Page last updated: 2024-09-04

phenyldiazene and aspartic acid

phenyldiazene has been researched along with aspartic acid in 2 studies

Compound Research Comparison

Studies
(phenyldiazene)
Trials
(phenyldiazene)
Recent Studies (post-2010)
(phenyldiazene)
Studies
(aspartic acid)
Trials
(aspartic acid)
Recent Studies (post-2010) (aspartic acid)
250423,0054174,018

Protein Interaction Comparison

ProteinTaxonomyphenyldiazene (IC50)aspartic acid (IC50)
Glutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Norway rat)1.638
Excitatory amino acid transporter 1Homo sapiens (human)90.1265
Excitatory amino acid transporter 2Homo sapiens (human)11
Glutamate receptor ionotropic, NMDA 2A Rattus norvegicus (Norway rat)1.638
Glutamate receptor ionotropic, NMDA 2BRattus norvegicus (Norway rat)1.638
Glutamate receptor ionotropic, NMDA 2CRattus norvegicus (Norway rat)1.638
Glutamate receptor ionotropic, NMDA 2DRattus norvegicus (Norway rat)1.638
Glutamate receptor ionotropic, NMDA 3BRattus norvegicus (Norway rat)1.638
Glutamate receptor ionotropic, NMDA 3ARattus norvegicus (Norway rat)1.638

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
Ellis, SW; Hayhurst, GP; Lennard, MS; Mackman, R; Ortiz de Montellano, PR; Smith, G; Tschirret-Guth, RA; Tucker, GT; Wolf, CR1
Davis, SC; Dierks, EA; Ortiz de Montellano, PR1

Other Studies

2 other study(ies) available for phenyldiazene and aspartic acid

ArticleYear
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
Glu-320 and Asp-323 are determinants of the CYP4A1 hydroxylation regiospecificity and resistance to inactivation by 1-aminobenzotriazole.
    Biochemistry, 1998, Feb-17, Volume: 37, Issue:7

    Topics: Amino Acid Substitution; Aspartic Acid; Binding Sites; Catalysis; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System; Enzyme Activation; Glutamic Acid; Humans; Hydroxylation; Imidazoles; Imines; Mixed Function Oxygenases; Mutagenesis, Site-Directed; Recombinant Proteins; Substrate Specificity; Triazoles

1998