alanine has been researched along with dithionite 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 |
|---|---|
| Arscott, LD; Gilberger, TW; Müller, S; Wang, PF; Williams, CH | 1 |
| Clair, P; Drin, G; Kaczorek, M; Mathieu, D; Mazel, M; Temsamani, J | 1 |
| Farrell, SR; Thorpe, C | 1 |
| Huang, HW; Inoue, M; Kataoka, K; Kitagawa, R; Naruse, D; Sakurai, T | 1 |
4 other study(ies) available for alanine and dithionite
| Article | Year |
|---|---|
Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol.
Topics: Alanine; Animals; Binding Sites; Cysteine; Disulfides; Dithionite; Dithionitrobenzoic Acid; Kinetics; Mutagenesis, Site-Directed; NADP; Oxidation-Reduction; Peptide Fragments; Plasmodium falciparum; Thioredoxin-Disulfide Reductase; Titrimetry; Toluene | 1999 |
Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Antennapedia Homeodomain Protein; Cell Membrane; Circular Dichroism; Dithionite; Endocytosis; Flow Cytometry; Fluorescent Dyes; Homeodomain Proteins; Humans; K562 Cells; Kinetics; Lipid Bilayers; Liposomes; Micelles; Molecular Sequence Data; Nuclear Proteins; Peptide Fragments; Phospholipids; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Sodium Dodecyl Sulfate; Static Electricity; Structure-Activity Relationship; Transcription Factors | 2001 |
Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity.
Topics: Aerobiosis; Alanine; Amino Acid Sequence; Amino Acid Substitution; Anaerobiosis; Animals; Catalysis; Cysteine; Cytochrome Reductases; Dithionite; Electron Transport Complex IV; Flavoproteins; Humans; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Photochemistry; Rats; Structural Homology, Protein | 2005 |
Point mutations at the type I Cu ligands, Cys457 and Met467, and at the putative proton donor, Asp105, in Myrothecium verrucaria bilirubin oxidase and reactions with dioxygen.
Topics: Alanine; Amino Acid Substitution; Asparagine; Aspartic Acid; Copper; Cysteine; Dithionite; Fungal Proteins; Glutamic Acid; Glutamine; Hypocreales; Ligands; Methionine; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Oxygen; Point Mutation; Protons; Serine | 2005 |