Jade Forwood

B.Biomed Sc. (Hons 1), James Cook University, 1997.
Ph.D. John Curtin School of Medical Research, Australian National University, 2002

Professor in Biochemistry
Wagga Wagga
Building 288 Room 216

Dr Forwood completed a BBiomedSc. (Hons I) at James Cook University and a PhD in Biochemistry and Molecular Biology at the John Curtin School of Medical Research (Australian National University). He was awarded a University Medal in 1998 and the Frank Fenner Medal in 2002 for most outstanding PhD thesis. Since completing his PhD, he undertook postdoctoral research in industry (Bresagen Ltd., Adelaide University), and under an NHMRC CJ Martin Fellowship, conducted research at the Department of Structural Studies in Cambridge (UK) for two years, followed by an additional two years at the University of Queensland. In 2007, he joined the School of Biomedical Sciences at Charles Sturt University to coordinate and lecture in Biochemistry. He has secured 18 research grants totalling more than $32 million (c. half as CIA), including grants from highly competitive national and international funding sources.

In 2009 he was awarded an international research grant from the Association Francaise contre les Myopathies (AFM, French Muscular Dystrophy Association), a granting body that funds only a very small number of grants per year outside Europe. In 2011 he was awarded an NHMRC Project Grant for 2012-2014 as sole CI; 2012 was CI on an NHMRC grant ~470K/3 years. He was the recipient of a Travel Award to attend the American Society of Cell Biology Conference in San Francisco; a highly competitive CJ Martin Fellowship (2002-2006); a Centre for Inland Health Research Fellowship (2009); Vice-Chancellors Award for Research Excellence (2012); Federation of Asian and Oceanian Biochemists and Molecular Biologists Young Scientist Award (under 35 years of age) (2012); ARC Future Fellowship (2013-2016); and Travel Award to attend the 13th FAOBMB Congress in Bangkok, Thailand (2012).

His research interests are medical biochemistry, molecular biology and pharmacology. Projects include sex determination and mutations with SRY that lead to genetic sex reversal in humans, nucleocytoplasmic transport of proteins involved in gene regulation, non-viral gene-therapy, and techniques to characterise protein-protein interactions including x-ray crystallography. He has conducted research on proteins responsible for replicating the Dengue virus genome, proteins involved in gene regulation and their application for gene therapy, neuralisation of stem cells, and crystallographic structure determination of proteins involved in colon cancer, development, macrophage activation, lipid metabolism, and the nucleocytoplasmic transport process. This work has been published in a number of journals including Proc Natl Acad Sci USA, Plant Cell, J Biol Chem, Proteins and Biochemistry and a number of book chapters. Please click on publications for details.


Teaching philosophy

Dr Forwood's primary teaching philosophy is to provide a stimulating and innovative teaching environment and to facilitate students to develop life-long learning practices. His approach includes offering a range of complementary and engaging learning resources, applying a range of subject specific pedagogies, and use of student and peer-reviewed evaluations and critical reflection to continually improve my teaching skills.

Current subjects taught
  • Biochemistry
  • Protein biochemistry


Please see my personal website:


Top 10 career-best Publications (click below for full list)

^ denotes publications as corresponding author

  1. *^Forwood JK, Thakur AS, Guncar G, Marfori M, Mouradov D, Meng W, Robinson J, Huber T, Kellie S, Martin JL, Hume DA, Kobe B. Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation. . Proceedings of the National Academy of Sciences of the United States of America. 2007; 104(25):10382-10387. [ISI Web of Science Journal Citation Reports (JCR) 5-year Impact Factor 10.6. A highly innovative approach utilising, chemical crosslinking, mass spectrometry, molecular modelling and x-ray crystallography to determine the structure and juxtaposition of six domains within Acot7.
  2. *^Kirkby B, Roman N, Kobe B, Kellie S, Forwood JK. Functional and Structural Properties of Mammalian Acyl-Coenzyme A Thioesterases. Progress in Lipid Research. 2010; 49(4):366-77. [JCR 5-year Impact Factor 11.7]. Described the structural and functional relationships within type-I and type-II acyl-CoA thioesterases. Prog in Lipid Research is a leading journal in the field of lipid research.
  3. *Harley VR, Layfield S, Mitchell CL, Forwood JK, John AP, Briggs LJ, McDowall SG, Jans DA. Defective importin beta recognition and nuclear import of the sex-determining factor SRY are associated with XY sex-reversing mutations. Proceeding of the National Academy of Sciences U.S.A. 2003; 100(12):7045-7050. [JCR 5-year Impact Factor 10.6]. Provided highly significant biological insights into the molecular mechanisms of human genetic sex reversal. A range of XY-sex reversal mutations were analysed using complementary assays to elucidate mechanisms of impaired SRY functionality.
  4. *Wang CA, Guncar G, Forwood JK, Teh T, Catanzariti A, Schirra H, Anderson PA, Ellis JG, Dodds PN, Kobe B. Crystal structures of flax rust avirulence proteins AvrL567-A and AvrL567–D reveal the structural basis for flax disease resistance specificity. Plant Cell 2007; 19(9):2898-2912. [JCR 5-year Impact Factor 10.6]. Provided an enhanced understanding of disease resistance in plants through the structural and characterisation of two avirulence proteins. The  journal Plant Cell has ranked first among journals publishing primary research in the plant sciences for the past 17 years.
  5. *^Forwood JK, Lange A, Zachariae U, Marfori M, Preast C, Grubm├╝ller H, Stewart M, Corbett AH, Kobe B. Quantitative Structural Analysis of Importin-╬▓ Flexibility: Paradigm for Solenoid Protein Structures. Structure. 2010; 18(9):1171-83. [JCR 5-year Impact Factor 5.9]. Described the first full-length structure of the nuclear import receptor importin beta in its unbound form. The flexibility and size of this receptor (861 amino acids) had eluded the crystallographic field for many years. The structure revealed important insights into the mechanism of nuclear transport.
  6. *^Marfori M, Kobe B, Forwood JK. Ligand-induced conformational changes within a hexameric Acyl-CoA thioesterase. Journal of Biological Chemistry. 2011; 286(41):35643-9. [JCR 5-year Impact Factor 5.5. Described the first structure of an apo-thioesterase and ligand induced changes within the thioesterase enzyme family and novel insights into regulation.
  7. *Forwood JK, Harley V, Jans DA. The C-terminal nuclear localization signal of the sex-determining region Y (SRY) high mobility group domain mediates nuclear import through importin beta 1. Journal of Biological Chemistry 2001; 276(49):46575-46582. [JCR 5-year Impact Factor 5.5]. Elucidated the mechanism of nuclear translocation of SRY to provide an enhanced understanding of sex determination during human embryonic development. Work presented at the American Society of Cell Biology (ASCB) conference in 2001 under an ASCB travel award.
  8. *^Forwood JK, Lonhienne TG, Marfori M, Robin G, Meng W, Guncar G, Liu SM, Stewart M, Carroll BJ, Kobe B. Kap95p Binding Induces the Switch Loops of RanGDP to Adopt the GTP-Bound Conformation: Implications for Nuclear Import Complex Assembly Dynamics. Journal of Molecular Biology. 2008; 383:772-82. [JCR 5-year Impact Factor 4.1]. Described the structure of the nuclear import receptor importin-beta with Ran in its GDP bound form. Provided important insights into how the highly flexible switch regions within Ran can mediate directionality of nuclear import through binding to importin-beta.
  9. *Lonhienne TG**, Forwood JK**, Marfori M, Robin G, Kobe B, Carroll BJ. Importin-beta is a GDP-TO-GTP exchange factor of RAN: Implications for the mechanism of nuclear import. Journal of Biological Chemistry. 2009; 284(34):22549-58  **Joint first authors. [JCR 5-year Impact Factor 5.5]. This paper described a new nucleotide exchange factor for Ran, and implications for how the differential nucleotide bound state across the nuclear envelope can mediate directionality of nuclear transport.
  10. *Forwood JK, Jans DA. Nuclear import pathway of the telomere elongation suppressor TRF1: inhibition by importin alpha. Biochemistry 2002; 41(30):9333-9340. [JCR 5-year Impact Factor 3.2]. This research provided important insights into the Ran-dependent mechanism through which TRF1 is transported across the nuclear envelope. Quantitative approaches were utilised to assess the rate of nuclear accumulation and affinity for nuclear import receptors.

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