About Dr Jacqui Matthews
I want to understand how the thousands of proteins encoded by our genome come together to regulate essentially every process in our bodies.
Dr Jacqui Matthews seeks to understand how key regulatory proteins function and how they can be controlled to treat diseases such as childhood leukemia and breast cancer.
My research has focused on understanding proteins at the molecular and atomic level and how we can modify those properties to redress biological problems. My specific focus is on regulatory proteins that have important roles in development, but under also contribute to human disease. I started out studying protein folding at the University of Cambridge for my PhD, and moved on to investigate the structure/function relationships of interleukin-6, a cytokine that is heavily involved in the body’s response to injury and infection. While looking at some of the key protein-protein interactions between IL-6 and its partners, I realized that the general field of protein-protein interactions was really opening up. Now, with the sequencing of the human genome project complete, we know the identity of most the protein gene products, but we are only really just discovering how all of these proteins interact to regulate essentially every single event within our bodies. My work now centers on the LMO (LIM-only) and LIM-HD (LIM-homeodomain) families of proteins, and their interaction partners. These proteins are essential for normal development but can also contribute to childhood leukemias, breast cancer and neural defects.
I have been awarded several prestigious research fellowships, including a Cambridge Commonwealth Trust Postgraduate Fellowship, an ARC Australian Research Fellowship (2000), and the 2004 Viertel Foundation Senior Medical Research Fellowship (2004). My laboratory is well funded by major competitive grants from the ARC, NHMRC, the NSW Leukemia Foundation and the Cancer Institute NSW.
Selected publications
- Chong, S., N. Vickaryous, A. Ashe, N. Zamudio, S. Hemley, T. Stopka, A. Skoultchi, H. Scott, J. M. Matthews, M. O-Bryan, M. Bluett, and E. Whitelaw. (2007) "Modifiers of epigenetic reprogramming produce paternal effects in the mouse." Nat. Genet.: in press (IF 25.8)
- Ryan, D. P., M. Sunde, A. H.-Y. Kwan, N. J. Marianayagam, A. L. Nancarrow, R. N. vanden Hoven, L. S. Thompson, M. Baca, J. P. Mackay, J. E. Visvader, and J. M. Matthews. (2006) "Identification of the key LMO2-binding determinants on Ldb1." J. Mol. Biol. 359(1): 66-75. PubMedId: 16616188
- Liew, C. K., R. J. Y. Simpson, A. H. Kwan, L. A. Crofts, F. E. Loughlin, J. M. Matthews, M. Crossley, and J. P. Mackay. (2005) "Zinc fingers as protein recognition motifs: structural basis for the GATA-1/Friend of GATA interaction." Proc. Natl Acad. Sci. USA 102(3): 583-588. PubMedId: 15644435
- Deane, J. E., D. P. Ryan, M. Sunde, M. J. Maher, J. M. Guss, J. E. Visvader, and J. M. Matthews. (2004) "Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex." EMBO J. 23(18): 3589-3598. PubMedId: 15343268
- Marianayagam, N. J., M. Sunde, and J. M. Matthews. (2004) "The power of two:protein dimerization in biology." Trends Biochem. Sci. 29(11):618-625. PubMedId: 15501681
- Deane, J. E., J. P. Mackay, A. H. Kwan, E. Y. Sum, J. E. Visvader, and J. M. Matthews. (2003) "Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4." EMBO J 22(9): 2224-2233. PubMedId: 12727888
- Simpson, R. J., A. Hammacher, D. K. Smith, J. M. Matthews, and L. D. Ward. (1997) "Interleukin-6: structure-function relationships." Protein Sci 6(5): 929-955. PubMedId: 9144766
- Matthews, J. M., and A. R. Fersht. (1995) "Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase." Biochemistry 34(20): 6805-6814. PubMedId: 7756312
- Fersht, A. R., L. S. Itzhaki, N. F. elMasry, J. M. Matthews, and D. E. Otzen. (1994) "Single versus parallel pathways of protein folding and fractional formation of structure in the transition state." Proc Natl Acad Sci U S A 91(22): 10426-10429. PubMedId: 7937968
- Horovitz, A., J. M. Matthews, and A. R. Fersht. (1992) "Alpha-helix stability in proteins. II. Factors that influence stability at an internal position." J Mol Biol 227(2): 560-568. PubMedId: 1404369