Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Expression of the standard scorpion alpha-toxin AaH II and AaH II mutants leading to the identification of some key bioactive elements.

Biochimica et biophysica acta - 25 May 2005

Legros Christian, Céard Brigitte, Vacher Hélène, Marchot Pascale, Bougis Pierre E, Martin-Eauclaire Marie-France

Abstract excerpt

The AaH II toxin from the scorpion Androctonus australis Hector is considered to be the standard alpha-toxin because it selectively binds with the highest known affinity to site 3 of mammalian voltage-activated Na+ channels (Na(v)) on rat brain synaptosomes but does not bind to insect synaptosomes. We generated two different constructs in pMALp allowing us to produce AaH II fused with the maltose-binding protein...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Neurotoxins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Recombinant Fusion Proteins

Share to Scorpion Venoms

Share to Sodium Channels

Share to Structure-Activity Relationship

Share to Synaptosomes

Source

Identifiers

PMID: 15725394
DOI: 10.1016/j.bbagen.2005.01.008

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expression of the standard scorpion alpha-toxin AaH II and AaH II mutants leading to the identification of some key bioactive elements.PMID 15725394Read ↗

Overview of scorpion toxins specific for Na+ channels and related peptides: biodiversity, structure-function relationships and evolution.Semantic proximity Read ↗

Evolutionary diversification of Mesobuthus α-scorpion toxins affecting sodium channels.Semantic proximity Read ↗

The amino acid sequence of toxin IV from the Androctonus australis scorpion: differing effects of natural mutations in scorpion alpha-toxins on their antigenic and toxic properties.Semantic proximity Read ↗

A robust platform for recombinant production of animal venom toxin modulators of ion channelsSemantic proximity Read ↗

Elucidation of the molecular basis of selective recognition uncovers the interaction site for the core domain of scorpion alpha-toxins on sodium channels.Semantic proximity Read ↗

[Solid-phase synthesis and biological characterization of S12A-HNTX-IV and R29A-HNTX-IV: two mutants of hainantoxin-IV].Semantic proximity Read ↗

Analysis of the effect of the scorpion toxin AaH-II on action potential generation in the axon initial segmentSemantic proximity Read ↗

Structure-activity relationship study of a scorpion toxin with high affinity for apamin-sensitive potassium channels by means of the solution structure of analogues.Semantic proximity Read ↗

[Natural alpha-conotoxins and their synthetic analogues in studies of nicotinic acetylcholine receptors].Semantic proximity Read ↗

The roles of conserved aromatic residues (Tyr5 and Tyr42) in interaction of scorpion toxin BmK AGP-SYPU1 with human Nav1.7.Semantic proximity Read ↗

Bacterial expression, NMR, and electrophysiology analysis of chimeric short/long-chain alpha-neurotoxins acting on neuronal nicotinic receptors.Semantic proximity Read ↗

Production in Escherichia coli, folding, purification and characterization of notexin with wild type sequence and with N-terminal and catalytic site mutations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.