alpha-ketoglutaramate has been researched along with asparagine in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (66.67) | 29.6817 |
2010's | 1 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cooper, AJ; Krasnikov, BF; Nostramo, R; Pinto, JT | 1 |
Callaway, M; Chien, CH; Cooper, AJ; Huebner, K; Krasnikov, BF; Nieves, E; Nostramo, R; Pinto, JT; Sun, J | 1 |
Chien, CH; Cooper, AJ; Gao, QZ; Lyu, JH; Sheu, SY | 1 |
3 other study(ies) available for alpha-ketoglutaramate and asparagine
Article | Year |
---|---|
Assay and purification of omega-amidase/Nit2, a ubiquitously expressed putative tumor suppressor, that catalyzes the deamidation of the alpha-keto acid analogues of glutamine and asparagine.
Topics: Amidohydrolases; Animals; Asparagine; Catalysis; Deamination; Glutamine; Ketoglutaric Acids; Liver; Rats; Spectrophotometry | 2009 |
Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination.
Topics: Amidohydrolases; Aminohydrolases; Animals; Asparagine; Electrophoresis, Polyacrylamide Gel; Glutamine; Humans; Ketoglutaric Acids; Kinetics; Liver; Mice; Mice, Knockout; Protein Subunits; Rats; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2009 |
Structural insights into the catalytic active site and activity of human Nit2/ω-amidase: kinetic assay and molecular dynamics simulation.
Topics: Amino Acid Sequence; Amino Acid Substitution; Aminohydrolases; Animals; Asparagine; Catalytic Domain; Conserved Sequence; Humans; Hydrolysis; Ketoglutaric Acids; Kinetics; Mice; Molecular Dynamics Simulation; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Recombinant Proteins; Sequence Deletion; Structural Homology, Protein; Substrate Specificity; Surface Properties; Thermodynamics | 2012 |