asparagine has been researched along with thiophenes 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 | 1 (33.33) | 29.6817 |
| 2010's | 2 (66.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brandt, M; Chambers, PA; Daines, RA; Doyle, ML; Gentry, DR; Khandekar, SS; Konstantinidis, AK; Lonsdale, JT; Silverman, C; Van Aller, GS; Warren, P; Xiang, H | 1 |
| Alcantara, SL; Brzozowski, MJ; Iravani, MM; Jenner, P; Rose, S | 1 |
| Ide, M; Irie, M; Kamikawa, T; Kashiwagi, H; Miura, T; Morikami, K; Muraoka, T; Nakamura, M; Nishihara, M | 1 |
3 other study(ies) available for asparagine and thiophenes
| Article | Year |
|---|---|
Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH).
Topics: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; Amino Acid Sequence; Anti-Bacterial Agents; Asparagine; Catalysis; Chromatography; Circular Dichroism; Cloning, Molecular; Cysteine; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Guanidine; Histidine; Indoles; Inhibitory Concentration 50; Isoelectric Focusing; Kinetics; Models, Chemical; Molecular Sequence Data; Sequence Homology, Amino Acid; Streptococcus pneumoniae; Substrate Specificity; Thiophenes; Ultraviolet Rays | 2001 |
The effect of nNOS inhibitors on toxin-induced cell death in dopaminergic cell lines depends on the extent of enzyme expression.
Topics: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine; Amidines; Animals; Asparagine; Caspase 3; Cell Death; Cell Line, Tumor; Citrulline; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dose-Response Relationship, Drug; Enzyme Inhibitors; Humans; Indazoles; L-Lactate Dehydrogenase; Leupeptins; Mice; Neuroblastoma; Neurotoxins; Nitric Oxide Synthase Type I; Thiophenes; Transfection; Tritium; Tyrosine 3-Monooxygenase; Vesicular Monoamine Transport Proteins | 2011 |
Discovery of a potent and highly selective transforming growth factor β receptor-associated kinase 1 (TAK1) inhibitor by structure based drug design (SBDD).
Topics: Animals; Asparagine; Crystallography, X-Ray; Drug Design; Enzyme Assays; Humans; Hydrogen Bonding; MAP Kinase Kinase Kinases; Mice; Microsomes, Liver; Molecular Structure; Protein Kinase Inhibitors; Pyrimidinones; Serine; Solubility; Structure-Activity Relationship; Thiophenes; Tyrosine | 2016 |