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Richard D. Cannon
Researcher at University of Otago
Publications - 171
Citations - 6883
Richard D. Cannon is an academic researcher from University of Otago. The author has contributed to research in topics: Candida albicans & Corpus albicans. The author has an hindex of 43, co-authored 150 publications receiving 6166 citations. Previous affiliations of Richard D. Cannon include Walsh University & Gifu University.
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Journal ArticleDOI
Efflux-Mediated Antifungal Drug Resistance
Richard D. Cannon,Erwin Lamping,Ann R. Holmes,Kyoko Niimi,Philippe Baret,Mikhail V. Keniya,Koichi Tanabe,Masakazu Niimi,André Goffeau,Brian C. Monk +9 more
TL;DR: Phylogenetic analysis of the ABC pleiotropic drug resistance family has provided a new view of the evolution of this important class of efflux pumps, and potential therapeutic approaches that could overcome azole resistance are proposed.
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Oral Candida: Clearance, Colonization, or Candidiasis?
TL;DR: Candida albicans is frequently isolated from the human mouth, yet few carriers develop clinical signs of candidiasis, which results from yeast overgrowth and penetration of the oral tissues when the host's physical and immunological defenses have been undermined.
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Oral Colonization By Candida Albicans
Richard D. Cannon,W.L. Chaffin +1 more
TL;DR: The relatively small number of commensal Candida cells in the oral flora raises the possibility that strategies can be devised to prevent oral colonization and infection, but the variety of oral niches and the complex adherence mechanisms of the yeast mean that such a goal will remain elusive until more is known about the contribution of each mechanism.
Journal ArticleDOI
Multiple efflux mechanisms are involved in Candida albicans fluconazole resistance.
TL;DR: The results suggest that fluconazole enters C. albicans cells by facilitated diffusion and that flu Conazole resistance may involve energy-dependent drug efflux associated with increased expression of Benr and/or Cdr1.
Journal ArticleDOI
Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer.
Brian C. Monk,Thomas M. Tomasiak,Mikhail V. Keniya,Franziska U. Huschmann,Joel D. A. Tyndall,Joseph D. O'Connell,Richard D. Cannon,Jeffrey G. McDonald,Andrew Rodriguez,Janet Finer-Moore,Robert M. Stroud +10 more
TL;DR: In this article, the authors report crystal structures of full-length Saccharomyces cerevisiae lanosterol 14α-demethylase, a membrane monospanning cytochrome P450 of the CYP51 family that catalyzes the first postcyclization step in ergosterol biosynthesis and is inhibited by triazole drugs.