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Article

The presence of an R467K amino acid substitution and loss of allelic variation correlate with an azole-resistant lanosterol 14alpha demethylase in Candida albicans.

Antimicrobial agents and chemotherapy - 1 Jul 1997

White T C

Abstract excerpt

Azole resistance in the pathogenic yeast Candida albicans is an emerging problem in the human immunodeficiency virus (HIV)-infected population. The target enzyme of the azole drugs is lanosterol 14alpha demethylase (Erg16p), a cytochrome P-450 enzyme in the biosynthetic pathway of ergosterol. Biochemical analysis demonstrates that Erg16p became less susceptible to fluconazole in isolate 13 in a series of isolates...

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Identifiers

PMID: 9210671
DOI: 10.1128/AAC.41.7.1488
PMCID: PMC163945

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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The presence of an R467K amino acid substitution and loss of allelic variation correlate with an azole-resistant lanosterol 14alpha demethylase in Candida albicans.PMID 9210671Read ↗

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<i>Erg11</i>mutations associated with azole resistance in clinical isolates of<i>Candida albicans</i>Semantic proximity Read ↗

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Multiple amino acid substitutions in lanosterol 14alpha-demethylase contribute to azole resistance in Candida albicans.Semantic proximity Read ↗

Triazole resistance mediated by mutations of a conserved active site tyrosine in fungal lanosterol 14α-demethylaseSemantic proximity Read ↗

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