Results 171 to 180 of about 5,580 (197)

Scorpion Toxins (a and /J)

2000
Abstract experimental neurobiologist and of importance for the clinical neurotoxicologist. The selectivity of these compounds is employed experimentally as a tool to localize ion channels in nerve, muscle, neuromuscular junctions, and other structures.
openaire   +1 more source

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

Scorpion toxins interact with nicotinic acetylcholine receptors

FEBS Letters, 2019
Neurotoxins are among the main components of scorpion and snake venoms. Scorpion neurotoxins affect voltage‐gated ion channels, while most snake neurotoxins target ligand‐gated ion channels, mainly nicotinic acetylcholine receptors (nAChRs). We report that scorpion venoms inhibit α‐bungarotoxin binding to both muscle‐type nAChR from Torpedo californica
Igor E. Kasheverov, Peter B. Oparin, Maxim N. Zhmak, Natalya S. Egorova, Igor A. Ivanov, Andrei M. Gigolaev, Oksana V. Nekrasova, Marina V. Serebryakova, Denis S. Kudryavtsev, Nikita A. Prokopev, Anh N. Hoang, Victor I. Tsetlin, Alexander A. Vassilevski, Yuri N. Utkin   +13 more
openaire   +2 more sources

Scorpion toxin: Specific binding to rat synaptosomes

Biochemical and Biophysical Research Communications, 1978
Summary The protein neurotoxin II from the venom of the scorpion Androctonus australis Hector was labeled with 125I by the lactoperoxidase method to a specific radioactivity of about 100 μCi/μg without loss of biological activity. The labeled neurotoxin binds specifically to a single class of non interacting binding sites of high affinity (KD = 0 ...
E, Jover, N, Martin-Moutot, F, Couraud, H, Rochat   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

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

Novel Australian Scorpion toxins

2012
Over hundreds of millions of years of evolutionary fine-tuning, animal venoms have evolved into potent chemical cocktails utilized for predation and defence. Venoms typically contain hundreds of pharmacologically diverse bioactive peptides, thus venomous animals are natural repositories containing vast arrays of toxins with potential pharmaceutical and
openaire   +1 more source

Evidence for the existence of a common ancestor of scorpion toxins affecting ion channels

Journal of Biochemical and Molecular Toxicology, 2003
Cao Zhijian, Wu Yingliang, Liu Wanhong   +2 more
exaly  

Correlation of Venom Toxinome Composition of Indian Red Scorpion (Mesobuthus tamulus) with Clinical Manifestations of Scorpion Stings: Failure of Commercial Antivenom to Immune-Recognize the Abundance of Low Molecular Mass Toxins of This Venom

Journal of Proteome Research, 2020
Bhabana Das, Aparup Patra, Ashis K Mukherjee   +2 more
exaly  

Isolation and characterization of two novel scorpion toxins: The α-toxin-like CeII8, specific for Nav1.7 channels and the classical anti-mammalian CeII9, specific for Nav1.4 channels

Toxicon, 2010
Thomas Vandendriessche, Timoteo Olamendi-Portugal, Fernando Z Zamudio   +2 more
exaly