propylparaben has been researched along with lysine in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (40.00) | 18.2507 |
| 2000's | 3 (60.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Choi, SS; Contrera, JF; Hastings, KL; Kruhlak, NL; Sancilio, LF; Weaver, JL; Willard, JM | 1 |
| Ballou, DP; Entsch, B; Moran, GR; Palfey, BA | 2 |
| Aeschliman, SM; Ballou, DP; Massey, V; Ortiz-Maldonado, M | 1 |
| Lamb, AL; Meneely, KM | 1 |
5 other study(ies) available for propylparaben and lysine
| Article | Year |
|---|---|
Development of a phospholipidosis database and predictive quantitative structure-activity relationship (QSAR) models.
Topics: | 2008 |
Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys.
Topics: 4-Hydroxybenzoate-3-Monooxygenase; Arginine; Binding Sites; Catalysis; Flavin-Adenine Dinucleotide; Flavins; Hydrogen-Ion Concentration; Kinetics; Lysine; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Mutation; NADP; Oxidation-Reduction; Parabens; Protein Conformation; Spectrophotometry | 1996 |
Electrostatic effects on substrate activation in para-hydroxybenzoate hydroxylase: studies of the mutant lysine 297 methionine.
Topics: 4-Hydroxybenzoate-3-Monooxygenase; Binding Sites; Catalysis; Electrochemistry; Enzyme Activation; Hydroxylation; Kinetics; Lysine; Methionine; Models, Molecular; Molecular Structure; Mutagenesis; Parabens; Structure-Activity Relationship | 1997 |
Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl-flavin.
Topics: 4-Hydroxybenzoate-3-Monooxygenase; Alanine; Amino Acid Substitution; Anaerobiosis; Asparagine; Aspartic Acid; Catalysis; Flavin-Adenine Dinucleotide; Hydroxylation; Lysine; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Parabens; Phenylalanine; Riboflavin; Serine; Spectrophotometry; Substrate Specificity; Tyrosine | 2001 |
Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism.
Topics: Animals; Chlorides; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Hydroxylation; Kinetics; Lysine; Microsomes, Liver; Mixed Function Oxygenases; NADP; Oligopeptides; Ornithine; Oxidation-Reduction; Parabens; Pseudomonas aeruginosa; Pseudomonas fluorescens; Schizosaccharomyces; Siderophores; Solubility; Substrate Specificity; Swine | 2007 |