pubmed-article:10417345 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10417345 | lifeskim:mentions | umls-concept:C0032212 | lld:lifeskim |
pubmed-article:10417345 | lifeskim:mentions | umls-concept:C0042479 | lld:lifeskim |
pubmed-article:10417345 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:10417345 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
pubmed-article:10417345 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:10417345 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
pubmed-article:10417345 | pubmed:dateCreated | 1999-9-16 | lld:pubmed |
pubmed-article:10417345 | pubmed:abstractText | Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel beta-sheet comprising residues 15-18 and 37-40 and a small 3(10) helix spanning residues 10-12. The overall three-dimensional fold is similar to that of beta-defensin-12, and similar to the sodium-channel neurotoxin ShI (Stichodactyla helianthus neurotoxin I). However, the side chains known to be functionally important in beta-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function. Consistent with this contention, we showed that DLP-1 possesses no anti-microbial properties and has no observable activity on rat dorsal-root-ganglion sodium-channel currents. | lld:pubmed |
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pubmed-article:10417345 | pubmed:language | eng | lld:pubmed |
pubmed-article:10417345 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10417345 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10417345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10417345 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10417345 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10417345 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:SmithRR | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:SutherlandS... | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:SimpsonR JRJ | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:KuchelP WPW | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:GallagherC... | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:TorresA MAM | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:KingG FGF | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:AlewoodP FPF | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:AlewoodDD | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:NicholsonG... | lld:pubmed |
pubmed-article:10417345 | pubmed:author | pubmed-author:FletcherJ IJI | lld:pubmed |
pubmed-article:10417345 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10417345 | pubmed:day | 1 | lld:pubmed |
pubmed-article:10417345 | pubmed:volume | 341 ( Pt 3) | lld:pubmed |
pubmed-article:10417345 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10417345 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10417345 | pubmed:pagination | 785-94 | lld:pubmed |
pubmed-article:10417345 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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pubmed-article:10417345 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10417345 | pubmed:articleTitle | Solution structure of a defensin-like peptide from platypus venom. | lld:pubmed |
pubmed-article:10417345 | pubmed:affiliation | Department of Biochemistry, University of Sydney, NSW 2006, Australia. | lld:pubmed |
pubmed-article:10417345 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10417345 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:10417345 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
family:PF08131.6 | family:pubmed | pubmed-article:10417345 | lld:pfam |
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