Cloning and characterization of BmK86, a novel K+-channel blocker from scorpion venom

X Mao, Z Cao, S Yin, Y Ma, Y Wu, W Li - Biochemical and biophysical …, 2007 - Elsevier
Scorpion venom represents a tremendous hitherto unexplored resource for understanding
ion channels. BmK86 is a novel K+-channel toxin gene isolated from a cDNA library of …

Molecular cloning, genomic organization and functional characterization of a new short‐chain potassium channel toxin‐like peptide BmTxKS4 from Buthus martensii …

S Jiqun, X Xiuling, C Zhijian, L Wanhong… - … of Biochemical and …, 2004 - Wiley Online Library
Scorpion venom contains many small polypeptide toxins, which can modulate Na+, K+, Cl−,
and Ca2+ ion–channel conductance in the cell membrane. A full‐length cDNA sequence …

Characterization of the first K+ channel blockers from the venom of the Moroccan scorpion Buthus occitanus Paris

MF Martin-Eauclaire, B Céard, M Belghazi, R Lebrun… - Toxicon, 2013 - Elsevier
The availability of a large variety of specific blockers, which inhibit different K+ currents,
would help to elucidate their differences in physiological function. Short peptide toxins …

Expression of recombinant α-toxin BmKM9 from scorpion Buthus martensii Karsch and its functional characterization on sodium channels

F Yang, S Liu, Y Zhang, C Qin, L Xu, W Li, Z Cao, W Li… - Peptides, 2018 - Elsevier
Scorpion toxins are invaluable pharmacological tools for studying ion channels and
potential drugs for channelopathies. The long-chain toxins from scorpion venom with four …

A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+ channels, isolated from Heterometrus spinnifer (Scorpionidae) venom

B LEBRUN, R ROMI-LEBRUN… - Biochemical …, 1997 - portlandpress.com
A new toxin, named HsTX1, has been identified in the venom of Heterometrus spinnifer
(Scorpionidae), on the basis of its ability to block the rat Kv1. 3 channels expressed in …

Purification, Characterization, and Synthesis of Three Novel Toxins from the Chinese Scorpion Buthus martensi, Which Act on K+ Channels

R Romi-Lebrun, B Lebrun, MF Martin-Eauclaire… - Biochemistry, 1997 - ACS Publications
Three novel toxins belonging to the scorpion K+ channel-inhibitor family were purified to
homogeneity from the venom of the Chinese scorpion Buthus martensi. They have been …

Molecular dissection of venom from Chinese scorpion Mesobuthus martensii: identification and characterization of four novel disulfide-bridged venom peptides

XC Zeng, F Luo, WX Li - Peptides, 2006 - Elsevier
Scorpion venom is composed of a large repertoire of biologically active polypeptides.
However, most of these peptides remain to be identified and characterized. In this paper, we …

Molecular cloning and genomic organization of a K+ channel toxin from the Chinese scorpion Buthus martensii Karsch

XC Zeng, ZH Zhu, WX Li, SY Zhu, F Peng, X Mao, H Liu - Toxicon, 2001 - Elsevier
A full-length cDNA encoding the precursor of a K+ channel toxin (BmTX2) was first isolated
from a venom-gland cDNA library of the Chinese scorpion Buthus martensii Karsch. The …

[HTML][HTML] A new class of scorpion toxin binding sites related to an A-type K+ channel: pharmacological characterization and localization in rat brain

H Vacher, R Romi-Lebrun, C Mourre, B Lebrun… - FEBS letters, 2001 - Elsevier
A new scorpion toxin (3751.8 Da) was isolated from the Buthus martensi venom, sequenced
and chemically synthesized (sBmTX3). The A-type current of striatum neurons in culture …

Two dyad-free Shaker-type K+ channel blockers from scorpion venom

L Zhu, B Gao, L Luo, S Zhu - Toxicon, 2012 - Elsevier
Most of scorpion toxins affecting voltage-gated K+ channels (KTxs) contain a functional dyad
composed of a lysine and an aromatic amino acid separated by a suitable distance. By …