Daphne L. Davis

TL;DR: The structure of the sterol 26-hydroxylase cDNA reveals it to be a mitochondrial cytochrome P-450, and blotting experiments revealed that the mRNA for this enzyme is expressed in many tissues and that it is encoded by a low copy number gene in the rabbit genome.

TL;DR: In this article, the authors used protein sequencing and molecular cloning techniques to isolate and characterize a cDNA encoding the rabbit mitochondrial sterol 26-hydroxylase, which catalyzes the first step in the oxidation of the side chain of sterol intermediates in the biosynthesis of bile acids.

TL;DR: Four substitution and two splice junction mutations were identified in the 17βHSD3 genes of five unrelated male pseudohermaphrodites that severely compromised the activity of the 17 β–HSD type 3 isozyme.

TL;DR: Molecular analysis of the SRD5A2 gene resulted in the identification of 18 mutations in 11 homozygote, 6 compound heterozygotes, and 4 inferred compoundheterozygotes from 23 families with 5 alpha-reductase deficiency, suggesting that the carrier frequency of mutations in the 5alpha- reductase type 2 gene may be higher than previously thought.

TL;DR: The findings indicate the quantitative importance of the acidic pathway in early life in humans and define a further inborn error in bile acid synthesis as a metabolic cause of severe cholestatic liver disease.