cysteine has been researched along with n-biotinylaminoethyl methanethiosulfonate in 7 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 7 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Czajkowski, C; Wagner, DA | 1 |
Ennion, SJ; Evans, RJ | 1 |
Ferrer, JV; Javitch, JA; Kuhn, DM; Park, SU | 1 |
Czajkowski, C; McDevitt, RA; Newell, JG | 1 |
Dangprapai, Y; Pelis, RM; Wright, SH; Wunz, TM | 1 |
Hanck, DA; Sheets, MF | 1 |
Cummins, TR | 1 |
7 other study(ies) available for cysteine and n-biotinylaminoethyl methanethiosulfonate
Article | Year |
---|---|
Structure and dynamics of the GABA binding pocket: A narrowing cleft that constricts during activation.
Topics: Animals; Binding Sites; Biotin; Cells, Cultured; Cysteine; Dose-Response Relationship, Drug; GABA Agonists; GABA Antagonists; GABA Modulators; gamma-Aminobutyric Acid; Ion Channel Gating; Ligands; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Protein Structure, Tertiary; Rats; Receptors, GABA-A; Structure-Activity Relationship; Sulfhydryl Reagents | 2001 |
Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface.
Topics: Adenosine Triphosphate; Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Biological Transport; Biotin; Biotinylation; Conserved Sequence; Cysteine; Disulfides; Dithiothreitol; Electrophysiology; Humans; Membrane Proteins; Mercaptoethanol; Molecular Sequence Data; Mutation; Oocytes; Protein Structure, Tertiary; Receptors, Purinergic P2; Receptors, Purinergic P2X; Reducing Agents; Sequence Homology, Amino Acid; Xenopus laevis | 2002 |
Peroxynitrite inactivates the human dopamine transporter by modification of cysteine 342: potential mechanism of neurotoxicity in dopamine neurons.
Topics: Antioxidants; Biological Transport; Biotin; Cell Line; Cysteine; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dose-Response Relationship, Drug; Free Radical Scavengers; Humans; Kidney; Membrane Glycoproteins; Membrane Transport Modulators; Membrane Transport Proteins; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Neurons; Neurotoxicity Syndromes; Peroxynitrous Acid; Structure-Activity Relationship; Substrate Specificity; Sulfhydryl Reagents; Transfection | 2002 |
Mutation of glutamate 155 of the GABAA receptor beta2 subunit produces a spontaneously open channel: a trigger for channel activation.
Topics: Animals; Binding Sites; Biotin; Cysteine; GABA-A Receptor Agonists; Glutamic Acid; Ion Channel Gating; Kinetics; Ligands; Mutagenesis, Site-Directed; Mutation; Patch-Clamp Techniques; Pentobarbital; Protein Conformation; Rats; Receptors, GABA-A; Recombinant Proteins; Xenopus laevis | 2004 |
Inorganic mercury interacts with cysteine residues (C451 and C474) of hOCT2 to reduce its transport activity.
Topics: Animals; Biological Transport; Biotin; CHO Cells; Cricetinae; Cricetulus; Cysteine; Humans; Kinetics; Mercuric Chloride; Organic Cation Transport Proteins; Organic Cation Transporter 2; Substrate Specificity; Tetraethylammonium | 2007 |
Outward stabilization of the S4 segments in domains III and IV enhances lidocaine block of sodium channels.
Topics: Anesthetics, Local; Anti-Arrhythmia Agents; Arginine; Binding Sites; Biotin; Cell Line; Cysteine; Dose-Response Relationship, Drug; Humans; Ion Channel Gating; Kinetics; Lidocaine; Membrane Potentials; Muscle Proteins; Mutation; NAV1.5 Voltage-Gated Sodium Channel; Protein Conformation; Protein Structure, Tertiary; Sodium Channel Blockers; Sodium Channels; Transfection | 2007 |
Setting up for the block: the mechanism underlying lidocaine's use-dependent inhibition of sodium channels.
Topics: Anesthetics, Local; Anti-Arrhythmia Agents; Arginine; Binding Sites; Biotin; Cell Line; Cysteine; Humans; Ion Channel Gating; Kinetics; Lidocaine; Membrane Potentials; Muscle Proteins; Mutation; NAV1.5 Voltage-Gated Sodium Channel; Protein Conformation; Protein Structure, Tertiary; Sodium Channel Blockers; Sodium Channels; Transfection | 2007 |