Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: A new fold for an HERG toxin
B Chagot, S Diochot, C Pimentel… - Proteins: Structure …, 2005 - Wiley Online Library
APETx1 is a 42‐amino acid toxin purified from the venom of the sea anemone Anthopleura
elegantissima. This cysteine‐rich peptide possesses three disulfide bridges (C4–C37, C6 …
elegantissima. This cysteine‐rich peptide possesses three disulfide bridges (C4–C37, C6 …
Maurotoxin versus Pi1/HsTx1 scorpion toxins: Toward new insights in the understanding of their distinct disulfide bridge patterns
Maurotoxin (MTX) is a scorpion toxin acting on several K+ channel subtypes. It is a 34-
residue peptide cross-linked by four disulfide bridges that are in an" uncommon" …
residue peptide cross-linked by four disulfide bridges that are in an" uncommon" …
Evolutionary trace analysis of scorpion toxins specific for K‐channels
S Zhu, I Huys, K Dyason, F Verdonck… - … Structure, Function, and …, 2004 - Wiley Online Library
Scorpion α‐K+ channel toxins are a large family of polypeptides with a similar structure but
diverse pharmacological activities. Despite many structural and functional data available at …
diverse pharmacological activities. Despite many structural and functional data available at …
Developing a comparative docking protocol for the prediction of peptide selectivity profiles: investigation of potassium channel toxins
PC Chen, S Kuyucak - Toxins, 2012 - mdpi.com
During the development of selective peptides against highly homologous targets, a reliable
tool is sought that can predict information on both mechanisms of binding and relative …
tool is sought that can predict information on both mechanisms of binding and relative …
Design of a disulfide-less, pharmacologically inert, and chemically competent analog of maurocalcine for the efficient transport of impermeant compounds into cells
N Ram, N Weiss, I Texier-Nogues, S Aroui… - Journal of biological …, 2008 - ASBMB
Maurocalcine is a 33-mer peptide initially isolated from the venom of a Tunisian scorpion. It
has proved itself valuable as a pharmacological activator of the ryanodine receptor and has …
has proved itself valuable as a pharmacological activator of the ryanodine receptor and has …
Solution structure of two insect‐specific spider toxins and their pharmacological interaction with the insect voltage‐gated Na+ channel
Abstract δ‐PaluIT1 and δ‐paluIT2 are toxins purified from the venom of the spider
Paracoelotes luctuosus. Similar in sequence to μ‐agatoxins from Agelenopsis aperta, their …
Paracoelotes luctuosus. Similar in sequence to μ‐agatoxins from Agelenopsis aperta, their …
A list of animal toxins and some other natural products with biological activity.
RDG Theakston, AS Kamiguti - 2002 - cabidigitallibrary.org
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Chemical synthesis and characterization of Pi1, a scorpion toxin from Pandinus imperator active on K+ channels
Z Fajloun, E Carlier, C Lecomte, S Geib… - European Journal of …, 2000 - Wiley Online Library
Pi1 is a 35‐residue toxin cross‐linked by four disulfide bridges that has been isolated from
the venom of the chactidae scorpion Pandinus imperator. Due to its very low abundance in …
the venom of the chactidae scorpion Pandinus imperator. Due to its very low abundance in …