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Omega-conotoxin: direct and persistent blockade of specific types of calcium channels in neurons but not muscle.
- E. Mccleskey, A. Fox, D. Yoshikami
- BiologyProceedings of the National Academy of Sciences…
- 1 June 1987
The tissue and channel-type specificity and the directness and slow reversibility of the block are features that favor use of omega-conotoxin as a tool for purifying particular neuronal Ca2+ channels and defining their physiological function.
A new conus peptide ligand for mammalian presynaptic Ca2+ channels
Peptide neurotoxins from fish-hunting cone snails.
Five new omega-conotoxins that block presynaptic calcium channels are described, and the fact that they inhibit sequential steps in neuromuscular transmission suggests that their action is synergistic rather than additive.
Conus geographus toxins that discriminate between neuronal and muscle sodium channels.
Diversity of Conus neuropeptides.
It now seems that the Conus species will each use a distinctive assortment of peptides and that the pharmacological diversity in Conus venoms may be ultimately comparable to that of plant alkaloids or secondary metabolites of microorganisms.
Purification and sequence of a presynaptic peptide toxin from Conus geographus venom.
A novel toxin, omega-conotoxin (omega-CgTX), from the venom of the fish-eating marine mollusc Conus geographus has been purified and biochemically characterized, providing a potentially powerful probe for exploring the vertebrate presynaptic terminal.
Neuronal calcium channel antagonists. Discrimination between calcium channel subtypes using omega-conotoxin from Conus magus venom.
It is demonstrated that a combination of two omega-conotoxins can be used for biochemically defining receptor subtypes and suggested that these correspond to subtypes of neuronal Ca2+ channels.
Conotoxins, in retrospect.
Contulakin-G, an O-Glycosylated Invertebrate Neurotensin*
It is concluded that O-linked glycosylation appears to be a highly unusual strategy for increasing the efficacy of toxins directed against neurotransmitter receptors.
μ-Conotoxin PIIIA, a New Peptide for Discriminating among Tetrodotoxin-Sensitive Na Channel Subtypes
It is demonstrated that Arginine-14 (Arg14) is a key residue; substitution by alanine significantly decreases affinity and results in a toxin unable to block channel conductance completely, and μ-PIIIA provides a key for further discriminating pharmacologically among different sodium channel subtypes.