Published in Biochem Biophys Res Commun on August 08, 1977
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Structural analysis of cloned cDNA for mRNA of microsomal cytochrome P-450(C21) which catalyzes steroid 21-hydroxylation in bovine adrenal cortex. J Biol Chem (1986) 1.07
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Molecular cloning and nucleotide sequence of cDNA of microsomal carboxyesterase E1 of rat liver. J Biochem (1988) 0.96
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Details of the arrangement of the outer capsid of rice dwarf phytoreovirus, as visualized by two-dimensional crystallography. J Virol (1997) 0.94
Immunochemical study on the electron pathway from NADH to cytochrome P-450 of liver microsomes. J Biochem (1978) 0.94
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Immunochemical and immunoelectron microscope studies on localization of NADPH-cytochrome c reductase on rat liver microsomes. J Cell Biol (1976) 0.93
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Hemoprotein H-450 identified as a form of cytochrome P-450 having an endogenous ligand at the 6th coordination position of the heme. J Biochem (1984) 0.91
The transmembrane region of microsomal cytochrome P450 identified as the endoplasmic reticulum retention signal. J Biochem (1994) 0.91
Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. J Biochem (1986) 0.91
Inhibition by angiotensin II type 1 receptor antagonist of cardiac phenotypic modulation after myocardial infarction. J Mol Cell Cardiol (1995) 0.91
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Synthesis and turnover of microsomal and mitochondrial NADH-cytochrome b5 reductases in rat liver. J Biochem (1978) 0.90
Mutagenicity of dimethylated metabolites of inorganic arsenics. Chem Pharm Bull (Tokyo) (1989) 0.89
The ratio of the G gamma and A gamma chains: variations due to anomalies at the molecular level. Ann N Y Acad Sci (1985) 0.89
Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. J Biochem (1980) 0.89
Evidence for molecular identity of microsomal and mitochondrial NADH-cytochrome b5 reductases of rat liver. J Biochem (1978) 0.89
Recognition of mitochondria-targeting signals by a cytosolic import stimulation factor, MSF. J Biol Chem (1994) 0.89
Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. J Biochem (1984) 0.89
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