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UP

Prof Michael Parker

Research Unit

Structural biology

Information

Head, ACRF Rational Drug Discovery Centre, SVI
Professorial Fellow and Professor, Department of Biochemistry abd Molecular Biology, and Director Bio21 Institute, University of Melbourne
NHMRC Senior Principal Research Fellow

Professional Experience

1980 B. Sc. (Hons.), Australian National University
1985 D. Phil., Oxford University, UK
1986-1991  Staff Scientist, European Molecular Biology Laboratory, Heidelberg, Germany
1991-1996 Welcome Australian Senior Research Fellow, SVI
1996-2000 Australian Research Council Senior Research Fellow, SVI
2000-2001 Australian Research Council Professorial Research Fellow
2002-2006 National Health & Medical Research Council Senior Principal Research Fellow
2007-2011 Australian Research Council Federation Fellow
2012-Present National Health & Medical Research Council Senior Principal Research Fellow

Achievements

1991 Wellcome Trust Senior Research Fellowship
1994 University of Melbourne Selwyn-Smith Medical Research Prize
1996 ASBMB Boehringer-Mannheim Medallist
1997 Australian Research Council Senior Research Fellowship
1999 Gottschalk Medal of the Australian Academy of Science
2001 NHMRC Senior Principal Research Fellowship
2004 GE Healthcare Bio-Sciences Award of the ASBMB
2006 Australian Research Council Federation Fellowship
2006 NHMRC Senior Principal Research Fellowship
2010 Fellow of the Australian Academy of Science
2011 ASBMB Lemberg Medal
2011 NHMRC Senior Principal Research Fellowship
2011 Ramaciotti Medal for Excellence in Biomedical Research
2012 Federation of Asian and Oceanian Biochemists and Molecular Biologists Award for Research Excellence
2014 NHMRC Research Excellence Award for top ranked Program grant application
2015 Fellow of the Australian Academy of Health and Medical Sciences
2016 NHMRC Senior Principal Research Fellowship
2016 Bob Robertson Award of the Australian Society for Biophysics for outstanding contributions to biophysics in Australia and New Zealand

Research Interests

Protein crystallography; structure-based drug design; cancer; infection; neurobiology
The ACRF Rational Drug Discovery Centre is focused on three disease areas: cancer, infection (bacterial toxins, parasites and viruses) and neurological diseases (Alzheimer's disease, memory loss, epilepsy, anxiety). Our aim is to understand the function of key proteins at a molecular level and to discover small molecules that alter the function of these proteins which may then be developed into clinically useful drugs. The lab uses a wide array of platform technologies including molecular biology, protein chemistry, protein characterisation tools, X-ray crystallography (including the Australian Synchrotron), electrophysiology, virtual screening and structure-based drug design.

Selected Publications

  1. Parker, M.W., Pattus, F., Tucker, A.D. & Tsernoglou, D. (1989) Structure of the membrane-pore-forming fragment of colicin A. Nature 337, 93-96.
  2. Parker, M.W., Buckley, J.T., Postma, J.P., Tucker, A.D., Leonard, K., Pattus, F. & Tsernoglou, D. (1994) Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367, 292-295.
  3. Hu, S.H., Parker, M.W., Lei, J.Y., Wilce, M.C., Benian, G.M. & Kemp, B.E.  (1994) Insights into autoregulation from the crystal structure of twitchin kinase. Nature 369, 581-584.
  4. Rossjohn, J., Feil, S.C., McKinstry, W.J., Tweten, R.K. & Parker, M.W. (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89, 685-692.
  5. Rossjohn, J., Cappai, R., Feil, S.C., Henry, A., McKinstry, W.J., Galatis, D., Hesse, L., Multhaup, G., Beyreuther, K., Masters, C.L. & Parker, M.W. (1999) Crystal structure of the N-terminal, growth factor-like domain of Alzheimer's amyloid precursor protein. Nature Struct. Biol. 6, 327-331.
  6. Barnham, K.J., McKinstry, W.J., Multhaup, G., Galatis, D., Morton, C.J., Curtain, C.C., Williamson, N.A., White, A.R., Hinds, M.G., Norton, R.S., Beyreuther, K., Masters, C.L., Parker, M.W. & Cappai, R. (2003) Structure of the Alzheimer’s disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. J. Biol. Chem. 278, 17401-17407.
  7. Brown, R.J., Adams, J.J., Pelekanos, R.A., Wan Y., McKinstry, W.J., Palethorpe, K., Seeber, R.M., Monks, T.A., Eidne, K.A., Parker, M.W. & Waters, M.J. (2005) Model for growth hormone receptor activation based on subunit rotation within a receptor dimer. Nature Struct. Mol. Biol.  12, 814-821.
  8. Albiston, A.L., Morton, C.J., Ng, H.L., Pham, V., Yeatman, H.R., Ye, S., Fernando, R.N., De Bundel, D., Ascher, D.B., Mendelsohn, F.A.O., Parker, M.W. & Chai, S.Y. (2008) Identification and characterization of a new cognitive enhancer based on inhibition of insulin-regulated aminopeptidase. FASEB J. 12, 4209-4217.
  9. Hansen, G., Hercus, T.R., McClure, B.J., Stomski, F.C., Dottore, M., Powell, J., Ramshaw, H., Woodcock, J.M., Xu, Y., Guthridge, M., McKinstry, W.J., Lopez, A.F. & Parker, M.W. (2008) The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation. Cell 134, 496-507.
  10. Miles, L.A., Crespi, G.A.N., Doughty. L. & Parker, M.W. (2013) Bapineuzumab captures the N-terminus of the Alzheimer’s disease amyloid-beta peptide in a helical conformation. Sci. Rep. 3, 1302; DOI:10.1038/srep01302.
  11. Bennetts, B. & Parker, M.W. (2013) Molecular determinants of common gating of a CIC chloride channel. Nature Commun. 4, 3507.
  12. Brooks, A.J., Dai, W., O’Mara, M.L., Abankwa, D., Chabra, Y., Pelekanos, R.A., Gardon, O., Tunny, K.A., Blucher, K.M., Morton, C.J., Parker, M.W., Sierecki, E., Gambin, Y., Alexandrov, K., Wilson, I.A., Doxastakis, M., Mark, A.E. & Waters, M.J. (2014) A new cytokine receptor activation paradigm: activation of JAK2 by the Growth Hormone Receptor. A mechanism for activation of JAK2 by the growth hormone receptor. Science, 344, 710, 1249783-1-1249783-12.
  13. Morton, C.J., Nero, T.N., Holien, J.K., Wielens, J. & Parker, M.W. (2014) Oncogenic protein interfaces: small molecules, big challenges. Nature Revs. Cancer, 14, 248-262.
  14. Ascher, D.B., Wielens, J., Nero, T.L., Morton, C.J. & Parker, M.W. (2014) Potent hepatitis inhibitors bind directly to NS5A and reduce its affinity for RNA. Sci. Reps, 4, 4765.
  15. Watt, A.D., Crespi, G.A.N., Down, R.A., Ascher, D.B., Gunn, A., Perez, K.A., McLean, C.A., Villemagne, V.L., Parker, M.W., Barnham, K.J. & Miles, L.A. (2014) Do current therapeutic anti-Abeta antibodies for Alzheimer’s disease engage the target? Acta Neuropathol. 127, 803-810.
  16. Broughton, S.E., Hercus, T.R., Hardy, M.P., McClure, B.J., Nero, T.L., Dottore, M., Huynh, H., Braley, H., Barry, E.F., Kan, W.L., Dhagat, U., Scotney, P., Hartman, D., Busfield, S.J., Owczarek, C.M., Nash, A.D., Wilson, N.J., Parker, M.W. & Lopez, A.F. (2014) Dual mechanism of IL-3 receptor blockade by an anti-cancer antibody. Cell Rep. 8, 410-419.
  17. Crespi, G.A.N., Hermans, S.J., Parker, M.W.* & Miles, L.A.* (*Joint senior authors) (2015) Molecular basis for mid-region amyloid-beta capture by leading Alzheimer’s disease immunotherapies. Sci. Reps.5, 9649.