2012-Present ARC Future Fellow, School of Biological Sciences, University of Wollongong 2013-Present Assoc Professor, School of Biological Sciences, University of Wollongong 2011-2012 Senior Lecturer, School of Biological Sciences, University of Wollongong 2009-2010 Lecturer, School of Biological Sciences, University of Wollongong 2005-2009 NHMRC Peter Doherty Fellow, School of Chemistry and Physics, University of Adelaide 2003-2004 Post-doctoral Fellow, Institut National de la Recherche Agronomique (INRA), Tours-Nouzilly, France 2000-2003 PhD, School of Environmental and Life Sciences, University of Newcastle

The cellular heat shock response and molecular chaperones Proteostasis and the role of the small heat shock family of molecular chaperones in this process. The structure-function relationship of small heat shock proteins Protein aggregation and its association with diseases such as Parkinson’s disease. The mechanism by which proteins aggregate and ways in which it can be prevented.

J.J. Yerbury, L. Ooi, A. Dillin, D.N. Saunders, D.M. Hatters, P.M. Beart, N.R. Cashman, M.R. Wilson and H. Ecroyd (2016) Walking the tightrope: Proteostasis and neurodegenerative disease. J Neurochem. doi: 10.1111/jnc.13575. B. Jovcevski, M.A. Kelly, A.P. Rote, T. Berg, H.Y. Gastall, J.L.P. Benesch, J.A. Aquilina and H. Ecroyd (2015) Phosphomimics destabilise Hsp27 oligomeric assemblies and enhance chaperone activity. Chem Biol. 22, 186-195. T.M. Treweek, S. Meehan, H. Ecroyd† and J.A. Carver† (2014) Small heat-shock proteins: important players in regulating cellular proteostasis. Cell Mol Life Sci. 72, 429-451. D. Cox, J.A. Carver and H. Ecroyd (2014) Preventing alpha-synuclein aggregation: The role of the small heat-shock molecular chaperone proteins. BBA – Mol Basis Dis. 1842, 1830-1843. G.K.A. Hochberg†, H. Ecroyd†, C. Liu, D. Cox, D. Cascio, M.R. Sawaya, M.P. Collier, J. Stroud, J.A. Carver, A.J. Baldwin, C.V. Robinson, D.S. Eisenberg, J.L.P. Benesch and A. Laganowsky (2014) The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity. Proc Nat Acad Sci USA. 111, E1562-E1570. K.J. Binger†, H. Ecroyd†, S. Yang, J.A. Carver, G.J. Howlett and M.D. Griffin (2013) Avoiding the oligomeric state: AlphaB-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils. FASEB J. 27, 1214-1222. J.A. Aquilina, S, Shrestha, A.M. Morris and H. Ecroyd (2013) Structural and functional aspects of hetero-oligomers formed by small heat shock proteins alphaB-crystallin and Hsp27. J Biol Chem. 288, 13602-13609. J.J. Yerbury, D. Gower, L. Vanags, K. Roberts, J.A. Lee and H. Ecroyd (2013) The small heat shock proteins alphaB-crystallin and Hsp27 suppress SOD1 aggregation in vitro. Cell Stress Chaperon. 18, 251-257. A.R. Wyatt, J.J. Yerbury, H. Ecroyd and M.R. Wilson (2013) Extracellular chaperones and proteostasis. Annu Rev Biochem. 82, 295-322. M. Kulig and H. Ecroyd (2012) The small heat shock protein alphaB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of alpha-lactalbumin. Biochem J. 448, 343-352. S.L. Shammas, C.A. Waudby, S. Wang, A.K. Buell, H. Ecroyd, M.E. Welland, J.A. Carver, C.M. Dobson and S. Meehan (2011) Binding of the molecular chaperone alphaB-crystallin to amyloid-beta amyloid fibrils inhibits their elongation. Biophys J. 101, 1681-1689. D.M. Williams, H. Ecroyd, K.L. Goodwin, H. Dai, H. Fu, J.M. Woodcock, L. Zhang and J.A. Carver (2011) NMR spectroscopy of 14-3-3zeta reveals a flexible C-terminal extension. Differentiation of the chaperone and phosphoserine binding activities of 14-3-3zeta. Biochem J. 437, 493-503.