cysteine and charybdotoxin

cysteine has been researched along with charybdotoxin in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's6 (60.00)18.2507
2000's3 (30.00)29.6817
2010's1 (10.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Buresh, TL; Conklin, JL; Murray, JA; O'Meara, BW; Picken, H; Shibata, EF1
Kolmakova-Partensky, L; Miller, C; Shimony, E; Sun, T1
Dang, W; Kozlowski, E; Miller, C; Naini, AA; Shaikh, T; Shimony, E1
Aniort, V; Bouet, F; Drakopoulou, E; Ménez, A; Neyton, J; Virelizier, H; Vita, C; Vizzavona, J1
Barber, JE; Bradley, KK; Bradley, ME; Buxton, IL; McGaw, T1
Abassi, A; Ali, SA; Kayed, R; Schütz, J; Stoeva, S; Voelter, W; Zaidi, ZH1
Buxton, IL; Kaiser, RA; Malmquist, NA; Tichenor, S1
Jiang, M; Liu, J; Pardo-Lopez, L; Possani, LD; Tseng, GN; Zhang, M1
Chen, X; Ding, J; Li, H; Wu, G; Wu, H; Xu, T; Yao, J; Yao, L; Zhang, N; Zhou, Y; Zhou, Z1
Hua, Z; Kobertz, WR1

Other Studies

10 other study(ies) available for cysteine and charybdotoxin

ArticleYear
Nitric oxide modulates a calcium-activated potassium current in muscle cells from opossum esophagus.
    The American journal of physiology, 1995, Volume: 269, Issue:4 Pt 1

    Topics: Animals; Calcium; Charybdotoxin; Cyclic GMP; Cysteine; Electric Conductivity; Electrophysiology; Esophagus; Female; Male; Muscle, Smooth; Nitric Oxide; Opossums; Potassium; S-Nitrosothiols; Thionucleotides

1995
Engineering a uniquely reactive thiol into a cysteine-rich peptide.
    Protein engineering, 1994, Volume: 7, Issue:4

    Topics: Animals; Cells, Cultured; Charybdotoxin; Cysteine; Escherichia coli; Genetic Engineering; Models, Molecular; Neurotoxins; Oxidation-Reduction; Point Mutation; Potassium Channel Blockers; Potassium Channels; Protein Binding; Protein Folding; Recombinant Fusion Proteins; Rhodamines; Scorpion Venoms; Sulfhydryl Compounds; Sulfhydryl Reagents

1994
Interaction of Ca2(+)-activated K+ channels with refolded charybdotoxins mutated at a central interaction residue.
    Neuropharmacology, 1996, Volume: 35, Issue:7

    Topics: Charybdotoxin; Cysteine; Escherichia coli; Large-Conductance Calcium-Activated Potassium Channels; Mutation; Ornithine; Potassium Channels; Potassium Channels, Calcium-Activated; Protein Binding; Protein Conformation; Protein Folding; Recombinant Fusion Proteins

1996
Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation.
    Biochemistry, 1998, Feb-03, Volume: 37, Issue:5

    Topics: Amino Acid Sequence; Animals; Charybdotoxin; Circular Dichroism; Conserved Sequence; Crystallography, X-Ray; Cysteine; Disulfides; Evolution, Molecular; Models, Molecular; Molecular Sequence Data; Muscle, Skeletal; Potassium Channel Blockers; Protein Conformation; Protein Folding; Rats; Structure-Activity Relationship

1998
Nitric oxide relaxes human myometrium by a cGMP-independent mechanism.
    The American journal of physiology, 1998, Volume: 275, Issue:6

    Topics: Aminoquinolines; Charybdotoxin; Cyclic GMP; Cysteine; Enzyme Inhibitors; Female; Guanylate Cyclase; Humans; Methylene Blue; Myometrium; Nitric Oxide; Nitric Oxide Donors; Nitroso Compounds; S-Nitrosothiols; Uterine Contraction

1998
Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom.
    Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, 1998, Volume: 121, Issue:4

    Topics: Animals; Charybdotoxin; Chromatography, High Pressure Liquid; Cysteine; Molecular Sequence Data; Molecular Weight; Peptide Fragments; Scorpion Venoms; Scorpions; Sequence Homology, Amino Acid

1998
NO-induced relaxation of labouring and non-labouring human myometrium is not mediated by cyclic GMP.
    British journal of pharmacology, 2001, Volume: 134, Issue:1

    Topics: Charybdotoxin; Cyclic GMP; Cysteine; Dose-Response Relationship, Drug; Enzyme Inhibitors; Female; Guanylate Cyclase; Humans; In Vitro Techniques; Labor, Obstetric; Molsidomine; Muscle Relaxation; Muscle, Smooth; Myometrium; Nitric Oxide; Nitric Oxide Donors; Nitroso Compounds; Oxadiazoles; Oxytocin; Penicillamine; Peptides; Pregnancy; Quinoxalines; S-Nitrosothiols; Scorpion Venoms; Time Factors; Uterus

2001
Mapping the binding site of a human ether-a-go-go-related gene-specific peptide toxin (ErgTx) to the channel's outer vestibule.
    The Journal of biological chemistry, 2002, May-10, Volume: 277, Issue:19

    Topics: Amino Acid Sequence; Binding Sites; Calcium Channel Blockers; Cation Transport Proteins; Charybdotoxin; Cysteine; DNA-Binding Proteins; DNA, Complementary; Dose-Response Relationship, Drug; Electrophysiology; ERG1 Potassium Channel; Ether-A-Go-Go Potassium Channels; Humans; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Potassium; Potassium Channels; Potassium Channels, Voltage-Gated; Protein Binding; Scorpion Venoms; Sequence Homology, Amino Acid; Shaker Superfamily of Potassium Channels; Tetraethylammonium; Time Factors; Trans-Activators; Transcriptional Regulator ERG

2002
BmP09, a "long chain" scorpion peptide blocker of BK channels.
    The Journal of biological chemistry, 2005, Apr-15, Volume: 280, Issue:15

    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
Chemical derivatization and purification of peptide-toxins for probing ion channel complexes.
    Methods in molecular biology (Clifton, N.J.), 2013, Volume: 995

    Topics: Animals; Cells, Cultured; Charybdotoxin; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Reverse-Phase; Cysteine; Hydrophobic and Hydrophilic Interactions; KCNQ1 Potassium Channel; Maleimides; Membrane Potentials; Potassium Channel Blockers; Potassium Channels, Voltage-Gated; Protein Binding; Staining and Labeling

2013