Page last updated: 2024-09-03

adenylosuccinate and glutamic acid

adenylosuccinate has been researched along with glutamic acid in 2 studies

Compound Research Comparison

Studies
(adenylosuccinate)
Trials
(adenylosuccinate)
Recent Studies (post-2010)
(adenylosuccinate)
Studies
(glutamic acid)
Trials
(glutamic acid)
Recent Studies (post-2010) (glutamic acid)
521541,75745212,876

Protein Interaction Comparison

ProteinTaxonomyadenylosuccinate (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 (2)

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

Authors

AuthorsStudies
Brosius, JL; Colman, RF1
Colman, RF; Cowley, D; McGown, I; Patterson, D; Sivendran, S; Spiegel, E1

Other Studies

2 other study(ies) available for adenylosuccinate and glutamic acid

ArticleYear
Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.
    Biochemistry, 2002, Feb-19, Volume: 41, Issue:7

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Alanine; Amino Acid Substitution; Arginine; Bacillus subtilis; Binding Sites; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Genetic Complementation Test; Glutamic Acid; Kinetics; Light; Lysine; Molecular Weight; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Secondary; Scattering, Radiation; Tritium

2002
Two novel mutant human adenylosuccinate lyases (ASLs) associated with autism and characterization of the equivalent mutant Bacillus subtilis ASL.
    The Journal of biological chemistry, 2004, Dec-17, Volume: 279, Issue:51

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Arginine; Aspartic Acid; Autistic Disorder; Bacillus subtilis; Circular Dichroism; DNA; Electrophoresis, Polyacrylamide Gel; Family Health; Female; Glutamic Acid; Heterozygote; Hot Temperature; Humans; Hydrogen-Ion Concentration; Kinetics; Male; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mothers; Mutagenesis, Site-Directed; Mutation; Polymerase Chain Reaction; Protein Binding; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Spectrophotometry; Temperature; Thermotoga maritima; Time Factors; Ultraviolet Rays

2004