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Special Issue "Ion Channels as a Therapeutic Target: Drug Design and Pharmacological Investigation 2.0. [PDF]
Guerrini G, Giovannoni MP.
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The Conopeptide αD-FrXXA, an Inhibitor of Voltage-Gated Potassium Channels. [PDF]
Martínez-Hernández L +3 more
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Toxicon, 2006
In the four decades since toxinologists in Australia and elsewhere started to investigate the active constituents of venomous cone snails, a wealth of information has emerged on the various classes of peptides and proteins that make their venoms such potent bioactive cocktails.
Raymond S, Norton, Baldomero M, Olivera
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In the four decades since toxinologists in Australia and elsewhere started to investigate the active constituents of venomous cone snails, a wealth of information has emerged on the various classes of peptides and proteins that make their venoms such potent bioactive cocktails.
Raymond S, Norton, Baldomero M, Olivera
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I‐conotoxin superfamily revisited
Journal of Peptide Science, 2006AbstractThe I‐conotoxin superfamily (I‐Ctx) is known to have four disulfide bonds with the cysteine arrangement C‐C‐CC‐CC‐C‐C, and the members inhibit or modify ion channels of nerve cells. Recently, Olivera and co‐workers (FEBS J. 2005; 272: 4178–4188) have suggested that the previously described I‐Ctx should now be divided into two different gene ...
Gough, Julie +4 more
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Conotoxins: Chemistry and Biology
Chemical Reviews, 2019The venom of the marine predatory cone snails (genus Conus) has evolved for prey capture and defense, providing the basis for survival and rapid diversification of the now estimated 750+ species. A typical Conus venom contains hundreds to thousands of bioactive peptides known as conotoxins.
Ai-Hua Jin +7 more
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Transforming conotoxins into cyclotides: Backbone cyclization of P‐superfamily conotoxins
Peptide Science, 2015ABSTRACTPeptide backbone cyclization is a widely used approach to improve the activity and stability of small peptides but until recently it had not been applied to peptides with multiple disulfide bonds. Conotoxins are disulfide‐rich conopeptides derived from the venoms of cone snails that have applications in drug design and development.
Akcan, Muharrem +9 more
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1996
Venom is a mixture of various substances produced in a specific gland in the body of the venomous animal and introduced through a piercing injecting mechanism into the body of another animal in order to paralyze it or to kill it. In nature, venoms are employed by slow predatory animals in order to capture through an immediate paralysis their relatively
E, Zlotkin +3 more
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Venom is a mixture of various substances produced in a specific gland in the body of the venomous animal and introduced through a piercing injecting mechanism into the body of another animal in order to paralyze it or to kill it. In nature, venoms are employed by slow predatory animals in order to capture through an immediate paralysis their relatively
E, Zlotkin +3 more
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Conotoxins and their regulatory considerations
Regulatory Toxicology and Pharmacology, 2014Venom derived peptides from marine cone snails, conotoxins, have demonstrated unique pharmacological targeting properties that have been pivotal in advancing medical research. The awareness of their true toxic origins and potent pharmacological nature is emphasized by their 'select agent' classification by the US Centers for Disease Control and ...
Parashar Thapa +3 more
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Conotoxin-sensitive and conotoxin-resistant Ca2+ currents in fish retinal ganglion cells
Journal of Neurobiology, 1996Using whole-cell patch-clamp methods, we tested whether omega-toxins from Conus block voltage-gated Ca2+ currents in teleost central neurons. The fractions omega-CTx-GVIA and omega-CTx-MVIIC, together with omega-toxins from Agelenopsis, the dihydropyridine BAY-K-8644, and voltage steps, produced effects indicating three types of Ca2+ current in ...
V P, Bindokas, A T, Ishida
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