Source:http://linkedlifedata.com/resource/pubmed/id/21147978
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 1
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pubmed:dateCreated |
2010-12-14
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pubmed:abstractText |
Diversity among Conus toxins mirrors the high species diversity in the Indo-Pacific region, and evolution of both is thought to stem from feeding-niche specialization derived from intra-generic competition. This study focuses on Conus californicus, a phylogenetic outlier endemic to the temperate northeast Pacific. Essentially free of congeneric competitors, it preys on a wider variety of organisms than any other cone snail. Using molecular cloning of cDNAs and mass spectrometry, we examined peptides isolated from venom ducts to elucidate the sequences and post-translational modifications of two eight-cysteine toxins (cal12a and cal12b of type 12 framework) that block voltage-gated Na(+) channels. Based on homology of leader sequence and mode of action, these toxins are related to the O-superfamily, but differ significantly from other members of that group. Six of the eight cysteine residues constitute the canonical framework of O-members, but two additional cysteine residues in the N-terminal region define an O+2 classification within the O-superfamily. Fifteen putative variants of Cal12.1 toxins have been identified by mRNAs that differ primarily in two short hypervariable regions and have been grouped into three subtypes (Cal12.1.1-3). This unique modular variation has not been described for other Conus toxins and suggests recombination as a diversity-generating mechanism. We propose that these toxin isoforms show specificity for similar molecular targets (Na(+) channels) in the many species preyed on by C. californicus and that individualistic utilization of specific toxin isoforms may involve control of gene expression.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1477-9145
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
214
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
147-61
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pubmed:meshHeading |
pubmed-meshheading:21147978-Animals,
pubmed-meshheading:21147978-Base Sequence,
pubmed-meshheading:21147978-California,
pubmed-meshheading:21147978-Cloning, Molecular,
pubmed-meshheading:21147978-Conus Snail,
pubmed-meshheading:21147978-DNA Primers,
pubmed-meshheading:21147978-Electrophysiology,
pubmed-meshheading:21147978-Gene Library,
pubmed-meshheading:21147978-Mass Spectrometry,
pubmed-meshheading:21147978-Molecular Sequence Data,
pubmed-meshheading:21147978-Mollusk Venoms,
pubmed-meshheading:21147978-Pacific Ocean,
pubmed-meshheading:21147978-Peptides,
pubmed-meshheading:21147978-Sequence Analysis, DNA,
pubmed-meshheading:21147978-Sodium Channel Blockers
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pubmed:year |
2011
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pubmed:articleTitle |
A diverse family of novel peptide toxins from an unusual cone snail, Conus californicus.
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pubmed:affiliation |
Hopkins Marine Station, Stanford University, Pacific Grove, CA 93950, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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