torpedo has been researched along with aspartic acid in 11 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 9 (81.82) | 18.2507 |
| 2000's | 2 (18.18) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Chatonnet, A; Duval, N; Krejci, E; Massoulié, J; Vincens, P | 1 |
| Kawamura, M; Morohashi, M; Noguchi, S; Ohtsubo, M; Takeda, K | 1 |
| Remoundos, MS; Tzartos, SJ | 1 |
| Ashani, Y; Doctor, BP; Pickering, NA; Quinn, DM; Radić, Z; Taylor, P; Tsigelny, I; Vellom, DC | 1 |
| Gentile, LN; Hawrot, E; Hsu, SH; Messier, NJ; Rosenthal, JA; Schneider, D; Vaslet, CA | 1 |
| Bartels, CF; Froment, MT; Lockridge, O; Masson, P | 2 |
| Czajkowski, C; Karlin, A; Martin, M | 1 |
| Berman, HA; Hosea, NA; Quinn, DM; Radić, Z; Taylor, P; Tsigelny, I | 1 |
| Mallender, WD; Rosenberry, TL; Szegletes, T | 1 |
| Aiello, R; Pusch, M; Traverso, S; Zifarelli, G | 1 |
11 other study(ies) available for torpedo and aspartic acid
| Article | Year |
|---|---|
Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.
Topics: Acetylcholinesterase; Amino Acid Sequence; Animals; Aspartic Acid; Biological Evolution; Cholinesterases; Enzymes; Humans; Molecular Sequence Data; Proteins; Sequence Homology, Nucleic Acid; Torpedo | 1991 |
Site-directed mutagenesis of Asp-376, the catalytic phosphorylation site, and Lys-507, the putative ATP-binding site, of the alpha-subunit of Torpedo californica Na+/K(+)-ATPase.
Topics: Adenosine Triphosphate; Animals; Aspartic Acid; Base Sequence; Binding Sites; Female; Gene Expression; Kinetics; Lysine; Macromolecular Substances; Molecular Sequence Data; Mutation; Oligodeoxyribonucleotides; Oocytes; Phosphorylation; Restriction Mapping; Sodium-Potassium-Exchanging ATPase; Torpedo; Xenopus | 1990 |
Fine localization of the major alpha-bungarotoxin binding site to residues alpha 189-195 of the Torpedo acetylcholine receptor. Residues 189, 190, and 195 are indispensable for binding.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Binding Sites; Bungarotoxins; In Vitro Techniques; Molecular Sequence Data; Peptides; Receptors, Nicotinic; Structure-Activity Relationship; Torpedo; Tyrosine | 1990 |
Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by mono- and bisquaternary oximes.
Topics: Acetylcholinesterase; Amino Acid Sequence; Animals; Aspartic Acid; Binding Sites; Butyrylcholinesterase; Cell Line; CHO Cells; Cholinesterase Inhibitors; Cholinesterase Reactivators; Cricetinae; Cytomegalovirus; Exons; Humans; Kidney; Kinetics; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Oximes; Promoter Regions, Genetic; Protein Conformation; Pyridinium Compounds; Quinolinium Compounds; Recombinant Proteins; Stereoisomerism; Structure-Activity Relationship; Torpedo; Transfection; Tryptophan; Tyrosine | 1995 |
Functional expression and site-directed mutagenesis of a synthetic gene for alpha-bungarotoxin.
Topics: Alanine; Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; Bungarotoxins; Cell Membrane; Chromatography, DEAE-Cellulose; Cloning, Molecular; Electric Organ; Escherichia coli; Factor Xa; Gene Expression; Genes, Synthetic; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Point Mutation; Protein Folding; Protein Structure, Secondary; Recombinant Fusion Proteins; Recombinant Proteins; Snakes; Torpedo | 1994 |
Asp7O in the peripheral anionic site of human butyrylcholinesterase.
Topics: Acetylcholinesterase; Amino Acid Sequence; Animals; Anions; Aspartic Acid; Binding Sites; Butyrylcholinesterase; Butyrylthiocholine; Enzyme Inhibitors; Humans; Kinetics; Methanol; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Osmolar Concentration; Protein Conformation; Sequence Homology, Amino Acid; Torpedo | 1996 |
The contributions of aspartyl residues in the acetylcholine receptor gamma and delta subunits to the binding of agonists and competitive antagonists.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Binding Sites; Cholinergic Agonists; Cholinergic Antagonists; Cloning, Molecular; In Vitro Techniques; Mice; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Receptors, Cholinergic; Recombinant Proteins; Sequence Homology, Amino Acid; Torpedo | 1996 |
Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates.
Topics: Acetylcholinesterase; Animals; Aspartic Acid; Cations; Cell Line; Cholinesterase Inhibitors; Diffusion; Electrochemistry; Humans; Mutation; Organophosphorus Compounds; Stereoisomerism; Substrate Specificity; Torpedo | 1996 |
Importance of aspartate-70 in organophosphate inhibition, oxime re-activation and aging of human butyrylcholinesterase.
Topics: Acetylcholinesterase; Animals; Aspartic Acid; Binding Sites; Butyrylcholinesterase; Cholinesterase Inhibitors; Cholinesterase Reactivators; Humans; Kinetics; Mutagenesis, Site-Directed; Organophosphorus Compounds; Paraoxon; Point Mutation; Pralidoxime Compounds; Recombinant Proteins; Tetraisopropylpyrophosphamide; Torpedo | 1997 |
Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway.
Topics: Acetylcholinesterase; Acetylthiocholine; Amino Acid Substitution; Animals; Aspartic Acid; Catalysis; Humans; Ligands; Models, Biological; Mutation; Phosphorylation; Recombinant Proteins; Substrate Specificity; Torpedo | 2000 |
Proton sensing of CLC-0 mutant E166D.
Topics: Animals; Aspartic Acid; Chloride Channels; Electric Conductivity; Female; Glutamic Acid; Hydrogen-Ion Concentration; Ion Channel Gating; Mathematics; Mutation; Oocytes; Patch-Clamp Techniques; Protons; Torpedo; Voltage-Dependent Anion Channels; Xenopus laevis | 2006 |