Compounds > cystine

cystine and charybdotoxin

cystine has been researched along with charybdotoxin in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (80.00)18.2507
2000's0 (0.00)29.6817
2010's1 (20.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chino, N; Kimura, T; Kobayashi, Y; Kuroda, H; Kyogoku, Y; Lambert, P; Sakakibara, S; Takashima, H; Tamaoki, H; Watanabe, TX1
Dauplais, M; Drakopoulou, E; Gilquin, B; Guenneugues, M; Jamin, N; Ménez, A; Song, J; Vita, C1
Garcia, ML; Hanner, M; Kaczorowski, GJ; Kamassah, A; Knaus, HG; Schmalhofer, WA; Vianna-Jorge, R1
Gómez-Lagunas, F; Gurrola, GB; Olamendi-Portugal, T; Possani, LD1
Cao, Z; Chen, Z; Han, S; Li, W; Wu, Y; Zhuo, R1

Other Studies

5 other study(ies) available for cystine and charybdotoxin

ArticleYear
The cystine-stabilized alpha-helix: a common structural motif of ion-channel blocking neurotoxic peptides.
    Biopolymers, 1991, Volume: 31, Issue:10

    Topics: Amino Acid Sequence; Animals; Charybdotoxin; Cystine; Ion Channels; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Neurotoxins; Peptides; Protein Conformation; Scorpion Venoms; Sequence Homology, Nucleic Acid

1991
NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing.
    Biochemistry, 1997, Apr-01, Volume: 36, Issue:13

    Topics: Amino Acid Sequence; Aminobutyrates; Charybdotoxin; Cystine; Disulfides; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Folding; Protein Structure, Secondary

1997
The beta subunit of the high conductance calcium-activated potassium channel. Identification of residues involved in charybdotoxin binding.
    The Journal of biological chemistry, 1998, Jun-26, Volume: 273, Issue:26

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Cattle; Charybdotoxin; COS Cells; Cystine; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits; Large-Conductance Calcium-Activated Potassium Channel beta Subunits; Large-Conductance Calcium-Activated Potassium Channels; Molecular Sequence Data; Mutagenesis, Site-Directed; Potassium Channels; Potassium Channels, Calcium-Activated; Protein Conformation; Protein Structure, Secondary; Structure-Activity Relationship

1998
Two similar peptides from the venom of the scorpion Pandinus imperator, one highly effective blocker and the other inactive on K+ channels.
    Toxicon : official journal of the International Society on Toxinology, 1998, Volume: 36, Issue:5

    Topics: Amino Acid Sequence; Animals; Binding, Competitive; Brain; Charybdotoxin; Cystine; Disulfides; Molecular Sequence Data; Peptides; Potassium Channel Blockers; Rats; Scorpion Venoms; Sequence Homology, Amino Acid; Structure-Activity Relationship; Synaptosomes

1998
Fusion expression and purification of four disulfide-rich peptides reveals enterokinase secondary cleavage sites in animal toxins.
    Peptides, 2013, Volume: 39

    Topics: Amino Acid Motifs; Amino Acid Sequence; Base Sequence; Charybdotoxin; Chromatography, Affinity; Cloning, Molecular; Cystine; Enteropeptidase; Escherichia coli; Glutathione Transferase; Isoelectric Point; Molecular Sequence Data; Molecular Weight; Proteolysis; Recombinant Fusion Proteins; Scorpion Venoms; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2013