malic acid and valine

malic acid has been researched along with valine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Oguchi, T; Piyarom, S; Yamamoto, K; Yonemochi, E	1
Hayashi, H; Hirotsu, K; Kagamiyama, H; Miyahara, I; Mizuguchi, H; Nakajima, Y	1

Other Studies

2 other study(ies) available for malic acid and valine

Article	Year
Effects of grinding and humidification on the transformation of conglomerate to racemic compound in optically active drugs. The Journal of pharmacy and pharmacology, 1997, Volume: 49, Issue:4 Topics: Calorimetry, Differential Scanning; Humidity; Leucine; Malates; Norleucine; Optical Rotation; Reference Standards; Serine; Spectrophotometry, Infrared; Stereoisomerism; Tartrates; Temperature; Valine; X-Ray Diffraction	1997
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. The Journal of biological chemistry, 2003, Mar-14, Volume: 278, Issue:11 Topics: Aspartate Aminotransferases; Aspartic Acid; Binding Sites; Catalysis; Escherichia coli; Glycine; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Malates; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Mutation; N-Methylaspartate; Oxygen; Photons; Plasmids; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry; Tyrosine; Valine	2003

Article

Year

Effects of grinding and humidification on the transformation of conglomerate to racemic compound in optically active drugs.

The Journal of pharmacy and pharmacology, 1997, Volume: 49, Issue:4

Topics: Calorimetry, Differential Scanning; Humidity; Leucine; Malates; Norleucine; Optical Rotation; Reference Standards; Serine; Spectrophotometry, Infrared; Stereoisomerism; Tartrates; Temperature; Valine; X-Ray Diffraction

1997

Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis.

The Journal of biological chemistry, 2003, Mar-14, Volume: 278, Issue:11

Topics: Aspartate Aminotransferases; Aspartic Acid; Binding Sites; Catalysis; Escherichia coli; Glycine; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Malates; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Mutation; N-Methylaspartate; Oxygen; Photons; Plasmids; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry; Tyrosine; Valine

2003