alanine has been researched along with cupric chloride in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (25.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bussiere, DE; Holzman, T; Katz, L; Park, CH; Pratt, SD; Severin, JM | 1 |
Kato, S; Kato-Yamada, Y; Yoshida, M | 1 |
Emmanouil, C; Kungolos, A; Tsiridis, V; Tsiropoulos, N | 1 |
Chung, RS; Howells, C; Karafin, A; Palumaa, P; Tõugu, V; West, AK; Zovo, K | 1 |
4 other study(ies) available for alanine and cupric chloride
Article | Year |
---|---|
The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance.
Topics: Alanine; Amino Acid Sequence; Animals; Bacterial Proteins; Binding Sites; Carboxypeptidases; Copper; Crystallography, X-Ray; Dipeptidases; Dipeptides; DNA Transposable Elements; Drug Resistance, Microbial; Enterococcus faecium; Enzyme Inhibitors; Hedgehog Proteins; Mice; Models, Molecular; Molecular Sequence Data; Organophosphorus Compounds; Propionates; Protein Conformation; Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Serine-Type D-Ala-D-Ala Carboxypeptidase; Structure-Activity Relationship; Trans-Activators; Vancomycin | 1998 |
Role of the epsilon subunit of thermophilic F1-ATPase as a sensor for ATP.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Alanine; Amino Acid Sequence; Bacillus; Binding Sites; Catalytic Domain; Chromatography, Gel; Copper; Escherichia coli; Molecular Conformation; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Secondary; Proton-Translocating ATPases | 2007 |
Evaluation of toxic and interactive toxic effects of three agrochemicals and copper using a battery of microbiotests.
Topics: Agrochemicals; Alanine; Aliivibrio fischeri; Animals; Complex Mixtures; Copper; Daphnia; Environmental Monitoring; Eukaryota; Imidazoles; Neonicotinoids; Nitro Compounds; Organophosphorus Compounds; Regression Analysis; Thiazolidines; Toxicity Tests | 2009 |
Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators.
Topics: Alanine; Amyloid; Amyloid beta-Peptides; Animals; Benzothiazoles; Cells, Cultured; Cerebral Cortex; Chelating Agents; Copper; Dose-Response Relationship, Drug; Histidine; Metallothionein 3; Microscopy, Electron, Transmission; Mutation; Nerve Tissue Proteins; Neurons; Peptide Fragments; Rats; Thiazoles; Time Factors; Zinc | 2009 |