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Creator | Title | Description | Subject | Date |
1 |
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Olivera, Baldomero M.; McIntosh, J. Michael; Hillyard, David R. | A-superfamily of conotoxins: structural and functional divergence | The generation of functional novelty in proteins encoded by a gene superfamily is seldom well documented. In this report, we define the A-conotoxin superfamily, which is widely expressed in venoms of the predatory cone snails (Conus), and show how gene products that diverge considerably in stru... | Conotoxins; A-superfamily conotoxin | 2004-02-03 |
2 |
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Olivera, Baldomero M. | Alternative splicing in the pore-forming region of shaker potassium channels | We have cloned cDNAs for the shaker potassium channel gene from the spiny lobster Panulirus interruptus. As previously found in Drosophila, there is alternative splicing at the 59 and 39 ends of the coding region. However, in Panulirus shaker, alternative splicing also occurs within the pore-forming... | Panulirus interruptus; Conotoxins; Shaker; Stomatogastric ganglion; Pore-forming region; Alternative splicing | 1997 |
3 |
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Olivera, Baldomero M. | Aminoglycoside effects on voltage-sensitive calcium channels and neurotoxicity | To the Editor: Since ototoxicity and neuromuscular toxicity of aminoglycoside antibiotics are reversed by calcium, 1,2 and presynaptic events appear to be involved in aminoglycoside-induced neuromuscular blockade, 3,4 we suspected a role for voltage-sensitive calcium channels in aminoglycoside neuro... | Conotoxins | 1987 |
4 |
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Olivera, Baldomero M. | Biochemical studies of ω-conotoxin GVIA; a peptide toxin inhibiting voltage-sensitive Ca++ channels | The fish-hunting cone snails use their venom to quickly paralyze their more agile prey. In the last few years, our laboratories have carried out a program of analyzing biologically active components present in the fish-hunting cone snail venoms (Cruz et al. 1985; Olivera et al. 1985). We have concen... | Conotoxins; Calcium channels; Conus geographus; Venom | 1987 |
5 |
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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 |
6 |
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Olivera, Baldomero M. | Calcium channel antagonists: ω-conotoxin defines a new high affinity site | The ω-conotoxins, a class of Ca2+ channel antagonists from fish-hunting marine snails, have recently been described (Olivera, B. M., McIntosh, J. M., Zeikus, R., Gray, W. R., Varga, J., Rivier, J., de Santos, V., and Cruz, L. J. (1985) Science, 230, 1338-1343). One of these peptide neurotoxins... | Conotoxins; Calcium channels; Synaptosomes; Neurotoxins | 1986 |
7 |
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Olivera, Baldomero M.; Parks, Thomas N. | Conantokin-T: a γ-carboxyglutamate containing peptide with N-methyl-D-aspartate antagonist activity | Conantokin-T, a 21-amino acid peptide which induces sleep-like symptoms in young mice was purified from the venom of the fish-hunting cone snail, Conus tulipa. The amino acid sequence of the peptide was determined and verified by chemical synthesis. The peptide has 4 residues of the modified amino ... | Conotoxins; Conantokin-T; N-methyl-D-aspartate antagonist; Conus tulipa | 1990 |
8 |
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Olivera, Baldomero M. | Conodipine-M, a novel phospholipase A2 isolated from the venom of the marine snail Conus magus | We describe the purification and first biochemical characterization of an enzymatic activity in venom from the marine snail Conus magus. This enzyme, named conodipine-M, is a novel phospholipase A2 with a molecular mass of 13.6 ĸDa and is comprised of two polypeptide chains linked by one or more di... | Conotoxins; Conodipine-M; Conus magus | 1994 |
9 |
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Olivera, Baldomero M.; Gray, William Robert | Conotoxin MI: disulfide bonding and conformational states | The toxic peptide from Conus magus venom (conotoxin MI) is a 14-amino acid peptide (McIntosh, M., Cruz, L. J., Hunkapiller, M. W., Gray, W. R., and Olivera, B. M. (1982) Arch. Biochem. Biophys. 218, 329-334) which inhibits the acetylcholine ceptor. In this work we have confirmed the primary structu... | Conotoxins; Disulfide bonding; Venom; Conus magus | 1983 |
10 |
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Olivera, Baldomero M.; Hillyard, David R. | Conotoxins | Many successful animal and plant families have developed distinctive biochemical strategies; one of the more unusual examples is found in a group of marine gastropods, the cone snails (Conus) (1). These animals have evolved a specialized biochemistry of small constrained peptides, the conotoxins. Th... | Conotoxins | 1991 |
11 |
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Olivera, Baldomero M.; Gray, William Robert | Contryphan is a D-tryptophan-containing Conus peptide | In this report, we document for the first time the occurrence of D-tryptophan in a normally translated polypeptide, contryphan. The peptide, isolated from the venom of the fish-hunting marine snail Conus radiatus, produces the "stiff-tail" syndrome in mice. | Conotoxins; Contryphan; D-tryptophan; Conus peptides; Conus radiatus; Stiff-tail syndrome | 1996 |
12 |
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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 |
13 |
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Olivera, Baldomero M.; McIntosh, J. Michael | Conus peptides as tools for the neuroscientist | Recombinant DNA technology has had a powerful impact on understanding receptors and ion channels, the key components in the nervous system that are involved in intercellular communication. Cloning genes encoding these proteins has revealed that for every receptor and ion channel type, multiple molec... | Conus peptides; Conotoxins | 1993 |
14 |
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Olivera, Baldomero M. | Conus peptides: biodiversity-based discovery and exogenomics | The venoms of the ~700 species of predatory cone snails (genus Conus) are being systematically characterized. Each Conus species contains 100-200 small, highly structured venom peptides (colloquially known as conotoxins), which are synthesized and secreted in a venom duct (for overviews, see Refs. ... | Conotoxins; Conus peptides; Exogenomics | 2006 |
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Olivera, Baldomero M. | Conus peptides: phylogenetic range of biological activity | The major function of the venoms of the predatory marine snails belonging to the genus Conus is to paralyze prey. Thus, the venom of each Conus species acts on receptors and ion channels of the prey; previous studies suggested much less activity on homologous receptor targets in more distant taxa.... | Conus peptides; Conopeptides; Conotoxins | 1992 |
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Olivera, Baldomero M. | Conus venom peptides, receptor and ion channel targets, and drug design: 50 million years of neuropharmacology | The predatory cone snails (Conus) are among the most successful living marine animals (~500 living species). Each Conus species is a specialist in neuropharmacology, and uses venom to capture prey, to escape from and defend against predators and possibly to deter competitors. An individual cone... | Conotoxins | 1997 |
17 |
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Olivera, Baldomero M.; Gray, William Robert; McIntosh, J. Michael | Differential targeting of nicotinic acetylcholine receptors by novel αA-conotoxins | We describe the isolation and characterization of two peptide toxins from Conus ermineus venom targeted to nicotinic acetylcholine receptors (nAChRs). The peptide structures have been confirmed by mass spectrometry and chemical synthesis. In contrast to the 12-18 residue, 4 Cys-containing α-co... | Conotoxins; aA-conotoxins; Conus ermineus; Peptide toxins | 1997 |
18 |
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Olivera, Baldomero M. | Distinction among neuronal subtypes of voltage-activated sodium channels by μ-conotoxin PIIIA | The functional properties of most sodium channels are too similar to permit identification of specific sodium channel types underlying macroscopic current. Such discrimination would be particularly advantageous in the nervous system in which different sodium channel family isoforms are coexpressed i... | Conotoxins; m-conotoxin | 2000 |
19 |
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Olivera, Baldomero M. | Identification of a novel pharmacophore for peptide toxins interacting with K+ channels | қM-conotoxin RIIIK blocks TSha1 K+ channels from trout with high affinity by interacting with the ion channel pore. As opposed to many other peptides targeting K+ channels, қM-RIIIK does not possess a functional dyad. In this study we combine thermodynamic mutant cycle analysis and docking calc... | Conotoxins; Peptide toxins; қM-conotoxin RIIIK; Pharmacophore | 2005 |
20 |
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Olivera, Baldomero M.; Gray, William Robert | Invertebrate vasopressin/oxytocin homologs: characterization of peptides from Conus geographus and Conus striatus venoms | The vasopressin-oxytocin family of peptides is of very ancient lineage, found in organisms as diverse as hydra and man. Although these peptides have been intensively studied in vertebrates, the presumably more extensive invertebrate series was defined primarily by immunological methods. In this repo... | Conus geographus; Conus striatus; Venom; Conotoxins; Neurotoxins; Postsynaptic inhibition; Vasopressin-oxytocin peptides; Conopressin | 1987 |
21 |
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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 |
22 |
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Olivera, Baldomero M.; ; McIntosh, J. Michael | Localization of [125I] ω-conotoxin GVIA binding in human hippocampus and cerebellum | THE peptide toxin ω-conotoxin GVIA (ω-CgTx) has been shown to be a high affinity ligand for N-type calcium channels in the brain. We have employed [125I]ω-CgTx to localize N-type channels in human hippocampus and cerebellum using autoradiography. Ten micron thick slidemounted tissue sections of... | Conotoxins; Peptide toxins | 1993 |
23 |
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Olivera, Baldomero M.; McIntosh, J. Michael; Gray, William Robert; Hillyard, David R. | New family of conotoxins that block voltage-gated sodium channels | Conus peptides, including ω-conotoxins and α-conotoxins (targeting calcium channels and nicotinic acetylcholine receptors, respectively) have been useful ligands in neuroscience. In this report, we describe a new family of sodium channel ligands, the μO-conotoxins. | Conotoxins; Sodium channel blockers | 1995 |
24 |
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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 |
25 |
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Olivera, Baldomero M.; Gray, William Robert; McIntosh, J. Michael | New α-conotoxin which targets α3ß2 nicotinic acetylcholine receptors | We have isolated a 16-amino acid peptide from the venom of the marine snail Conus magus which potently blocks nicotinic acetylcholine receptors (nAChRs) composed of α3ß2 subunits. This peptide, named a-conotoxin MII, was identified by electrophysiologically screening venom fractions against cl... | Conotoxins; a-conotoxin MII; Conus magus | 1996 |