lysine has been researched along with charybdotoxin in 9 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 5 (55.56) | 18.2507 |
2000's | 4 (44.44) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Miller, C; Park, CS | 1 |
Eberhart, A; Garcia, ML; Kaczorowski, GJ; Knaus, HG | 1 |
Garcia, ML; Kaczorowski, GJ; Knaus, HG; Munujos, P | 1 |
Miller, C; Naranjo, D | 1 |
Fozzard, HA; Lipkind, GM | 1 |
Bernard, C; Bischoff, U; Darbon, H; Ferrat, G; Legros, C; Marquardt, A; Pongs, O | 1 |
Damjanovich, S; Gáspár, R; Hajdu, P; Horjales, E; Panyi, G; Péter, M; Possani, LD; Varga, Z | 1 |
Chen, X; Ding, J; Li, H; Wu, G; Wu, H; Xu, T; Yao, J; Yao, L; Zhang, N; Zhou, Y; Zhou, Z | 1 |
Chen, M; Ding, J; Gan, G; Wang, L; Wu, Y | 1 |
9 other study(ies) available for lysine and charybdotoxin
Article | Year |
---|---|
Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel.
Topics: Animals; Calcium; Charybdotoxin; Electric Conductivity; Electrochemistry; Escherichia coli; Kinetics; Lipid Bilayers; Lysine; Mutagenesis; Potassium; Potassium Channels; Rats; Recombinant Proteins; Scorpion Venoms; Structure-Activity Relationship | 1992 |
Covalent attachment of charybdotoxin to the beta-subunit of the high conductance Ca(2+)-activated K+ channel. Identification of the site of incorporation and implications for channel topology.
Topics: Amino Acid Sequence; Animals; Antibodies; Autoradiography; Calcium; Cattle; Charybdotoxin; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Glycoproteins; Lysine; Molecular Sequence Data; Potassium Channels; Precipitin Tests; Scorpion Venoms | 1994 |
Cross-linking of charybdotoxin to high-conductance calcium-activated potassium channels: identification of the covalently modified toxin residue.
Topics: Animals; Binding Sites; Calcium; Cattle; Charybdotoxin; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Lysine; Membrane Proteins; Muscle, Smooth; Mutagenesis, Site-Directed; Peptides; Potassium Channels; Protein Conformation; Sarcolemma; Scorpion Venoms | 1995 |
A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K+ channel.
Topics: Amino Acid Sequence; Animals; Binding Sites; Charybdotoxin; Drosophila melanogaster; Drosophila Proteins; Ion Channel Gating; Lysine; Molecular Sequence Data; Oocytes; Phenylalanine; Potassium; Potassium Channels; Protein Binding; Protein Conformation; Recombinant Fusion Proteins; Scorpions; Shaker Superfamily of Potassium Channels; Threonine; Transfection; Xenopus laevis | 1996 |
A model of scorpion toxin binding to voltage-gated K+ channels.
Topics: Amino Acid Sequence; Animals; Charybdotoxin; Energy Transfer; Ion Channel Gating; Kv1.3 Potassium Channel; Lysine; Models, Molecular; Molecular Sequence Data; Molecular Structure; Potassium Channels; Potassium Channels, Voltage-Gated; Scorpion Venoms | 1997 |
Solution structure of hpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel.
Topics: Amino Acid Sequence; Animals; Anisotropy; Charybdotoxin; CHO Cells; Conotoxins; Cricetinae; Disulfides; Electrophysiology; Escherichia coli; Lysine; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Neuropeptides; Neurotoxins; omega-Conotoxins; Potassium Channels; Potassium Channels, Voltage-Gated; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Shal Potassium Channels; Spider Venoms; Time Factors | 2000 |
Effects of toxins Pi2 and Pi3 on human T lymphocyte Kv1.3 channels: the role of Glu7 and Lys24.
Topics: Amino Acid Sequence; Animals; Charybdotoxin; Glutamic Acid; Humans; In Vitro Techniques; Kinetics; Kv1.3 Potassium Channel; Lysine; Membrane Potentials; Models, Molecular; Molecular Sequence Data; Point Mutation; Potassium Channel Blockers; Potassium Channels; Potassium Channels, Voltage-Gated; Protein Conformation; Scorpion Venoms; Sequence Homology, Amino Acid; T-Lymphocytes | 2001 |
BmP09, a "long chain" scorpion peptide blocker of BK channels.
Topics: Adrenal Medulla; Amino Acid Sequence; Animals; Charybdotoxin; Chromatography; Cysteine; Disulfides; Dose-Response Relationship, Drug; Electrophysiology; Hydrogen Bonding; Kinetics; Large-Conductance Calcium-Activated Potassium Channels; Lysine; Methionine; Mice; Models, Molecular; Molecular Sequence Data; Mutagenesis; Oocytes; Patch-Clamp Techniques; Peptides; Potassium Channels, Calcium-Activated; Protein Structure, Tertiary; Scorpion Venoms; Scorpions; Sequence Homology, Amino Acid; Sodium; Sulfoxides; Time Factors; Xenopus | 2005 |
Lysine-rich extracellular rings formed by hbeta2 subunits confer the outward rectification of BK channels.
Topics: Amino Acid Sequence; Animals; Calcium; Charybdotoxin; Epitopes; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits; Large-Conductance Calcium-Activated Potassium Channel beta Subunits; Large-Conductance Calcium-Activated Potassium Channels; Lysine; Patch-Clamp Techniques; Peptide Fragments; Potassium; Protein Subunits; Static Electricity | 2008 |