Structure-Function Relationships of Cytochrome P-450 Laurate (ω-1)-Hydroxylase

This publication has 13 references indexed in Scilit:

• High-resolution crystal structure of cytochrome P450cam
  Published by Elsevier ,2005
• The importance of threonine‐301 from cytochromes P‐450 (laurate (ω‐1)‐hydroxylase and testosterone 16α‐hydroxylase) in substrate binding as demonstrated by site‐directed mutagenesis
  FEBS Letters, 1988
• Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide.
  Proceedings of the National Academy of Sciences, 1988
• Characterization of Rabbit Liver Cytochrome P-450 (Laurate ω-1 Hydroxylase) Synthesized in Transformed Yeast Cells1
  The Journal of Biochemistry, 1988
• Comparison of primary structures deduced from cDNA nucleotide sequences for various forms of liver microsomal cytochrome P-450 from phenobarbital-treated rabbits
  Biochemistry, 1988
• Expression of P1-450 and P3-450 DNA coding sequences as enzymatically active cytochromes P-450 in mammalian cells.
  Proceedings of the National Academy of Sciences, 1987
• P450 GENES: STRUCTURE, EVOLUTION, AND REGULATION
  Annual Review of Biochemistry, 1987
• Cytochrome P-450 Related to P-4504 from Phenobarbital-Treated Rabbit Liver: Molecular Cloning of cDNA and Characterization of Cytochrome P-450 Obtained by Its Expression in Yeast Cells1
  The Journal of Biochemistry, 1987
• Expression of cytochrome P‐450_d by Saccharomyces cerevisiae
  FEBS Letters, 1986
• Expression of Rat Liver Cytochrome P-450MC cDNA inSaccharomyces cerevisiae
  DNA, 1985