lysine has been researched along with xanthine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ito, M; Kato, S; Nakamura, M; Ogawa, H; Takagi, Y | 1 |
| Chin, MS; Munagala, NR; Wang, CC | 1 |
| Munagala, NR; Wang, CC | 1 |
| Barnes, VM; Devizio, W; Guo, L; Lee, DP; Milburn, MV; Mitchell, MW; Teles, R; Trivedi, HM; Wulff, JE; Xu, T | 1 |
1 trial(s) available for lysine and xanthine
| Article | Year |
|---|---|
Assessment of the effects of dentifrice on periodontal disease biomarkers in gingival crevicular fluid.
Topics: Adult; Aged; Biomarkers; Chronic Periodontitis; Double-Blind Method; Female; Gingival Crevicular Fluid; Gingivitis; Humans; Inosine; Lysine; Male; Metabolome; Middle Aged; Putrescine; Toothpastes; Triclosan; Xanthine; Young Adult | 2010 |
3 other study(ies) available for lysine and xanthine
| Article | Year |
|---|---|
Structural analysis of the rat uricase gene and evidence that lysine 164 is involved in the substrate-binding site of the enzyme.
Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cloning, Molecular; Cosmids; Escherichia coli; Genomic Library; Kinetics; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Rats; Recombinant Proteins; Restriction Mapping; Urate Oxidase; Xanthine; Xanthines | 1991 |
Steady-state kinetics of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus: the role of threonine-47.
Topics: Amino Acid Substitution; Animals; Binding, Competitive; Guanosine Monophosphate; Hypoxanthine Phosphoribosyltransferase; Inosine Monophosphate; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Ribonucleotides; Threonine; Tritrichomonas foetus; Xanthine | 1998 |
Altering the purine specificity of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus by structure-based point mutations in the enzyme protein.
Topics: Adenine Phosphoribosyltransferase; Amino Acid Substitution; Animals; Arginine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Enzyme Activation; Glutamic Acid; Guanine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Isoleucine; Lysine; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Purines; Ribonucleotides; Serine; Structure-Activity Relationship; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine | 1998 |