Page last updated: 2024-09-04

phenyldiazene and glutamic acid

phenyldiazene has been researched along with glutamic acid in 3 studies

Compound Research Comparison

Studies
(phenyldiazene)
Trials
(phenyldiazene)
Recent Studies (post-2010)
(phenyldiazene)
Studies
(glutamic acid)
Trials
(glutamic acid)
Recent Studies (post-2010) (glutamic acid)
250441,75745212,876

Protein Interaction Comparison

ProteinTaxonomyphenyldiazene (IC50)glutamic acid (IC50)
Chain A, GLUTAMATE RECEPTOR SUBUNIT 2Rattus norvegicus (Norway rat)0.821
Chain A, Glutamate Receptor Subunit 2Rattus norvegicus (Norway rat)0.821
Chain B, Glutamate Receptor Subunit 2Rattus norvegicus (Norway rat)0.821
Metabotropic glutamate receptor 8Homo sapiens (human)0.0057
Glutamate receptor ionotropic, NMDA 2DHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 3BHomo sapiens (human)0.07
Glutamate receptor 1Rattus norvegicus (Norway rat)0.5885
Glutamate receptor 2Rattus norvegicus (Norway rat)0.5885
Glutamate receptor 3Rattus norvegicus (Norway rat)0.5885
Glutamate receptor 4Rattus norvegicus (Norway rat)0.5885
Glutamate receptor ionotropic, kainate 1Rattus norvegicus (Norway rat)0.38
Glutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, kainate 2Rattus norvegicus (Norway rat)0.38
Glutamate receptor 1Homo sapiens (human)0.613
Glutamate receptor 2Homo sapiens (human)0.613
Glutamate receptor 3Homo sapiens (human)0.613
Glutamate receptor ionotropic, kainate 3Rattus norvegicus (Norway rat)0.38
Excitatory amino acid transporter 1Homo sapiens (human)207
Glutamate receptor 4Homo sapiens (human)0.613
Glutamate receptor ionotropic, NMDA 2A Rattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, NMDA 2BRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, NMDA 2CRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, kainate 4Rattus norvegicus (Norway rat)0.38
Glutamate receptor ionotropic, NMDA 1Homo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2AHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2BHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2CHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2DRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, kainate 5Rattus norvegicus (Norway rat)0.38
Glutamate receptor ionotropic, NMDA 3AHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 3BRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, NMDA 3ARattus norvegicus (Norway rat)0.1533

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hatano, M; Hiroya, K; Ortiz de Montellano, PR; Shimizu, T; Tuck, SF1
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

3 other study(ies) available for phenyldiazene and glutamic acid

ArticleYear
The cytochrome P450 1A2 active site: topology and perturbations caused by glutamic acid-318 and threonine-319 mutations.
    Biochemistry, 1993, Mar-16, Volume: 32, Issue:10

    Topics: Amino Acid Sequence; Animals; Binding Sites; Cytochrome P-450 CYP1A2; Cytochrome P-450 Enzyme System; Glutamates; Glutamic Acid; Imines; Liver; Mutagenesis, Site-Directed; Oxidoreductases; Protein Conformation; Rats; Recombinant Proteins; Saccharomyces cerevisiae; Threonine

1993
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