histidine has been researched along with sodium sulfate in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (25.00) | 18.7374 |
1990's | 1 (25.00) | 18.2507 |
2000's | 2 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bailey, JM; Mas, MT; Resplandor, ZE | 1 |
Gelfi, C; Righetti, PG; Stellwagen, NC | 1 |
Bathe, S; Griesbeck, C; Hauska, G; Mederer, N; Nausch, L; Schödl, T; Schütz, M; Vielreicher, M | 1 |
Bertlik, K; Brucet, M; Celada, A; Fita, I; Lloberas, J; Querol-Audí, J | 1 |
4 other study(ies) available for histidine and sodium sulfate
Article | Year |
---|---|
Site-directed mutagenesis of histidine-388 in the hinge region of yeast 3-phosphoglycerate kinase: effects on catalytic activity and activation by sulfate.
Topics: Base Sequence; Enzyme Activation; Genes; Genes, Fungal; Histidine; Kinetics; Models, Molecular; Molecular Weight; Mutation; Phosphoglycerate Kinase; Protein Conformation; Saccharomyces cerevisiae; Sulfates | 1988 |
DNA-histidine complex formation in isoelectric histidine buffers.
Topics: Anions; Base Pairing; Bromides; Buffers; Calcium Chloride; Cations, Divalent; DNA; Drug Stability; Electrophoresis, Capillary; Histidine; Magnesium Chloride; Molecular Weight; Osmolar Concentration; Potassium Compounds; Sodium Chloride; Static Electricity; Sulfates | 1999 |
Mechanism of sulfide-quinone reductase investigated using site-directed mutagenesis and sulfur analysis.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Bacterial Proteins; Benzoquinones; Chromatography, High Pressure Liquid; Electron Transport; Enzyme Activation; Gene Expression Regulation, Bacterial; Histidine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Quinone Reductases; Recombinant Fusion Proteins; Spectrometry, Fluorescence; Substrate Specificity; Sulfates; Sulfides; Sulfur; Valine | 2002 |
Structural and biochemical studies of TREX1 inhibition by metals. Identification of a new active histidine conserved in DEDDh exonucleases.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Catalytic Domain; Cations, Monovalent; Crystallography, X-Ray; Exodeoxyribonucleases; Histidine; Lithium; Lithium Compounds; Mice; Molecular Sequence Data; Phosphoproteins; Sodium; Sulfates | 2008 |