Cytochrome P450 3A4 (CYP3A4) is a major enzymatic determinant of drug and xenobiotic metabolism that demonstrates remarkable substrate diversity and complex kinetic properties. The complex… Read More »Time-resolved fluorescence studies of heterotropic ligand binding to cytochrome P450 3A4
Previously human cytochrome P450 3A4 was efficiently and specifically photolabeled by the photoaffinity ligand lapachenole. One of the modification sites was identified as cysteine 98… Read More »Cysteine 98 in CYP3A4 contributes to conformational integrity required for P450 interaction with CYP reductase
Cytochrome P450’s (P450’s) catalyze the oxidative metabolism of most drugs and toxins. Although extensive studies have proven that some P450’s demonstrate both homotropic and heterotropic… Read More »NMR studies of ligand binding to P450(eryF) provides insight into the mechanism of cooperativity
The mechanism of CYP3A4-substrate interactions has been investigated using a battery of techniques including cysteine scanning mutagenesis, photoaffinity labeling, and structural modeling. In this study,… Read More »Probing the CYP3A4 active site by cysteine scanning mutagenesis and photoaffinity labeling
Complementary oligodeoxynucleotides (ODNs) that contain 2-aminoadenine and 2-thiothymine interact weakly with each other but form stable hybrids with unmodified complements. These selectively binding complementary (SBC)… Read More »Antisense oligonucleotides containing modified bases inhibit in vitro translation of Leishmania amazonensis mRNAs by invading the mini-exon hairpin
G/A motif triplex-forming oligonucleotides (TFOs) complementary to a 21 base pair homopurine/homopyrimidine run were conjugated at one or both ends to chlorambucil. These TFOs were… Read More »Factors influencing the extent and selectivity of alkylation within triplexes by reactive G/A motif oligonucleotides