Michael Ellison

TL;DR: The isolation and characterization of two peptide toxins from Conus ermineus venom targeted to nicotinic acetylcholine receptors (nAChRs) are described, which represent novel probes for the α/γ as well as theα/δ binding sites of the nAChR.

TL;DR: The identification and characterization of a novel polypeptide from the venom of a predatory marine snail Conus striatus that specifically disrupts the desensitization of AMPA receptors (AMPARs) are reported, providing insight into the mechanisms that regulate receptor desensitized state and revealing the fundamental importance of desensItization for regulating neural function.

TL;DR: The isolation and characterization of a novel Conus peptide from venom milked from Hawaiian specimens of Conus obscurus and results indicate that the αA-conotoxin family is both more structurally diverse and broadly distributed than previously believed.

TL;DR: It is speculated that the alpha4/3 toxins may be a rich source of functionally diverse all-alpha subunit nAChR inhibitors, and models of receptor-toxin binding that may account for the different subtype specificities of alpha 4/3 peptides are derived.