| pubmed-article:20189991 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20189991 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
| pubmed-article:20189991 | lifeskim:mentions | umls-concept:C0042479 | lld:lifeskim |
| pubmed-article:20189991 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:20189991 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:20189991 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20189991 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
| pubmed-article:20189991 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:20189991 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:20189991 | pubmed:dateCreated | 2010-4-26 | lld:pubmed |
| pubmed-article:20189991 | pubmed:abstractText | Venoms of snakes, scorpions, spiders, insects, sea anemones, and cone snails are complex mixtures of mostly peptides and small proteins that have evolved for prey capture and/or defense. These deadly animals have long fascinated scientists and the public. Early studies isolated lethal components in the search for cures and understanding of their mechanisms of action. Ion channels have emerged as targets for many venom peptides, providing researchers highly selective and potent molecular probes that have proved invaluable in unraveling ion channel structure and function. This minireview highlights molecular details of their toxin-receptor interactions and opportunities for development of peptide therapeutics. | lld:pubmed |
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| pubmed-article:20189991 | pubmed:language | eng | lld:pubmed |
