1. Adelaide Research & Scholarship

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Results 11-20 of 21 (Search time: 0.003 seconds).
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PreviewIssue DateTitleAuthor(s)
2012Selective inhibition of biotin protein ligase from Staphylococcus aureusSoares da Costa, T.; Tieu, W.; Yap, M.; Pendini, N.; Polyak, S.; Pedersen, D.; Morona, R.; Turnidge, J.; Wallace, J.; Wilce, M.; Booker, G.; Abell, A.
2009A Novel Approach to Identify Two Distinct Receptor Binding Surfaces of Insulin-like Growth Factor IIAlvino, C.; McNeil, K.; Ong, S.; Delaine, C.; Booker, G.; Wallace, J.; Whittaker, J.; Forbes, B.
2008An investigation of the ligand binding properties and negative cooperatively of soluble insulin-like growth factor receptorsSurinya, K.; Forbes, B.; Occhiodoro, F.; Booker, G.; Francis, G.; Siddle, K.; Wallace, J.; Cosgrove, L.
2012Localization of inhibitory antibodies to the biotin domain of human pyruvate carboxylaseArpornsuwan, T.; Carey, K.; Booker, G.; Polyak, S.; Wallace, J.
2006Production and characterization of monoclonal antibodies against insulin-like growth factor type 1 receptorKeyhanfar, M.; Forbes, B.; Cosgrove, L.; Wallace, J.; Booker, G.
2007Precise mapping of an IGF-I-binding site on the IGF-1RKeyhanfar, M.; Booker, G.; Whittaker, J.; Wallace, J.; Forbes, B.
2012Biotin analogues with antibacterial activity are potent inhibitors of biotin protein ligaseSoares da Costa, T.; Tieu, W.; Yap, M.; Zvarec, O.; Bell, J.; Turnidge, J.; Wallace, J.; Booker, G.; Wilce, M.; Abell, A.; Polyak, S.
2007Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramersJitrapakdee, S.; Surinya, K.; Adina-Zada, A.; Polyak, S.; Stojkoski, C.; Smyth, R.; Booker, G.; Cleland, W.; Attwood, P.; Wallace, J.
2005Molecular interactions of the IGF systemDenley, A.; Cosgrove, L.; Booker, G.; Wallace, J.; Forbes, B.
2013Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: An antibiotic targetPendini, N.; Yap, M.; Polyak, S.; Cowieson, N.; Abell, A.; Booker, G.; Wallace, J.; Wilce, J.; Wilce, M.

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