Primary and secondary structural patterns in eukaryotic cytochrome P-450 families correspond to structures of the helix-rich domain of Pseudomonas patida cytochrome P-450cam
Crystallographic and molecular modelling studies on 3-ethyl-3-(4-pyridyl)piperidine-2,6-dione and its butyl analogue, inhibitors of mammalian aromatase. Comparison with natural substrates prediction of enantioselectivity for N-alkyl derivatives
Inhibitors of the P450 and enzymes aromatase and lyase. Crystallographic and molecular modeling studies suggest structural features of pyridylacetic acid derivatives responsible for differences in enzyme inhibitory activity
The active site of aromatase cytochrome P-450. Differential effects of cyanide provide evidence for proximity of heme-iron and carbon-19 in the enzyme-substrate complex.
Structure function studies of human aromatase by site-directed mutagenesis kinetic properties of mutants Pro-308→Phe, Tyr-361→Phe, Tyr-361→Leu, and Phe-406→Arg.