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Diane E. Kelly

Researcher at Swansea University

Publications -  135
Citations -  11300

Diane E. Kelly is an academic researcher from Swansea University. The author has contributed to research in topics: Azole & Sterol. The author has an hindex of 47, co-authored 134 publications receiving 10323 citations. Previous affiliations of Diane E. Kelly include Royal Hallamshire Hospital & University of Sheffield.

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Functional profiling of the Saccharomyces cerevisiae genome.

Guri Giaever, +72 more
- 25 Jul 2002 - 
TL;DR: It is shown that previously known and new genes are necessary for optimal growth under six well-studied conditions: high salt, sorbitol, galactose, pH 8, minimal medium and nystatin treatment, and less than 7% of genes that exhibit a significant increase in messenger RNA expression are also required for optimal Growth in four of the tested conditions.
Journal ArticleDOI

Resistance to fluconazole and cross-resistance to amphotericin B in Candida albicans from AIDS patients caused by defective sterol Δ5,6-desaturation

TL;DR: It is shown in two clinical isolates that resistance was caused by defective sterol Δ5,6‐desaturation and growth arrest after fluconazole treatment of C. albicans in clinical conditions is caused by 14α‐methylergosta‐8,24(28)‐dien‐3β,6α‐diol accumulation.
Journal ArticleDOI

Mode of action and resistance to azole antifungals associated with the formation of 14 alpha-methylergosta-8,24(28)-dien-3 beta,6 alpha-diol.

TL;DR: It is shown that cell growth arrest correlates with the accumulation of 14α-methyl-ergosta-8,24(28)-dien-3β,6α-diol in a yeast strain with a sterol 14 α-demethylase gene disruption, which mimics stringent treatment conditions.
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The Mutation T315A in Candida albicans Sterol 14α-Demethylase Causes Reduced Enzyme Activity and Fluconazole Resistance through Reduced Affinity

TL;DR: This work undertook site-directed mutagenesis of the Candida albicans heterologously expressed in Saccharomyces cerevisiae to probe a model structure for the sterol 14α-demethylase, and made the first example of a single base change in the target enzyme conferring resistance to azoles through reduced azole affinity.