ethoxyresorufin and lysine

ethoxyresorufin has been researched along with lysine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hatano, M; Hiroya, K; Krainev, AG; Shimizu, T	1
Cvrk, T; Strobel, HW	1

Other Studies

2 other study(ies) available for ethoxyresorufin and lysine

Article	Year
Effect of mutations at Lys250, Arg251, and Lys253 of cytochrome P450 1A2 on the catalytic activities and the bindings of bifunctional axial ligands. Archives of biochemistry and biophysics, 1992, Volume: 298, Issue:1 Topics: Amino Acid Sequence; Animals; Arginine; Catalysis; Cytochrome P-450 CYP1A2; Cytochrome P-450 Enzyme System; Kinetics; Ligands; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxazines; Oxidoreductases; Protein Conformation; Spectrum Analysis; Structure-Activity Relationship	1992
Role of LYS271 and LYS279 residues in the interaction of cytochrome P4501A1 with NADPH-cytochrome P450 reductase. Archives of biochemistry and biophysics, 2001, Jan-15, Volume: 385, Issue:2 Topics: Amino Acid Substitution; Benzene Derivatives; Binding Sites; Circular Dichroism; Coumarins; Cytochrome P-450 CYP1A1; Electron Transport; Flavin-Adenine Dinucleotide; Heme; Iron; Kinetics; Lysine; Mutation; NADPH-Ferrihemoprotein Reductase; Oxazines; Protein Binding; Protein Structure, Secondary	2001

Article

Year

Effect of mutations at Lys250, Arg251, and Lys253 of cytochrome P450 1A2 on the catalytic activities and the bindings of bifunctional axial ligands.

Archives of biochemistry and biophysics, 1992, Volume: 298, Issue:1

Topics: Amino Acid Sequence; Animals; Arginine; Catalysis; Cytochrome P-450 CYP1A2; Cytochrome P-450 Enzyme System; Kinetics; Ligands; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxazines; Oxidoreductases; Protein Conformation; Spectrum Analysis; Structure-Activity Relationship

1992

Role of LYS271 and LYS279 residues in the interaction of cytochrome P4501A1 with NADPH-cytochrome P450 reductase.

Archives of biochemistry and biophysics, 2001, Jan-15, Volume: 385, Issue:2

Topics: Amino Acid Substitution; Benzene Derivatives; Binding Sites; Circular Dichroism; Coumarins; Cytochrome P-450 CYP1A1; Electron Transport; Flavin-Adenine Dinucleotide; Heme; Iron; Kinetics; Lysine; Mutation; NADPH-Ferrihemoprotein Reductase; Oxazines; Protein Binding; Protein Structure, Secondary

2001