2001)
- Xiao Z, Maher MJ, Cross M, Bond CS, Guss JM, Wedd AG, “Mutation of the surface valine residues 8 and 44 in the rubredoxin from Clostridium pasteurianum: solvent access versus structural changes as determinants of reversible potential”, J. Biol. Inorg. Chem., 5, 75-84 (2000)