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2003 Conference Publication Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthasePang, S. S., Guddat, L. W. and Duggleby, R.G. (2003). Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase. East Coast Protein Meeting, Coffs Harbour, 27-29 June, 2003. |
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2003 Journal Article Systematic characterization of mutations in yeast acetohydroxyacid synthase: Interpretation of herbicide-resistance dataDuggleby, Ronald G., Pang, Siew Siew, Yu, Hongqi and Guddat, Luke W. (2003). Systematic characterization of mutations in yeast acetohydroxyacid synthase: Interpretation of herbicide-resistance data. European Journal of Biochemistry, 270 (13), 2895-2904. doi: 10.1046/j.1432-1033.2003.03671.x |
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2003 Conference Publication The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediateDuggleby, R.G., Pang, S. S., Schowen, R. L. and Guddat, L. W. (2003). The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate. East Coast Protein Meeting, Coffs Harbour, 27-29 June, 2003. |
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2003 Conference Publication Crystal structure and mechanism of a purple acid phosphatase from sweet potato: an enzyme with a novel Fe-Mn binuclear metal centreSchenk, G., Carrington, L., Valizadeh, M., De Jersey, J., Hamilton, S. E. and Guddat, L.W. (2003). Crystal structure and mechanism of a purple acid phosphatase from sweet potato: an enzyme with a novel Fe-Mn binuclear metal centre. International Conference on Biological Inorganic Chemistry, Cairns, 19-23 July, 2003. |
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2002 Journal Article Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniaePang, S. S., Guddat, L. W. and Duggleby, R.G. (2002). Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae. Acta Crystallographica Section D - Biological Crystallography, D58 (7), 1237-1239. doi: 10.1107/S0907444902008132 |
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2002 Journal Article Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic propertiesBourne, P. C., Ramsland, P. A., Shan, L., Fan, Z. C., DeWitt, C. R., Shultz, B. B., Terzyan, S. S., Moomaw, C. R., Slaughter, C. A., Guddat, L. W. and Edmundson, A. B. (2002). Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties. Acta Crystallographica Section D: Biological Crystallography, 58 (5), 815-823. doi: 10.1107/S0907444902004183 |
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2002 Journal Article Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitorsPang, S. S., Duggleby, R. G. and Guddat, L. W. (2002). Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors. Journal of Molecular Biology, 317 (2), 249-262. doi: 10.1006/jmbi.2001.5419 |
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2002 Journal Article Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferaseGuddat, L. W., Vos, S., Martin, J. L., Keough, D. T. and De Jersey, J. (2002). Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase. Protein Science, 11 (7), 1626-1638. doi: 10.1110/ps.0201002 |
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2002 Conference Publication Substrate analogues discriminate between human and Plasmodium falciparum 6-oxopurine phosphoribosyltransferasesKeough, D. T., Dulley, G., Guddat, L. W., Naesens, L. and De Jersey, J. (2002). Substrate analogues discriminate between human and Plasmodium falciparum 6-oxopurine phosphoribosyltransferases. ComBio 2002, Sydney, 29 September - 3 October, 2002. |
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2002 Journal Article Structure of CcmG/DsbE at 1.14 angstrom resolution: High-fidelity reducing activity in an indiscriminately oxidizing environmentEdeling, M. A., Guddat, L. W., Fabianek, R. A., Thony-Meyer, L. and Martin, J. L. (2002). Structure of CcmG/DsbE at 1.14 angstrom resolution: High-fidelity reducing activity in an indiscriminately oxidizing environment. Structure, 10 (7), 973-979. doi: 10.1016/S0969-2126(02)00794-3 |
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2002 Conference Publication Yeast acetohydroxyacid synthase. Crystal structure of an enzyme containing non-catalytic FADPang, S. S., Guddat, L. W. and Duggleby, R.G. (2002). Yeast acetohydroxyacid synthase. Crystal structure of an enzyme containing non-catalytic FAD. 14th Int Symposium on Flavins and Flavoproteins, Cambridge, UK, 14-18 July, 2002. |
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2001 Journal Article Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydroyacid synthasePang, S. S., Guddat, L. W. and Duggleby, R.G. (2001). Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydroyacid synthase. Acta Crystallographica Section D: Biological Crystallography, 57 (9), 1321-1323. doi: 10.1107/S0907444901011635 |
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2001 Journal Article Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE)Edeling, M. A., Guddat, L. W., Fabianek, R. A., Halliday, J. A., Jones, A., Thony-Meyer, L. and Martin, J. L. (2001). Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE). Acta Crystallographica Section D-Biological Crystallography, D57 (9), 1293-1295. doi: 10.1107/S0907444901009982 |
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2001 Conference Publication Structural analysis of the hnRNP A proteins: Understanding the interaction between hnRNP A2 and the A2RE trafficking elementLandsberg, M., Guddat, L. W., Hawkins, B. L. and Smith, R. W. (2001). Structural analysis of the hnRNP A proteins: Understanding the interaction between hnRNP A2 and the A2RE trafficking element. ASBMB, Canberra, 31 Sept-4 Oct, 2001. |
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2000 Journal Article Structure, function and regulation of tartrate-resistant acid phosphataseOddie, G. W., Schenk, G., Angel, N. Z., Walsh, N., Guddat, L. W., deJersey, J., Cassady, A. I., Hamilton, S. E. and Hume, D. A. (2000). Structure, function and regulation of tartrate-resistant acid phosphatase. Bone, 27 (5), 575-584. doi: 10.1016/S8756-3282(00)00368-9 |
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2000 Journal Article The three-dimensional structure of a complex of a murine Fab (NC10.14) with a potent sweetener (NC174): An illustration of structural diversity in antigen recognition by immunoglobulinsGuddat, Luke W., Shan, Lin, Broomell, Christopher, Ramsland, Paul A., Fan, Zhao-Chang, Anchin, Jerry M., Linthicum, D. Scott and Edmundson, Allen B. (2000). The three-dimensional structure of a complex of a murine Fab (NC10.14) with a potent sweetener (NC174): An illustration of structural diversity in antigen recognition by immunoglobulins. Journal of Molecular Biology, 302 (4), 853-872. doi: 10.1006/jmbi.2000.4083 |
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2000 Conference Publication Sweet potato purple acid phosphatase: first example of a strongly antiferromagnetically coupled Fe-Mn binuclear centre in a proteinSchenk, G., Boutchard, C., Noble, C. J., Moubaraki, B., Murray, K. S., Hanson, G. R., De Jersey, J., Hamilton, S. E., Guddat, L. W. and Carrington, L. (2000). Sweet potato purple acid phosphatase: first example of a strongly antiferromagnetically coupled Fe-Mn binuclear centre in a protein. EUROBIC-5, Toulouse, France, 17-20 July 2000. |
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2000 Journal Article Identification of mammalian-like purple acid phosphatases in a wide range of plantsSchenk, G., Ge, Y., Guddat, L., Carrington, L. E., Hume, D. A., Hamilton, S. E. and deJersey, J. (2000). Identification of mammalian-like purple acid phosphatases in a wide range of plants. Gene, 250 (1-2), 117-125. doi: 10.1016/S0378-1119(00)00186-4 |
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1999 Journal Article Crystallization and preliminary X-ray diffraction data for a purple acid phosphastase from sweet potatoSchenk, G., Carrington, L., Hamilton, S. E., De Jersey, J. and Guddat, L. W. (1999). Crystallization and preliminary X-ray diffraction data for a purple acid phosphastase from sweet potato. Acta Crystallographica Section D: Biological Crystallography, 55 (12), 2051-2052. doi: 10.1107/S0907444999012597 |
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1999 Conference Publication Planrtpurple acid phosphatases: Novel forms of the enzymeSchenk, G., Carrington, L., Guddat, L. W., De Jersey, J. and Hamilton, S. E. (1999). Planrtpurple acid phosphatases: Novel forms of the enzyme. ComBio 99, Conrad Jupiters, Gold Coast, 27-30 September, 1999. Kent Town, SA: Aust. Society for Biochemistry and Molecular Biology. |
