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

Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function.

The Journal of biological chemistry - 21 Jun 2002

Maggio Francesco, King Glenn F

Abstract excerpt

The Janus-faced atracotoxins (J-ACTXs) are a family of insect-specific excitatory neurotoxins isolated from the venom of Australian funnel web spiders. In addition to a strikingly asymmetric distribution of charged residues, from which their name is derived, these toxins contain an extremely rare vicinal disulfide bond. To shed light on the mechanism of action of these toxins and to enhance their utility as lead...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Arginine
Share to Circular Dichroism

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

Share to Disulfides

Share to Insecta

Share to Potassium

Share to Proline

Share to Tyrosine

Source

Identifiers

PMID: 11937509
DOI: 10.1074/jbc.M202297200

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

Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function.PMID 11937509Read ↗

Molecular surface of JZTX-V (β-Theraphotoxin-Cj2a) interacting with voltage-gated sodium channel subtype NaV1.4.Semantic proximity Read ↗

Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels.Semantic proximity Read ↗

Mutational analysis of ProTx-I and the novel venom peptide Pe1b provide insight into residues responsible for selective inhibition of the analgesic drug target NaV1.7.Semantic proximity Read ↗

Scanning Mutagenesis of ω-Atracotoxin-Hv1a Reveals a Spatially Restricted Epitope That Confers Selective Activity against Insect Calcium ChannelsSemantic proximity Read ↗

Diversification of a single ancestral gene into a successful toxin superfamily in highly venomous Australian funnel-web spiders.Semantic proximity Read ↗

Active Sites of Spinoxin, a Potassium Channel Scorpion Toxin, Elucidated by Systematic Alanine Scanning.Semantic proximity Read ↗

Understanding the molecular basis of toxin promiscuity: the analgesic sea anemone peptide APETx2 interacts with acid-sensing ion channel 3 and hERG channels via overlapping pharmacophores.Semantic proximity Read ↗

Structural and Functional Diversity of Peptide Toxins from Tarantula Haplopelma hainanum (Ornithoctonus hainana) Venom Revealed by Transcriptomic, Peptidomic, and Patch Clamp Approaches.Semantic proximity Read ↗

Three-fingered RAVERs: Rapid Accumulation of Variations in Exposed Residues of snake venom toxins.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 ↗

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

Mutant cycle analysis with modified saxitoxins reveals specific interactions critical to attaining high-affinity inhibition of hNaV1.7.Semantic proximity Read ↗

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