Page last updated: 2024-08-23

torpedo and aspartic acid

torpedo has been researched along with aspartic acid in 11 studies

Research

Studies (11)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's9 (81.82)18.2507
2000's2 (18.18)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chatonnet, A; Duval, N; Krejci, E; Massoulié, J; Vincens, P1
Kawamura, M; Morohashi, M; Noguchi, S; Ohtsubo, M; Takeda, K1
Remoundos, MS; Tzartos, SJ1
Ashani, Y; Doctor, BP; Pickering, NA; Quinn, DM; Radić, Z; Taylor, P; Tsigelny, I; Vellom, DC1
Gentile, LN; Hawrot, E; Hsu, SH; Messier, NJ; Rosenthal, JA; Schneider, D; Vaslet, CA1
Bartels, CF; Froment, MT; Lockridge, O; Masson, P2
Czajkowski, C; Karlin, A; Martin, M1
Berman, HA; Hosea, NA; Quinn, DM; Radić, Z; Taylor, P; Tsigelny, I1
Mallender, WD; Rosenberry, TL; Szegletes, T1
Aiello, R; Pusch, M; Traverso, S; Zifarelli, G1

Other Studies

11 other study(ies) available for torpedo and aspartic acid

ArticleYear
Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.
    Proceedings of the National Academy of Sciences of the United States of America, 1991, Aug-01, Volume: 88, Issue:15

    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.
    Biochimica et biophysica acta, 1990, Jan-29, Volume: 1021, Issue:2

    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.
    The Journal of biological chemistry, 1990, Dec-15, Volume: 265, Issue:35

    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.
    The Journal of biological chemistry, 1995, Mar-17, Volume: 270, Issue:11

    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.
    The Journal of biological chemistry, 1994, Apr-15, Volume: 269, Issue:15

    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.
    European journal of biochemistry, 1996, Jan-15, Volume: 235, Issue:1-2

    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.
    The Journal of biological chemistry, 1996, Jun-07, Volume: 271, Issue:23

    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.
    Biochemistry, 1996, Aug-20, Volume: 35, Issue:33

    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.
    The Biochemical journal, 1997, Jul-01, Volume: 325 ( Pt 1)

    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.
    Biochemistry, 2000, Jul-04, Volume: 39, Issue:26

    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.
    The Journal of general physiology, 2006, Volume: 127, Issue:1

    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