Results 131 to 140 of about 4,835 (174)

Deduction of functional peptide motifs in scorpion toxins

Journal of Peptide Science, 2006
AbstractScorpion toxins are important physiological probes for characterizing ion channels. Molecular databases have limited functional annotation of scorpion toxins. Their function can be inferred by searching for conserved motifs in sequence signature databases that are derived statistically but are not necessarily biologically relevant.
Tan, P.T.J., Brusic, V., Ranganathan, S.
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Scorpion Toxin Polyptides as Therapeutic Agents: An Overview

Protein & Peptide Letters, 2016
Scorpions are distributed throughout the world and numerous biological molecules are found in their venom most importantly peptide toxins. These toxins modulate the ion channels either by blocking the pore of the channel or by altering the voltage gating. Molecules which block the pores have been useful in deciphering the structure of the ion channels.
Janardhan, Bhavya, Niyonzima N, Francois, Veena S, More, Sunil S, More   +3 more
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β-Scorpion toxins

1997
Abstract β-Toxins are responsible for the life hazard constituted, in Central and South America, by scorpion stings. They are qualitatively and quantitatively the most important polypeptides of the venom. They are made of one single polypeptide chain of 60 to 66 amino acid residues crosslinked by four disulfide bridges (Possani et al ...
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Scorpion Toxins Affecting Insects

1992
Publisher Summary This chapter provides an overview of the scorpion toxins affecting insects. The scorpion toxins specific for insects are divided into two different categories—contraction-inducing toxins, which causes rapid excitatory contraction paralysis in Sarcophaga argyrostoma fly larvae, and depressant toxins, which induces a slow depressant ...
Erwann P. Loret, François Sampieri, Claude Granier, Françis Miranda, Hervé Rochat   +4 more
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Binding of .beta.-scorpion toxin: a physicochemical study

Biochemistry, 1984
The binding to rat brain synaptosomes of a beta-scorpion toxin, i.e., toxin II of Centruroides suffusus suffusus (Css II), was studied as a function of pH, temperature, and concentration of some monovalent and divalent cations. At 10 degrees C and pH 6.0, the specific binding of 125I-labeled Css II corresponds to a single class of noninteracting high ...
E, Jover, J, Bablito, F, Couraud
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Physiological Action of the Toxin of the Egyptian Scorpion

Nature, 1950
THE main physiological effects produced by the toxin of the Egyptian scorpion1 are: (1) inhibition of rabbit smooth muscle; (2) acceleration of the isolated rabbit and frog heart (antagonized by ergotoxin); (3) rise of blood pressure of the dog (reversed by ergotoxin); (4) vomiting, and contraction of intestine and bladder of rabbit and dog in the ...
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Scorpion Toxins and Potassium Channels

2000
Potassium channels are a group of proteins that have in common the property of selectively allowing the movement of K+ through aqueous pores in the membrane. Gating of these proteins occurs through conformational changes that are controlled by voltage and/or ligand binding.
Maria L. Garcia, Markus Hanner, Hans-Günther Knaus, Robert S. Slaughter, Gregory J. Kaczorowski   +4 more
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Enzymes and toxins of the scorpion venom Palamneus gravimanus

Toxicon, 1977
Abstract Hyaluronidase activity (300 units per mg protein) and alkaline phosphatase activity (0.62 × 10-3 units per mg protein) were found in the venom of the scorpion, Palamneus gravimanus. In addition, two toxins have been isolated from the crude venom by gel filtration on Sephadex G-100 and Sephadex G-25, and by isoelectric focusing. The molecular
R P, Wright, T K, Chan, L, Honetschlager, D E, Howell, G V, Odell   +4 more
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Unique interaction of scorpion toxins with the hERG channel

Journal of Molecular Recognition, 2004
AbstractERG potassium channels specify one component of the delayed rectifier in the heart and are likely to play an important functional role in other excitable cells. Compared to other K+ channels, the human ERG (hERG) channel possesses an unusually long S5‐P linker that presumably forms an alpha‐helix important for channel function.
Yuliya V, Korolkova, Gea-Ny, Tseng, Eugene V, Grishin   +2 more
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Respiratory arrhythmias produced by purified scorpion toxin

Toxicon, 1973
Abstract Bilateral section of vagi nerves and denervation of carotid bodies prevented the gasping, ataxic and periodic respirations produced by purified scorpion toxin ( Tityus serrulatus ) in the rat. The apnea recorded in intact rats after toxin injection was of long duration in comparison with that observed in denervated animals.
L, Freire-Maia, A D, Azevedo, V P, Costa VAL   +2 more
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