Journal ArticleDOI
New toxins acting on sodium channels from the scorpion Leiurus quinquestriatus hebraeus suggest a clue to mammalian vs insect selectivity.
Pierre Sautière,Sandrine Cestèle,Charles Kopeyan,Arlette Martinage,Hervé Drobecq,Yvon Doljansky,Dalia Gordon +6 more
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TLDR
Two new toxins were purified from Leiurus quinquestriatus hebraeus (Lqh) scorpion venom, Lqh II and LqH III, which represent two different scorpion toxin groups, the alpha- and alpha-like toxins, respectively, according to the structural and pharmacological criteria.About:
This article is published in Toxicon.The article was published on 1998-08-01. It has received 71 citations till now. The article focuses on the topics: Scorpion toxin & Buthus occitanus.read more
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Scorpion toxins specific for Na+-channels.
TL;DR: A classification containing 10 different groups of toxins is proposed in this review, based on functional and structural features of the known toxins, and the limited success obtained in the search for the site through which these peptides bind to the channels.
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Overview of scorpion toxins specific for Na+ channels and related peptides: biodiversity, structure-function relationships and evolution.
TL;DR: A critical view on problems associated with the study of these scorpion peptides is presented, drawing special attention to the points that need revision and to the subjects under intensive research at this moment, regarding scorpion toxins specific for Na(+) channels and the other related long-chain peptides recently described.
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Peptides and genes coding for scorpion toxins that affect ion-channels.
TL;DR: The entire repertoire of toxins, independently of their specificity, was analyzed together by computational programs and a phylogenetic tree was built showing two separate branches, showing clear similarities among them.
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Neurotoxins and Their Binding Areas on Voltage-Gated Sodium Channels
TL;DR: This review focuses on the current status of research on neurotoxins acting on VGSC, their contribution to further unravel the structure and function of VGSC and their potential as novel lead compounds in drug development.
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Voltage-gated sodium channel modulation by scorpion α-toxins
Frank Bosmans,Jan Tytgat +1 more
TL;DR: An overview on scorpion venoms, their alpha-toxins and the Na+ channel targets they are built for, as well as on the molecular determinants that govern the selectivity and affinity of this ‘inseparable duo’.
References
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Neurotoxins that Act on Voltage-Sensitive Sodium Channels in Excitable Membranes
TL;DR: This review focuses on experiments that have given insight into the cellular and molecular mechanisms of action of these toxins and have revealed common features of their interaction with voltage-sensi tive sodium channels.
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Cellular and molecular biology of voltage-gated sodium channels.
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Molecular Properties of Voltage-Sensitive Sodium Channels
TL;DR: This chapter will focus primarily on skeletal muscle calcium channels, which have been investigated most thoroughly in skeletal muscle which has a particularly high density of calcium channels.
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Molecular analysis of the para locus, a sodium channel gene in Drosophila.
TL;DR: The results support the conclusion that para encodes a functionally predominant class of sodium channels in Drosophila neurons and the para transcript appears to undergo alternative splicing to produce several distinct subtypes of this channel.
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Molecular Determinants of High Affinity Binding of α-Scorpion Toxin and Sea Anemone Toxin in the S3-S4 Extracellular Loop in Domain IV of the Na+ Channel α Subunit
TL;DR: Results indicate that nonidentical amino acids of the IVS3-S4 loop participate in α-scorpion toxin and sea anemone toxin binding to overlapping sites and that neighboring amino acid residues in theIVS3 segment contribute to the difference inα-sc Scorpion toxin binding affinity between cardiac and neuronal Na+ channels.