Results 181 to 190 of about 9,314 (214)

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
openaire   +1 more source

Les toxines des venins de scorpion

Annales de l'Institut Pasteur / Actualités, 1999
Les toxines de venins de scorpion sont des mini-proteines basiques, de 60–70 residus d'acides amines, possedant quatre ponts disulfure dans le cas des toxines modulant les canaux Na+ voltage-dependants des cellules excitables, et de 30–40 residus, avec trois ou quatre ponts disulfure, pour les toxines bloquant divers canaux K+.
Marie-France Martin-Eauclaire, Christian Legros, Pierre E. Bougis, Hervé Rochat   +3 more
openaire   +1 more source

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
openaire   +2 more sources

[The rational evolution of scorpion toxins].

Bioorganicheskaia khimiia, 1997
A theoretical method for the rational design of a "universal" scorpion toxin with a wider spectrum of specificity for K+ channels and a more stable alpha/beta-folding than in its natural homologues is described. On the basis of the analysis of molecular hydrophobic potentials (MHP) of the protein spatial structures, structural features for a family of ...
Zharavin , V.A., Golovanov, Alexander, Arsen'ev, A. S.   +2 more
openaire   +2 more sources

Tityus serrulatus Scorpion Venom and Toxins: An Overview

Protein & Peptide Letters, 2009
Tityus serrulatus is considered the most dangerous scorpion in South America and responsible for most of the fatal cases. This review will focus on Tityus serrulatus scorpion venom (Tsv), its long-chain Na(+)-channel toxins (NaTx), which include alpha- and beta-neurotoxins, short-chain K(+)-channel toxins (KTx), hyaluronidase, proteases and other ...
Cologna, Camila T., Marcussi, Silvana, Giglio, Jose R., Soares, Andreimar M., Arantes, Eliane C.   +4 more
openaire   +2 more sources

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
openaire   +2 more sources

Florescent scorpion toxin lights up tumours

New Scientist, 2007
The new “paint” allows surgeons to accurately pinpoint the edges of a tumour during surgery to remove all cancerous ...
openaire   +1 more source

Clostridioides difficile toxins: mechanisms of action and antitoxin therapeutics

Nature Reviews Microbiology, 2021
Dana Borden Lacy
exaly  

Gastric secretion induced by scorpion toxin

Toxicon, 1979
H M, Gonzaga, F, Alzamora, J R, Cunha-Melo, L, Freire-Maia   +3 more
openaire   +2 more sources

Nanobodies against AahII scorpion toxin

Toxicology Letters, 2009
Rahma Ben Abderrazek, Issam Hmila, Cécile Vincke, Zakaria Benlasfar, Hafedh Dabbek, Mohamed El Ayeb, Serge Muyldermans, Balkiss Bouhaouala-Zahar   +7 more
openaire   +1 more source