Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/80639
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dc.contributor.authorTieu, W.-
dc.contributor.authorSoares da Costa, T.-
dc.contributor.authorYap, M.-
dc.contributor.authorKeeling, K.-
dc.contributor.authorWilce, M.-
dc.contributor.authorWallace, J.-
dc.contributor.authorBooker, G.-
dc.contributor.authorPolyak, S.-
dc.contributor.authorAbell, A.-
dc.date.issued2013-
dc.identifier.citationChemical Science, 2013; 4(9):3533-3537-
dc.identifier.issn2041-6520-
dc.identifier.issn2041-6539-
dc.identifier.urihttp://hdl.handle.net/2440/80639-
dc.description.abstractA 'leaky mutant' (SaBPL-R122G) of Staphylococcus aureus biotin protein ligase (SaBPL) is used to enhance the turnover rate for the reaction of biotin alkyne with an azide to give a triazole. This allows the enzyme to select the optimum triazole-based inhibitor using a library of such azides in a single experiment with greatly improved efficiency and sensitivity of detection, difficulties that can restrict the general utility of a multi-component in situ click approach to ligand optimisation. © 2013 The Royal Society of Chemistry.-
dc.description.statementofresponsibilityWilliam Tieu, Tatiana P. Soares da Costa, Min Y. Yap, Kelly L. Keeling, Matthew C. J. Wilce, John C. Wallace, Grant W. Booker, Steven W. Polyak and Andrew D. Abell-
dc.language.isoen-
dc.publisherRSC Publications-
dc.rights© Royal Society of Chemistry 2013-
dc.titleOptimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors-
dc.typeJournal article-
dc.identifier.doi10.1039/c3sc51127h-
pubs.publication-statusPublished-
dc.identifier.orcidTieu, W. [0000-0002-7161-4152]-
dc.identifier.orcidBooker, G. [0000-0001-7207-4699]-
dc.identifier.orcidPolyak, S. [0000-0002-8458-5194]-
dc.identifier.orcidAbell, A. [0000-0002-0604-2629]-
Appears in Collections:Aurora harvest 4
Chemistry and Physics publications

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