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Creator | Title | Description | Subject | Date |
1 |
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Olivera, Baldomero M. | Block of Shaker K+ channels by ĸ-conotoxin PVIIA is state dependent | ĸ-conotoxin PVIIA is the first conotoxin known to interact with voltage-gated potassium channels by inhibiting Shaker-mediated currents. We studied the mechanism of inhibition and concluded that PVIIA blocks the ion pore with a 1:1 stoichiometry and that binding to open or closed channels is very d... | Conotoxins; k-conotoxin PVIIA; Potassium channel blockers; Shaker K+ channels | 1999 |
2 |
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Olivera, Baldomero M.; McIntosh, J. Michael | Novel post-translational modification involving bromination of tryptophan: identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom | We report a novel post-translational modification involving halogenation of tryptophan in peptides recovered from the venom of carnivorous marine cone snails (Conus). The residue, L-6-bromotryptophan, was identified in the sequence of a heptapeptide, isolated from Conus imperialis, a worm-hunting... | Conotoxins; Conus imperialis; Conus radiatus; L-6-bromotryptophan | 1997 |
3 |
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Olivera, Baldomero M.; Yoshikami, Doju; Bulaj, Grzegorz | Structural basis for tetrodotoxin-resistant sodium channel binding by μ-conotoxin SmIIIA | SmIIIA is a new μ-conotoxin isolated recently from Conus stercusmuscarum. Although it shares several biochemical characteristics with other μ-conotoxins (the arrangement of cysteine residues and a conserved arginine believed to interact with residues near the channel pore), it has several distin... | Conotoxins; Conotoxin SmIIIA; Tetrodotoxin | 2003 |
4 |
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Olivera, Baldomero M. | T-superfamily of conotoxins | We report the discovery and initial characterization of the T-superfamily of conotoxins. Eight different T-superfamily peptides from five Conus species were identified; they share a consensus signal sequence, and a conserved arrangement of cysteine residues (- -CC- -CC-). T-superfamily peptides... | Conotoxins; T-superfamily | 1999 |
5 |
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Olivera, Baldomero M. | Nicotinic acetylcholine receptor ligand of unique specificity, α-conotoxin ImI | We report the isolation, characterization, and total synthesis of a small peptide ligand for nicotinic acetylcholine receptors (nAChRs). It is highly active against the neuromuscular receptor in frog but noitn mice. In contrast, it induces seizures when injected centrally in mice and rats, suggesti... | Conotoxins; a-conotoxin ImI | 1994 |
6 |
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Olivera, Baldomero M.; McIntosh, J. Michael | Nuclear magnetic resonance solution conformation of α-conotoxin AuIB, an α3ß4 subtype-selective neuronal nicotinic acetylcholine receptor antagonist | The neuronal nicotinic acetylcholine receptors constitute a highly diverse group, with subtypes consisting of pentameric combinations of α and ß subunits. α-Conotoxins are a homologous series of small peptides that antagonize these receptors. We present the three-dimensional solution structure ... | Conotoxins; a-conotoxin AuIB | 2000 |
7 |
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Olivera, Baldomero M.; McIntosh, J. Michael | Solution structure of αA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus | We report the solution three-dimensional structure of an αA-conotoxin EIVA determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. The αA-conotoxin EIVA consists of 30 amino acids representing the largest peptide among the α/αAfamily conotoxins discovered so f... | Conotoxins; A-conotoxin EIVA; Conus ermineus | 2003 |
8 |
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Olivera, Baldomero M.; McIntosh, J. Michael | Isolation and characterization of a novel Conus peptide with apparent antinociceptive activity | Cone snails are tropical marine mollusks that envenomate prey with a complex mixture of neuropharmacologically active compounds. We report the discovery and biochemical characterization of a structurally unique peptide isolated from the venom of Conus marmoreus. The new peptide, mr10a, potently incr... | Conotoxins; Conus peptides; Conus marmoreus; mr10a; antinociceptive activity | 2000 |
9 |
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Olivera, Baldomero M.; Ireland, Chris M. | NMR structures of conotoxins | This review discusses the methodology, structural details, and biological implications regarding NMR structures of conotoxins. NMR and molecular modeling techniques have improved to the point that three-dimensional structures of conotoxins can now be determined with a significant degree of confiden... | Conotoxins | 1996 |
10 |
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Olivera, Baldomero M.; Yoshikami, Doju; Bulaj, Grzegorz | Post-translational amino acid isomerization: a functionally important D-amino acid in an excitatory peptide | The post-translational modification of an L- to a D-amino acid has been documented in relatively few gene products, mostly in small peptides under 10 amino acids in length. In this report, we demonstrate that a 46-amino acid polypeptide toxin has one D-phenylalanine at position 44, and that the ... | D-amino acid; Excitatory peptides; Conotoxins | 2005 |
11 |
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Olivera, Baldomero M.; Hillyard, David R.; Gray, William Robert | ĸ-Conotoxin PVIIA is a peptide inhibiting the Shaker K+ channel | ĸ-Conotoxin PVIIA (k-PVIIA), a 27-amino acid toxin from Conus purpurascens venom that inhibits the Shaker potassium channel, was chemically synthesized in a biologically active form. The disulfide connectivity of the peptide was determined. ĸ-Conotoxin PVIIA has the following structure. | Conotoxins; k-Conotoxin PVIIA; Conus purpurascens | 1998 |
12 |
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Olivera, Baldomero M.; Bulaj, Grzegorz | Structure of a novel P-superfamily spasmodic conotoxin reveals an inhibitory cystine knot motif | Conotoxin gm9a, a putative 27-residue polypeptide encoded by Conus gloriamaris, was recently identified as a homologue of the "spasmodic peptide", tx9a, isolated from the venom of the mollusk-hunting cone shell Conus textile (Lirazan, M. B., Hooper, D., Corpuz, G. P., Ramilo, C. A., Bandyopadhyay... | Conotoxins; P-superfamily spasmodic conotoxin; Cystine knot motif | 2002 |
13 |
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Olivera, Baldomero M.; Zhang, MinMin; Azam, Layla; Yoshikami, Doju; Bulaj, Grzegorz | Structure/function characterization of μ-Conotoxin KIIIA, an analgesic, nearly irreversible blocker of mammalian neuronal sodium channels | Peptide neurotoxins from cone snails continue to supply compounds with therapeutic potential. Although several analgesic conotoxins have already reached human clinical trials, a continuing need exists for the discovery and development of novel nonopioid analgesics, such as subtype-selective sodium c... | Conotoxins; 956;-Conotoxin KIIIA; Neuronal blocker; Neurotoxins; Sodium channel blockers | 2007 |
14 |
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Olivera, Baldomero M. | Uniquely selective inhibitor of the mammalian fetal neuromuscular nicotinic acetylcholine receptor | We have purified and characterized a novel conotoxin from the venom of Conus obscurus, which has the unique property of selectively and potently inhibiting the fetal form of the mammalian neuromuscular nicotinic acetylcholine receptor (nAChR) (α1β1γδ-subunits). Although this conotoxin, αA-cono... | Conotoxins; Conus obscurus; Fetal; Muscle; nAChR; Inhibitor; Receptor | 2005-01-19 |
15 |
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Olivera, Baldomero M.; Gray, William Robert | New family of Conus peptides targeted to the nicotinic acetylcholine receptor | In this work, a new family of Conus peptides, the αA-conotoxins, which target the nicotinic acetylcholine receptor, is defined. The first members of this family have been characterized from the eastern Pacific species, Conus purpurascens (the purple cone); three peptides that cause paralysis in fis... | Conotoxins; Conus peptides; Conus purpurascens; Purple cone snail | 1995 |
16 |
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Olivera, Baldomero M.; Gray, William Robert; Yoshikami, Doju | Conus geographus toxins that discriminate between neuronal and muscle sodium channels | We describe the properties of a family of 22-amino acid peptides, the μ-conotoxins, which are useful probes for investigating voltage-dependent sodium channels of excitable tissues. The μ-conotoxins are present in the venom of the piscivorous marine snail, Conus geographus L. We have purified even... | Conus geographus; Venom; Conotoxins; Sodium channels; Neurotoxins | 1985 |