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protoporphyrin ix and phenyldiazene

protoporphyrin ix has been researched along with phenyldiazene 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
Ellis, SW; Hayhurst, GP; Lennard, MS; Mackman, R; Ortiz de Montellano, PR; Smith, G; Tschirret-Guth, RA; Tucker, GT; Wolf, CR	1
Schrag, ML; Wienkers, LC	1

Other Studies

2 other study(ies) available for protoporphyrin ix and phenyldiazene

Article	Year
Active-site topologies of human CYP2D6 and its aspartate-301 --> glutamate, asparagine, and glycine mutants. Archives of biochemistry and biophysics, 1996, Jul-01, Volume: 331, Issue:1 Topics: Asparagine; Aspartic Acid; Binding Sites; Cytochrome P-450 CYP2D6; Cytochrome P-450 Enzyme System; Electrochemistry; Glutamic Acid; Glycine; Humans; Hydrazines; Imines; Mixed Function Oxygenases; Models, Molecular; Molecular Structure; Mutation; Protoporphyrins; Saccharomyces cerevisiae; Structure-Activity Relationship	1996
Topological alteration of the CYP3A4 active site by the divalent cation Mg(2+). Drug metabolism and disposition: the biological fate of chemicals, 2000, Volume: 28, Issue:10 Topics: Binding Sites; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Humans; Hydroxylation; Imines; Kinetics; Magnesium; Mixed Function Oxygenases; Oxidation-Reduction; Protein Conformation; Protoporphyrins; Pyrenes; Spectrometry, Mass, Electrospray Ionization; Substrate Specificity; Triazolam	2000

Article

Year

Active-site topologies of human CYP2D6 and its aspartate-301 --> glutamate, asparagine, and glycine mutants.

Archives of biochemistry and biophysics, 1996, Jul-01, Volume: 331, Issue:1

Topics: Asparagine; Aspartic Acid; Binding Sites; Cytochrome P-450 CYP2D6; Cytochrome P-450 Enzyme System; Electrochemistry; Glutamic Acid; Glycine; Humans; Hydrazines; Imines; Mixed Function Oxygenases; Models, Molecular; Molecular Structure; Mutation; Protoporphyrins; Saccharomyces cerevisiae; Structure-Activity Relationship

1996

Topological alteration of the CYP3A4 active site by the divalent cation Mg(2+).

Drug metabolism and disposition: the biological fate of chemicals, 2000, Volume: 28, Issue:10

Topics: Binding Sites; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Humans; Hydroxylation; Imines; Kinetics; Magnesium; Mixed Function Oxygenases; Oxidation-Reduction; Protein Conformation; Protoporphyrins; Pyrenes; Spectrometry, Mass, Electrospray Ionization; Substrate Specificity; Triazolam

2000