ArticleJournal of toxicology2012
Potassium Channels Blockers from the Venom of Androctonus mauretanicus mauretanicus.
Article in Journal of toxicology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed.
- Review
- Differential venom gland gene expression analysis of juvenile and adult scorpions Androctonus crassicauda.BMC genomics · 2022Article
- Cross Pharmacological, Biochemical and Computational Studies of a Human Kv3.1b Inhibitor fromInternational journal of molecular sciences · 2021Article
- Australian ScorpionBiomolecules · 2020Article
- In vitro studies with renal proximal tubule cells show direct cytotoxicity of Androctonus australis hector scorpion venom triggered by oxidative stress, caspase activation and apoptosis.Toxicon : official journal of the International Society on Toxinology · 2016Article
- Scorpion toxins prefer salt solutions.Journal of molecular modeling · 2015Article
- Scorpions: a presentation.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
- Dipeptidyl-peptidase-like-proteins confer high sensitivity to the scorpion toxin AmmTX3 to Kv4-mediated A-type K+ channels.The Journal of physiology · 2013Article
- Characterization of Functional Effects of Two New Active Fractions Isolated From Scorpion Venom on Neuronal CaBasic and clinical neuroscienceArticle
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
K(+) channels selectively transport K(+) ions across cell membranes and play a key role in regulating the physiology of excitable and nonexcitable cells. Their activation allows the cell to repolarize after action potential firing and reduces excitability, whereas channel inhibition increases excitability. In eukaryotes, the pharmacology and pore topology of several structural classes of K(+) channels have been well characterized in the past two decades. This information has come about through the extensive use of scorpion toxins. We have participated in the isolation and in the characterization of several structurally distinct families of scorpion toxin peptides exhibiting different K(+) channel blocking functions. In particular, the venom from the Moroccan scorpion Androctonus mauretanicus mauretanicus provided several high-affinity blockers selective for diverse K(+) channels (SK(Ca), K(v)4.x, and K(v)1.x K(+) channel families). In this paper, we summarize our work on these toxin/channel interactions.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.