Page last updated: 2024-09-02

benzyloxyresorufin and androstenedione

benzyloxyresorufin has been researched along with androstenedione in 2 studies

Compound Research Comparison

Studies
(benzyloxyresorufin)
Trials
(benzyloxyresorufin)
Recent Studies (post-2010)
(benzyloxyresorufin)
Studies
(androstenedione)
Trials
(androstenedione)
Recent Studies (post-2010) (androstenedione)
20027,175377960

Protein Interaction Comparison

ProteinTaxonomybenzyloxyresorufin (IC50)androstenedione (IC50)
CholinesteraseHomo sapiens (human)1.55
AromataseHomo sapiens (human)0.3
Androgen receptorRattus norvegicus (Norway rat)0.6761
Testosterone 17-beta-dehydrogenase 3Homo sapiens (human)0.6826

Research

Studies (2)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Halpert, JR; Klekotka, PA1
Halpert, JR; He, YQ; Szklarz, GD1

Other Studies

2 other study(ies) available for benzyloxyresorufin and androstenedione

ArticleYear
Benzyloxyresorufin as a specific substrate for the major phenobarbital-inducible dog liver cytochrome P450 (P4502B11).
    Drug metabolism and disposition: the biological fate of chemicals, 1995, Volume: 23, Issue:12

    Topics: Androstenedione; Animals; Aryl Hydrocarbon Hydroxylases; Cytochrome P-450 Enzyme System; Dogs; Enzyme Induction; In Vitro Techniques; Kinetics; Microsomes, Liver; Oxazines; Phenobarbital; Steroid Hydroxylases; Substrate Specificity

1995
Interconversion of the androstenedione hydroxylase specificities of cytochromes P450 2B4 and 2B5 upon simultaneous site-directed mutagenesis of four key substrate recognition residues.
    Archives of biochemistry and biophysics, 1996, Nov-01, Volume: 335, Issue:1

    Topics: Androstenedione; Animals; Aryl Hydrocarbon Hydroxylases; Base Sequence; Binding Sites; Cloning, Molecular; Cytochrome P-450 Enzyme System; Cytochrome P450 Family 2; DNA Primers; Escherichia coli; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxazines; Point Mutation; Polymerase Chain Reaction; Progesterone; Protein Conformation; Rabbits; Recombinant Proteins; Steroid 16-alpha-Hydroxylase; Steroid Hydroxylases; Substrate Specificity

1996