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A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid‐sensitive channel in sensory neurons
A new toxin (APETx2) from the sea anemone Anthopleura elegantissima is isolated, which inhibits ASIC3 homomeric channels and ASIC3‐containing heteromersic channels both in heterologous expression systems and in primary cultures of rat sensory neurons. Expand
Tarantulas: eight-legged pharmacists and combinatorial chemists.
  • P. Escoubas, L. Rash
  • Biology, Medicine
  • Toxicon : official journal of the International…
  • 1 April 2004
Tarantula venoms appear to be a good model for the discovery of novel compounds with important therapeutic potential, and for the study of the molecular evolution of peptide toxins. Expand
Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies.
Three novel peptides with the ability to inhibit voltage-dependent potassium channels in the shab (KV2) and shal (Kv4) subfamilies were identified from the venom of the African tarantulas and are new tools for the investigation of the physiological role of the different potassium channel subunits in cellular physiology. Expand
A tarantula peptide against pain via ASIC1a channels and opioid mechanisms
The analgesic properties of the peptide are suppressed by antagonists of the μ and δ-opioid receptors and are lost in Penk1−/− mice. Expand
Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton‐gated cation channels
Psalmotoxin 1 (PcTx1), the first potent and specific blocker of the ASIC1a proton‐sensing channel, has been successfully expressed in the Drosophila melanogaster S2 cell recombinant expression system used here for the first time to produce a spider toxin. Expand
AKAP150, a switch to convert mechano‐, pH‐ and arachidonic acid‐sensitive TREK K+ channels into open leak channels
It is shown that the A‐kinase‐anchoring protein AKAP150 is a constituent of native TREK‐1 channels that transforms low‐activity outwardly rectifying currents into robust leak conductances insensitive to AA, stretch and acidification. Expand
A rational nomenclature for naming peptide toxins from spiders and other venomous animals.
A rational nomenclature is introduced that can be applied to the naming of peptide toxins from spiders and other venomous animals to enable these toxins to be rationally classified, catalogued, and compared. Expand
Structure and pharmacology of spider venom neurotoxins.
Following diverse molecular evolution mechanisms, and in particular selective hypermutation, short spider peptides appear to have functionally diversified while retaining a conserved molecular scaffold. Expand
Venom landscapes: mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach.
This work shows that the venoms of Australian funnel-web spiders contain many hundreds of peptides that follow a bimodal distribution, and proposes that three-dimensional 'venom landscapes' derived from LC-MALDI analysis might have predictive value for the discovery of various groups of pharmacologically distinct toxins in complex venoms. Expand
Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton‐gated channels
A putative channel interaction surface is suggested for APETx2, encompassing its N terminus together with the type I‐β turn connecting β‐strands III and IV, which could play a role in the specificity observed for these different ion channel effectors. Expand