pubmed-article:11522785 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11522785 | lifeskim:mentions | umls-concept:C0021585 | lld:lifeskim |
pubmed-article:11522785 | lifeskim:mentions | umls-concept:C0006685 | lld:lifeskim |
pubmed-article:11522785 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:11522785 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:11522785 | lifeskim:mentions | umls-concept:C0205250 | lld:lifeskim |
pubmed-article:11522785 | lifeskim:mentions | umls-concept:C1880355 | lld:lifeskim |
pubmed-article:11522785 | pubmed:issue | 43 | lld:pubmed |
pubmed-article:11522785 | pubmed:dateCreated | 2001-10-22 | lld:pubmed |
pubmed-article:11522785 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:abstractText | We have isolated a novel family of insect-selective neurotoxins that appear to be the most potent blockers of insect voltage-gated calcium channels reported to date. These toxins display exceptional phylogenetic specificity, with at least a 10,000-fold preference for insect versus vertebrate calcium channels. The structure of one of the toxins reveals a highly structured, disulfide-rich core and a structurally disordered C-terminal extension that is essential for channel blocking activity. Weak structural/functional homology with omega-agatoxin-IVA/B, the prototypic inhibitor of vertebrate P-type calcium channels, suggests that these two toxin families might share a similar mechanism of action despite their vastly different phylogenetic specificities. | lld:pubmed |
pubmed-article:11522785 | pubmed:language | eng | lld:pubmed |
pubmed-article:11522785 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11522785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11522785 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11522785 | pubmed:month | Oct | lld:pubmed |
pubmed-article:11522785 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:SmithRR | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:WilsonDD | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:ShawDD | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:ChristieM JMJ | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:ConnorMM | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:WangX HXH | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:KingG FGF | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:AlewoodP FPF | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:NicholsonG... | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:WilsonH IHI | lld:pubmed |
pubmed-article:11522785 | pubmed:author | pubmed-author:MackayJ PJP | lld:pubmed |
pubmed-article:11522785 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11522785 | pubmed:day | 26 | lld:pubmed |
pubmed-article:11522785 | pubmed:volume | 276 | lld:pubmed |
pubmed-article:11522785 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11522785 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11522785 | pubmed:pagination | 40306-12 | lld:pubmed |
pubmed-article:11522785 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:11522785 | pubmed:meshHeading | pubmed-meshheading:11522785... | lld:pubmed |
pubmed-article:11522785 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11522785 | pubmed:articleTitle | Discovery and structure of a potent and highly specific blocker of insect calcium channels. | lld:pubmed |
pubmed-article:11522785 | pubmed:affiliation | Department of Biochemistry, University of Connecticut Health Center, Farmington, CT 06032, USA. | lld:pubmed |
pubmed-article:11522785 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11522785 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:11522785 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |