Dominique de Vries

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In the course of screening for activity at the phorbol ester binding site of protein kinase C, activity was identified within an unidentified calcareous sponge (class Calcarea) collected in the central region of the Great Barrier Reef off the north-east coast of Australia. Using high-performance liquid chromatographic fractionation guided by activity at the(More)
Protein kinase C is a ubiquitous enzyme with a key role in cellular function, making it an attractive drug target. Utilising a competitive binding assay for the phorbol ester binding site of the enzyme in a rat brain membrane preparation, screening was undertaken on 686 marine macroorganisms representing a broad range of taxa and environments from(More)
Using a high throughput radioligand binding assay, we assessed aqueous ethanol extracts from 2885 marine organisms representing 17 phyla from the Indo-Pacific for their capacity to influence [125I]epidermal growth factor binding to human A431 cells in culture. Initial screening employed extracts pooled from five unrelated organisms to cells incubated at 37(More)
The joint substitution of three active-site residues in Escherichia coli (L)-aspartate aminotransferase increases the ratio of l-cysteine sulfinate desulfinase to transaminase activity 10(5)-fold. This change in reaction specificity results from combining a tyrosine-shift double mutation (Y214Q/R280Y) with a non-conservative substitution of a(More)
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