Characterization of cationic binding sites of neurotoxins from venom of the scorpion (Centruroides sculpturatus Ewing) using lanthanides as binding probes
References (33)
- et al.
Structure of Variant-3 scorpion neurotoxin from Centruroides sculpturatus Ewing, refined at 1.8 Å resolution
J. Mol. Biol.
(1983) - et al.
Amino acid sequences of neurotoxic protein variants from the venom of Centruroides sculpturatus Ewing
Arch. Bioch. Biophys.
(1974) - et al.
Amino acid sequence of Neurotoxin I from Centruroides sculpturatus Ewing
Arch. Bioch. Biophys.
(1975) - et al.
Preliminary X-ray investigation of Variant-2 scorpion toxin from Centruroides sculpturatus Ewing
J. biol. Chem.
(1984) - et al.
Architecture of scorpion neurotoxins: a class of membrane-binding proteins
TIBS
(1981) - et al.
The three-dimensional structure of scorpion neurotoxins
Toxicon
(1982) - et al.
Lanthanide probes in biological systems: characterization of luminescence excitation spectra of terbium complexes with proteins
Biophys. Chem.
(1981) - et al.
Terbium binding to troponin C: binding stoichiometry and structural changes induced in the protein
Arch. Biochem. Biophys.
(1980) - et al.
Protein measurement with the Folin phenol reagent
J. biol. Chem.
(1951) - et al.
Scatchard plot: common misinterpretation of binding experiments
Analyt. Biochem.
(1980)
Interaction of proteins with hydrogen ions and other small ions and molecules
Oscillation in resting tension of chick skeletal muscle treated with Toxin V from scorpion venom, reduced [calcium] and cadmium
Comp. Biochem. Physiol.
(1982)
Three-dimensional structures of scorpion neurotoxins
Terbium(III) emission as a probe of calcium(II) binding sites in proteins
J. Am. Chem. Soc.
(1976)
Classification of scorpion toxins according to amino acid composition and sequence
J. Mol. Evol.
(1984)
Binding of lanthanides and of divalent metal ions to porcine trypsin
Biochemistry
(1974)
Cited by (3)
Biochemical characterization and insecticidal activity of isolated peptides from the venom of the scorpion Centruroides tecomanus
2022, ToxiconCitation Excerpt :However, in the pharmacological group of MIBTXs, two toxins isolated from scorpions Tityus bahiensis and T. serrulatus have high percentages of identity with Ct-IT1: Tb2-II (59.09%) and Ts1 (58.46%), respectively (Pimenta et al., 2001; Sampaio et al., 1991). Ct-IT toxins also share some identity with Ts2 and CsE-V, isolated from the scorpions T. serrulatus and C. sculpturatus, respectively (David et al., 1991; Sampaio et al., 1991), despite these last toxins belong to α-NaScTxs. CsE-V, an Old World-like neurotoxin isolated from the venom of this New World scorpion, is an insect-specific neurotoxin with high specificity for insect sodium channels (Jablonsky et al., 2001).
Isolation and neurotoxicity of four low molecular weight toxins isolated from the venom of scorpion, Vachonus atrostriatus
1996, Pakistan Journal of Zoology
Copyright © 1991 Published by Elsevier Ltd.