ReviewProtein & cell2011
Exploring the obscure profiles of pharmacological binding sites on voltage-gated sodium channels by BmK neurotoxins.
Review in Protein & cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Mass spectrometry-based top-down and bottom-up approaches for proteomic analysis of the Moroccan Buthus occitanus scorpion venom.FEBS open bio · 2021Article
- Modulatory effects of bufalin, an active ingredient from toad venom on voltage-gated sodium channels.Molecular biology reports · 2018Article
- Allosteric interactions between receptor site 3 and 4 of voltage-gated sodium channels: a novel perspective for the underlying mechanism of scorpion sting-induced pain.The journal of venomous animals and toxins including tropical diseases · 2015Article
- Recombinant expression and functional characterization of martentoxin: a selective inhibitor for BK channel (α + β4).Toxins · 2014Article
- A first exploration of the venom of the Buthus occitanus scorpion found in southern France.Toxicon : official journal of the International Society on Toxinology · 2014Article
- Activation of mammalian target of rapamycin contributes to pain nociception induced in rats by BmK I, a sodium channel-specific modulator.Neuroscience bulletin · 2014Article
- Activation of mammalian target of rapamycin mediates rat pain-related responses induced by BmK I, a sodium channel-specific modulator.Molecular pain · 2013Article
- Pharmacological kinetics of BmK AS, a sodium channel site 4-specific modulator on Nav1.3.Neuroscience bulletin · 2012Article
- Mining the virgin land of neurotoxicology: a novel paradigm of neurotoxic peptides action on glycosylated voltage-gated sodium channels.Journal of toxicology · 2012Article
- Neurotoxins and their binding areas on voltage-gated sodium channels.Frontiers in pharmacology · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diverse subtypes of voltage-gated sodium channels (VGSCs) have been found throughout tissues of the brain, muscles and the heart. Neurotoxins extracted from the venom of the Asian scorpion Buthus martensi Karsch (BmK) act as sodium channel-specific modulators and have therefore been widely used to study VGSCs. α-type neurotoxins, named BmK I, BmK αIV and BmK abT, bind to receptor site-3 on VGSCs and can strongly prolong the inactivation phase of VGSCs. In contrast, β-type neurotoxins, named BmK AS, BmK AS-1, BmK IT and BmK IT2, occupy receptor site-4 on VGSCs and can suppress peak currents and hyperpolarize the activation kinetics of sodium channels. Accumulating evidence from binding assays of scorpion neurotoxins on VGSCs, however, indicate that pharmacological sensitivity of VGSC subtypes to different modulators is much more complex than that suggested by the simple α-type and β-type neurotoxin distinction. Exploring the mechanisms of possible dynamic interactions between site 3-/4-specific modulators and region- and/or species-specific subtypes of VGSCs would therefore greatly expand our understanding of the physiological and pharmacological properties of diverse VGSCs. In this review, we discuss the pharmacological and structural diversity of VGSCs as revealed by studies exploring the binding properties and cross-competitive binding of site 3- or site 4-specific modulators in VGSC subtypes in synaptosomes from distinct tissues of diverse species.
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