adenylosuccinate has been researched along with arginine in 4 studies
| Studies (adenylosuccinate) | Trials (adenylosuccinate) | Recent Studies (post-2010) (adenylosuccinate) | Studies (arginine) | Trials (arginine) | Recent Studies (post-2010) (arginine) |
|---|---|---|---|---|---|
| 52 | 1 | 5 | 46,388 | 1,688 | 11,176 |
| Protein | Taxonomy | adenylosuccinate (IC50) | arginine (IC50) |
|---|---|---|---|
| Cationic amino acid transporter 3 | Homo sapiens (human) | 283 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 4 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brosius, JL; Colman, RF | 1 |
| Colman, RF; Palenchar, JB | 1 |
| Colman, RF; Segall, ML | 1 |
| Colman, RF; Cowley, D; McGown, I; Patterson, D; Sivendran, S; Spiegel, E | 1 |
4 other study(ies) available for adenylosuccinate and arginine
| Article | Year |
|---|---|
Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.
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 |
Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural role.
Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Aminoimidazole Carboxamide; Arginine; Asparagine; Bacillus subtilis; Bacterial Proteins; Circular Dichroism; Enzyme Activation; Humans; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Ribonucleotides; Substrate Specificity; Threonine | 2003 |
Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.
Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Animals; Arginine; Asparagine; Bacillus subtilis; Binding Sites; Catalysis; Circular Dichroism; Glutamine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Sequence Alignment; Thermodynamics | 2004 |
Two novel mutant human adenylosuccinate lyases (ASLs) associated with autism and characterization of the equivalent mutant Bacillus subtilis ASL.
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 |