s-2-aminoethyl cysteine has been researched along with alanine in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 3 (60.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Sen, SK | 1 |
Cavallini, D; Costa, M; Fontana, M; Pecci, I; Pensa, B | 1 |
Cavallini, D; Federici, G; Nardini, M; Ricci, G | 1 |
Ageta, T; Duprè, S; Fontana, M; Kodama, H; Sugahara, K; Yu, S; Zhang, J | 1 |
Bochar, DA; Rodwell, VW; Stauffacher, CV; Tabernero, L | 1 |
5 other study(ies) available for s-2-aminoethyl cysteine and alanine
Article | Year |
---|---|
Isolation method for lysine-excreting mutants of Arthrobacter globiformis.
Topics: Alanine; Arthrobacter; Bacteriological Techniques; Cysteine; Drug Resistance, Microbial; Lysine; Methylnitronitrosoguanidine; Mutation | 1991 |
High-performance liquid chromatography of cystathionine, lanthionine and aminoethylcysteine using o-phthaldialdehyde precolumn derivatization.
Topics: Alanine; Chromatography, High Pressure Liquid; Cystathionine; Cysteine; Indicators and Reagents; o-Phthalaldehyde; Sulfides | 1989 |
The transamination of L-cystathionine, L-cystine and related compounds by a bovine kidney transaminase.
Topics: Alanine; Amino Acids; Animals; Cattle; Cystathionine; Cysteine; Cystine; Electrophoresis, Polyacrylamide Gel; Hot Temperature; Hydrogen-Ion Concentration; Kidney; Kinetics; Molecular Weight; Rats; Species Specificity; Structure-Activity Relationship; Substrate Specificity; Sulfides; Transaminases | 1986 |
Simultaneous determination of urinary cystathionine, lanthionine, S-(2-aminoethyl)-L-cysteine and their cyclic compounds using liquid chromatography-mass spectrometry with atmospheric pressure chemical ionization.
Topics: Alanine; Atmospheric Pressure; Chromatography, Ion Exchange; Cystathionine; Cysteine; Humans; Ions; Mass Spectrometry; Reference Values; Sulfides | 1997 |
Aminoethylcysteine can replace the function of the essential active site lysine of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase.
Topics: Alanine; Amino Acid Substitution; Binding Sites; Catalysis; Cysteine; Enzyme Activation; Hydroxymethylglutaryl CoA Reductases; Iodoacetamide; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Pseudomonas | 1999 |