Structural Chemistry

, Volume 21, Issue 5, pp 1117–1129 | Cite as

Merging structural biology with chemical biology: Structural Chemistry at Eskitis

  • Andreas Hofmann
  • Conan K. Wang
  • Asiah Osman
  • David Camp
Review Article

Abstract

This review introduces the Structural Chemistry Program at Griffith University’s Eskitis Institute, and provides a brief overview over its current and future research portfolio. Capitalising on the co-location with the Queensland Compound Library (QCL), Australia’s only small molecule repository, our laboratory investigates the structure and function of proteins with the aim of learning about their molecular mechanisms. Consequently, these studies also feed into drug discovery and design. The thematic focus of our Program is on proteins involved in infection, inflammation and neurological diseases, and this review highlights a few of our recent research efforts in this area.

Keywords

Molecular mechanisms Protein crystallography Protein structure–function Rational drug design 

Notes

Acknowledgments

Research in the Structural Chemistry Program is funded by the Australian Research Council, Griffith University, the James N Kirby Foundation, the National Health and Medical Research Council (Fellowship to CKW) and the Rebecca L Cooper Foundation. We gratefully acknowledge the Australian Synchrotron for beam time awards. Funding to establish the QCL was received from Griffith University and the Queensland State Government's Department of Employment, Economic Development and Innovation. Further support has been received from the Agilent Foundation and Prostate Cancer foundation of Australia.

References

  1. 1.
    Hofmann A, Wlodawer A (2002) PCSB—a program collection for structural biology and biophysical chemistry. Bioinformatics 18:209–210CrossRefGoogle Scholar
  2. 2.
    Hofmann A (2008) ACDP—a Java application for data processing and analysis of protein circular dichroism spectra. J Appl Crystallogr 42:137–139CrossRefGoogle Scholar
  3. 3.
    Dobson CM (2004) Chemical space and biology. Nature 432:824–828CrossRefGoogle Scholar
  4. 4.
    Buskirk AR, Liu DR (2005) Creating small-molecule-dependent switches to modulate biological functions. Chem Biol 12:151–161CrossRefGoogle Scholar
  5. 5.
    Stockwell BR (2004) Exploring biology with small organic molecules. Nature 432:846–854CrossRefGoogle Scholar
  6. 6.
    Bohacek RS, McMartin C, Guida WC (1996) The art and practice of structure-based drug design: a molecular modeling perspective. Med Res Rev 16:3–50CrossRefGoogle Scholar
  7. 7.
    Spring DR (2003) Diversity-oriented synthesis; a challenge for synthetic chemists. Org Biomol Chem 1:3867–3870CrossRefGoogle Scholar
  8. 8.
    Newman DJ, Cragg GM (2007) Natural products as sources of new drugs over the last 25 years. J Nat Prod 70:461–477CrossRefGoogle Scholar
  9. 9.
    Lipinski C, Lombardo F, Dominy B, Feeney P (1997) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 23:3–25CrossRefGoogle Scholar
  10. 10.
    Leeson P, Davis A, Steele J (2004) Drug-like properties: guiding principles for design-or chemical prejudice? Drug Discov Today Technol 1:189–195CrossRefGoogle Scholar
  11. 11.
    Teague SJ, Davis AM, Leeson PD, Oprea T (1999) The design of leadlike combinatorial libraries. Angew Chem Int Ed Engl 38:3743–3747CrossRefGoogle Scholar
  12. 12.
    Hann MM, Oprea TI (2004) Pursuing the leadlikeness concept in pharmaceutical research. Curr Opin Chem Biol 8:255–263CrossRefGoogle Scholar
  13. 13.
    Leeson PD, Davis AM (2004) Time-related differences in the physical property profiles of oral drugs. J Med Chem 47:6338–6348CrossRefGoogle Scholar
  14. 14.
    Ganesan A (2008) The impact of natural products upon modern drug discovery. Curr Opin Chem Biol 12:306–317CrossRefGoogle Scholar
  15. 15.
    Lipinski CA, Hopkins A (2004) Navigating chemical space for biology and medicine. Nature 432:855–861CrossRefGoogle Scholar
  16. 16.
    Bredel M, Jacoby E (2004) Chemogenomics: an emerging strategy for rapid target and drug discovery. Nat Rev Genet 5:262–275CrossRefGoogle Scholar
  17. 17.
    Golebiowski A, Klopfenstein SR, Portlock DE (2001) Lead compounds discovered from libraries. Curr Opin Chem Biol 5:273–284CrossRefGoogle Scholar
  18. 18.
    Prien O (2005) Target-family-oriented focused libraries for kinases—conceptual design aspects and commercial availability. ChemBioChem 6:500–505CrossRefGoogle Scholar
  19. 19.
    Player MR (2004) Target-based compound library design and synthesis. Drug Discov Today Targets 3:48–50CrossRefGoogle Scholar
  20. 20.
    De Simone RW, Currie KS, Mitchell SA, Darrow JW, Pippin DA (2004) Privileged structures: applications in drug discovery. Comb Chem High Throughput Screen 7:473–493Google Scholar
  21. 21.
    Burke MD, Berger EM, Schreiber SL (2003) Generating diverse skeletons of small molecules combinatorially. Science 302:613–618CrossRefGoogle Scholar
  22. 22.
    Fergus S, Bender A, Spring DR (2005) Assessment of structural diversity in combinatorial synthesis. Curr Opin Chem Biol 9:304–309CrossRefGoogle Scholar
  23. 23.
    Camp D (2007) Establishment of an open access compound management facility in Australia to stimulate applied, basic and translational biomedical research. Drug Discov World 8:61–66Google Scholar
  24. 24.
    Camp D, Avery VM, Street I, Quinn RJ (2007) Progress towards establishing an open access molecular screening capability in the Australasian region. ACS Chem Biol 2:764–767CrossRefGoogle Scholar
  25. 25.
    Mueller D, Davis RA, Duffy S, Avery VM, Camp D, Quinn RJ (2009) Antimalarial activity of azafluorenone alkaloids from the Australian tree Mitrephora diversifolia. J Nat Prod 72:1538–1540CrossRefGoogle Scholar
  26. 26.
    Davis RA, Duffy S, Avery VM, Camp D, Hooper JNA, Quinn RJ (2010) (+)-7-Bromotrypargine, an antimalarial beta-carboline from the Australian marine Sponge, Ancorina sp. Tetrahedron Lett 51:583–585CrossRefGoogle Scholar
  27. 27.
    Feng Y, Davis RA, Sykes ML, Avery VM, Camp D, Quinn RJ (2010) Antitrypanosomal cyclic polyketide peroxides from the Australian marine sponge Plakortis sp. J Nat Prod 73:716–719CrossRefGoogle Scholar
  28. 28.
    Feng Y, Davis RA, Sykes ML, Avery VM, Carroll AR, Camp D, Quinn RJ (2010) Antitrypanosomal pyridoacridine alkaloids from the Australian ascidian, Polysyncraton echinatum. Tetrahedron Lett 51:2477–2479CrossRefGoogle Scholar
  29. 29.
    Yang X, Davis RA, Buchanan MS, Duffy S, Avery VM, Camp D, Quinn RJ (2010) Antimalarial bromotyrosine derivatives from the Australian marine sponge Hyattella sp. J Nat Prod 73:985–987CrossRefGoogle Scholar
  30. 30.
    Lopez M, Paul B, Hofmann A, Innocenti A, Vullo D, Supuran C, Poulsen S (2009) S-glycosyl primary sulfonamides—a new structural class for selective inhibition of cancer-associated carbonic anhydrases. J Med Chem 52:6421–6432CrossRefGoogle Scholar
  31. 31.
    Besier B (2007) New anthelmintics for livestock: the time is right. Trends Parasitol 23:21–24CrossRefGoogle Scholar
  32. 32.
    Kutz S, Dobson A, Hoberg E (2009) Where are the parasites? Science 326:1187–1188CrossRefGoogle Scholar
  33. 33.
    Cantacessi C, Campbell BE, Visser A, Geldhof P, Nolan MJ, Nisbet AJ, Matthews JB, Loukas A, Hofmann A, Otranto D et al (2009) A portrait of the “SCP/TAPS” proteins of eukaryotes—developing a framework for fundamental research and biotechnological outcomes. Biotechnol Adv 27:376–388CrossRefGoogle Scholar
  34. 34.
    Hanks SK, Quinn AM, Hunter T (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241:42–52CrossRefGoogle Scholar
  35. 35.
    Barford D, Das A, Egloff M (1998) The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu Rev Biophys Biomol Struct 27:133–164CrossRefGoogle Scholar
  36. 36.
    Hu M, Abs El-Osta YG, Campbell BE, Boag PR, Nisbet AJ, Beveridge I, Gasser RB (2007) Trichostrongylus vitrinus (Nematoda: Strongylida): molecular characterisation and transcriptional analysis of Tv-stp-1, a serine/threonine phosphatase gene. Exp Parasitol 117:22–34CrossRefGoogle Scholar
  37. 37.
    Campbell B, Rabelo E, Hofmann A, Hu M, Gasser R (2010) Characterization of a Caenorhabditis elegans glc seven-like phosphatase (gsp) orthologue from Haemonchus contortus (Nematoda). Mol Cell Probes (in press)Google Scholar
  38. 38.
    Campbell BE, McCluskey A, Hofmann A, Gasser R (2010) Serine/threonine phosphatases in socioeconomically important parasitic nematodes—prospects as novel drug targets? Biotechnol Adv (in press)Google Scholar
  39. 39.
    Nolan MJ, Hofmann A, Jex AR, Gasser RB (2010) A theoretical study to establish the relationship between the three-dimensional structure of triose-phosphate isomerase of Giardia duodenalis and point mutations in the respective gene. Mol Cell Probes (in press)Google Scholar
  40. 40.
    Loukas A, Bethony J, Brooker S, Hotez P (2006) Hookworm vaccines: past, present, and future. Lancet Infect Dis 6:733–741CrossRefGoogle Scholar
  41. 41.
    Muchowski PJ, Zhang L, Chang ER, Soule HR, Plow EF, Moyle M (1994) Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18. J Biol Chem 269:26419–26423Google Scholar
  42. 42.
    Asojo OA, Goud G, Dhar K, Loukas A, Zhan B, Deumic V, Liu S, Borgstahl GEO, Hotez PJ (2005) X-ray structure of Na-ASP-2, a pathogenesis-related-1 protein from the nematode parasite, Necator americanus, and a vaccine antigen for human hookworm infection. J Mol Biol 346:801–814CrossRefGoogle Scholar
  43. 43.
    Henriksen A, King TP, Mirza O, Monsalve RI, Meno K, Ipsen H, Larsen JN, Gajhede M, Spangfort MD (2001) Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins 45:438–448CrossRefGoogle Scholar
  44. 44.
    Fernández C, Szyperski T, Bruyère T, Ramage P, Mösinger E, Wüthrich K (1997) NMR solution structure of the pathogenesis-related protein P14a. J Mol Biol 266:576–593CrossRefGoogle Scholar
  45. 45.
    Hofmann A, Zdanov A, Genschik P, Ruvinov S, Filipowicz W, Wlodawer A (2000) Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction. EMBO J 19:6207–6217CrossRefGoogle Scholar
  46. 46.
    Hofmann A, Huber R (2003) Structural conservation and functional versatility: allostery as a common annexin feature. In: Bandorowicz-Pikula J (ed) Annexins: biological importance and annexin-related pathologies. Landes Bioscience, GeorgetownGoogle Scholar
  47. 47.
    Sopkova J, Renouard M, Lewit-Bentley A (1993) The crystal structure of a new high-calcium form of annexin V. J Mol Biol 234:816–825CrossRefGoogle Scholar
  48. 48.
    Pathuri P, Nguyen ET, Svard SG, Luecke H (2007) Apo and calcium-bound crystal structures of alpha-11 giardin, an unusual annexin from Giardia lamblia. J Mol Biol 368:493–508CrossRefGoogle Scholar
  49. 49.
    Pathuri P, Nguyen ET, Ozorowski G, Svärd SG, Luecke H (2009) Apo and calcium-bound crystal structures of cytoskeletal protein alpha-14 giardin (annexin E1) from the intestinal protozoan parasite Giardia lamblia. J Mol Biol 385:1098–1112CrossRefGoogle Scholar
  50. 50.
    Hofmann A (2004) Annexins in the plant kingdom—perspectives and potentials. Annexins 1:51–61Google Scholar
  51. 51.
    Dabitz N, Hu NJ, Yusof AM, Tranter N, Winter A, Daley M, Zschörnig O, Brisson A, Hofmann A (2005) Structural determinants for plant annexin-membrane interactions. Biochemistry 44:16292–16300CrossRefGoogle Scholar
  52. 52.
    Hu N, Yusof A, Winter A, Osman A, Reeve A, Hofmann A (2008) The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum indicates different mechanisms of membrane binding in plant and animal annexins. J Biol Chem 283:18314–18322CrossRefGoogle Scholar
  53. 53.
    Winter A, Yusof AM, Gao E, Yan HL, Hofmann A (2006) Biochemical characterization of annexin B1 from Cysticercus cellulosae. FEBS J 273:3238–3247CrossRefGoogle Scholar
  54. 54.
    Römisch J, Heimburger N (1990) Purification and characterization of six annexins from human placenta. Biol Chem Hoppe Seyler 371:383–388Google Scholar
  55. 55.
    Weiland M, Palm J, Griffiths W, McCaffery J, Svärd S (2003) Characterisation of alpha-1 giardin: an immunodominant Giardia lamblia annexin with glycosaminoglycan-binding activity. Int J Parasitol 33:1341–1351CrossRefGoogle Scholar
  56. 56.
    Capila I, Hernaiz M, Mo Y, Mealy T, Campos B, Dedman J, Linhardt R, Seaton B (2001) Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surface. Structure 9:57–64CrossRefGoogle Scholar
  57. 57.
    Hofmann A, Osman A, Leow CY, Driguez P, Jones M (2010) Parasite annexins—new molecules with potential for drug and vaccine development. BioEssays (in press)Google Scholar
  58. 58.
    Kaneko N, Ago H, Matsuda R, Inagaki E, Miyano M (1997) Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor. J Mol Biol 274:16–20CrossRefGoogle Scholar
  59. 59.
    Hofmann A, Escherich A, Lewit-Bentley A, Benz J, Raguenes-Nicol C, Russo-Marie F, Gerke V, Moroder L, Huber R (1998) Interactions of benzodiazepine derivatives with annexins. J Biol Chem 273:2885–2894CrossRefGoogle Scholar
  60. 60.
    Parente L, Solito E (2004) Annexin 1: more than an anti-phospholipase protein. Inflamm Res 53:125–132CrossRefGoogle Scholar
  61. 61.
    Meers P, Mealy T, Pavlotsky N, Tauber AI (1992) Annexin I-mediated vesicular aggregation: mechanism and role in human neutrophils. Biochemistry 31:6372–6382CrossRefGoogle Scholar
  62. 62.
    Bitto E, Li M, Tikhonov AM, Schlossman ML, Cho W (2000) Mechanism of annexin I-mediated membrane aggregation. Biochemistry 39:13469–13477CrossRefGoogle Scholar
  63. 63.
    Streicher WW, Lopez MM, Makhatadze GI (2009) Annexin I and annexin II n-terminal peptides binding to s100 protein family members: specificity and thermodynamic characterization. Biochemistry 48:2788–2798CrossRefGoogle Scholar
  64. 64.
    Hu N, Bradshaw J, Lauter H, Buckingham J, Solito E, Hofmann A (2008) Membrane-induced folding and structure of membrane-bound annexin A1 N-terminal peptides—implications for annexin-induced membrane aggregation. Biophys J 94:1773–1781CrossRefGoogle Scholar
  65. 65.
    Burgoyne R (2007) Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling. Nat Rev Neurosci 8:182–193CrossRefGoogle Scholar
  66. 66.
    Genin A, Davis S, Meziane H, Doyere V, Jeromin A, Roder J, Mallet J, Laroche S (2001) Regulated expression of the neuronal calcium sensor-1 gene during long-term potentiation in the dentate gyrus in vivo. Neuroscience 106:571–577CrossRefGoogle Scholar
  67. 67.
    Braunewell K, Brackmann M, Manahan-Vaughan D (2003) Group I mGlu receptors regulate the expression of the neuronal calcium sensor protein VILIP-1 in vitro and in vivo: implications for mGlu receptor-dependent hippocampal plasticity. Neuropharmacology 44:707–715CrossRefGoogle Scholar
  68. 68.
    Kabbani N, Negyessy L, Lin R, Goldman-Rakic P, Levenson R (2002) Interaction with neuronal calcium sensor NCS-1 mediates desensitization of the D2 dopamine receptor. J Neurosci 22:8476–8486Google Scholar
  69. 69.
    Bahi N, Friocourt G, Carrié A, Graham ME, Weiss JL, Chafey P, Fauchereau F, Burgoyne RD, Chelly J (2003) IL1 receptor accessory protein like, a protein involved in X-linked mental retardation, interacts with Neuronal Calcium Sensor-1 and regulates exocytosis. Hum Mol Genet 12:1415–1425CrossRefGoogle Scholar
  70. 70.
    Cheng HM, Pitcher GM, Laviolette SR, Whishaw IQ, Tong KI, Kockeritz LK, Wada T, Joza NA, Crackower M, Goncalves J et al (2002) DREAM is a critical transcriptional repressor for pain modulation. Cell 108:31–43CrossRefGoogle Scholar
  71. 71.
    Mahloogi H, Gonzalez-Guerrico AM, Lopez De Cicco R, Bassi DE, Goodrow T, Braunewell KH, Klein-Szanto AJ (2003) Overexpression of the calcium sensor visinin-like protein-1 leads to a cAMP-mediated decrease of in vivo and in vitro growth and invasiveness of squamous cell carcinoma cells. Cancer Res 63:4997–5004Google Scholar
  72. 72.
    Heo WD, Inoue T, Park WS, Kim ML, Park BO, Wandless TJ, Meyer T (2006) PI(3, 4, 5)P3 and PI(4, 5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314:1458–1461CrossRefGoogle Scholar
  73. 73.
    Czech MP (2000) PIP2 and PIP3: complex roles at the cell surface. Cell 100:603–606CrossRefGoogle Scholar
  74. 74.
    Tang K, Hofmann A, Freund C, Danker K (2009) The cytoplasmic tail of the alpha1 integrin subunit associates with phosphoinositides. SubmittedGoogle Scholar
  75. 75.
    O’Callaghan DW, Haynes LP, Burgoyne RD (2005) High-affinity interaction of the N-terminal myristoylation motif of the neuronal calcium sensor protein hippocalcin with phosphatidylinositol 4,5-bisphosphate. Biochem J 391:231–238CrossRefGoogle Scholar
  76. 76.
    Braunewell KH, Brackmann M, Hofmann A (2006) VILIP-1, a novel regulator of the guanylate cyclase transduction system in neurons. Calcium Bind Proteins 1:12–15Google Scholar
  77. 77.
    Brackmann M, Hofmann A, Braunewell KH (2006) Structure, function and expression of members of the vilip (visinin-like protein) subfamily of neuronal calcium sensor proteins. In: Philippov P, Koch K (eds) Neuronal calcium sensor proteins. Nova Science Publisher, HauppaugeGoogle Scholar
  78. 78.
    Braunewell K, Paul B, Altarche-Xifro W, Noack C, Lange K, Hofmann A (2010) Interactions of Visinin-like proteins with phospho-inositides. Aust J Chem 63:350–356CrossRefGoogle Scholar
  79. 79.
    Krylov D, Hurley J (2001) Identification of proximate regions in a complex of retinal guanylyl cyclase 1 and guanylyl cyclase-activating protein-1 by a novel mass spectrometry-based method. J Biol Chem 276:30648–30654CrossRefGoogle Scholar
  80. 80.
    Chen K, Wang L, Chang L (2009) Regulatory elements and functional implication for the formation of dimeric visinin-like protein-1. J Pept Sci 15:89–94CrossRefGoogle Scholar
  81. 81.
    McArdle B, Hofmann A (2008) Coronin structure and implications. In: Clemen C, Eichinger L, Rybakin V (eds) The coronin family of proteins. Landes Bioscience, AustinGoogle Scholar
  82. 82.
    Hudson AM, Cooley L (2008) Phylogenetic, structural and functional relationships between WD- and Kelch-repeat proteins. Subcell Biochem 48:6–19CrossRefGoogle Scholar
  83. 83.
    Smith TF (2008) Diversity of WD-repeat proteins. Subcell Biochem 48:20–30CrossRefGoogle Scholar
  84. 84.
    Smith TF, Gaitatzes C, Saxena K, Neer EJ (1999) The WD repeat: a common architecture for diverse functions. Trends Biochem Sci 24:181–185CrossRefGoogle Scholar
  85. 85.
    Li D, Roberts R (2001) WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. Cell Mol Life Sci 58:2085–2097CrossRefGoogle Scholar
  86. 86.
    Appleton B, Wu P, Wiesmann C (2006) The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes. Structure 14:87–96CrossRefGoogle Scholar
  87. 87.
    de Hostos EL (1999) The coronin family of actin-associated proteins. Trends Cell Biol 9:345–350CrossRefGoogle Scholar
  88. 88.
    Rybakin V, Clemen C (2005) Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking. BioEssays 27:625–632CrossRefGoogle Scholar
  89. 89.
    Rosentreter A, Hofmann A, Xavier CP, Stumpf M, Noegel AA, Clemen CS (2007) Coronin 3 involvement in F-actin-dependent processes at the cell cortex. Exp Cell Res 313:878–895CrossRefGoogle Scholar
  90. 90.
    Gatfield J, Albrecht I, Zanolari B, Steinmetz M, Pieters J (2005) Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules. Mol Biol Cell 16:2786–2798CrossRefGoogle Scholar
  91. 91.
    Gandhi M, Goode B (2008) Coronin: the double-edged sword of actin dynamics. In: Clemen C, Eichinger L, Rybakin V (eds) The coronin family of proteins. Landes Bioscience, GeorgetownGoogle Scholar
  92. 92.
    Xavier C, Rosentreter A, Reimann J, Cornfine S, Linder S, van Vliet V, Hofmann A, Morgan RO, Fernandez M, Stumpf M et al (2009) Structural and functional diversity of novel coronin-1C (CRN2) isoforms. J Mol Biol 393:287–299CrossRefGoogle Scholar
  93. 93.
    Cai L, Holoweckyj N, Schaller M, Bear J (2005) Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility. J Biol Chem 280:31913–31923CrossRefGoogle Scholar
  94. 94.
    Spoerl Z, Stumpf M, Noegel AA, Hasse A (2002) Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus. J Biol Chem 277:48858–48867CrossRefGoogle Scholar
  95. 95.
    Schutt CE, Lindberg U (2000) The new architectonics: an invitation to structural biology. Anat Rec 261:198–216CrossRefGoogle Scholar
  96. 96.
    DeLano W (2002) The PyMOL Molecular Graphics System. http://www.pymol.org

Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Andreas Hofmann
    • 1
  • Conan K. Wang
    • 1
  • Asiah Osman
    • 1
  • David Camp
    • 2
  1. 1.Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith UniversityNathanAustralia
  2. 2.Queensland Compound Library, Eskitis Institute for Cell and Molecular Therapies, Griffith UniversityNathanAustralia

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