| pubmed-article:12429019 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C0218111 | lld:lifeskim |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C0036451 | lld:lifeskim |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:12429019 | lifeskim:mentions | umls-concept:C1176299 | lld:lifeskim |
| pubmed-article:12429019 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:12429019 | pubmed:dateCreated | 2003-2-19 | lld:pubmed |
| pubmed-article:12429019 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12429019 | pubmed:abstractText | An alpha-helical II-III loop segment of the dihydropyridine receptor activates the ryanodine receptor calcium-release channel. We describe a novel manipulation in which this agonist's activity is increased by modifying its surface structure to resemble that of a toxin molecule. In a unique system, native beta-sheet scorpion toxins have been reported to activate skeletal muscle ryanodine receptor calcium channels with high affinity by binding to the same site as the lower-affinity alpha-helical dihydropyridine receptor segment. We increased the alignment of basic residues in the alpha-helical peptide to mimic the spatial orientation of active residues in the scorpion toxin, with a consequent 2-20-fold increase in the activity of the alpha-helical peptide. We hypothesized that, like the native peptide, the modified peptide and the scorpion toxin may bind to a common site. This was supported by (i) similar changes in ryanodine receptor channel gating induced by the native or modified alpha-helical peptide and the beta-sheet toxin, a 10-100-fold reduction in channel closed time, with a < or = 2-fold increase in open dwell time and (ii) a failure of the toxin to further activate channels activated by the peptides. These results suggest that diverse structural scaffolds can present similar conformational surface properties to target common receptor sites. | lld:pubmed |
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| pubmed-article:12429019 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12429019 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12429019 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12429019 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12429019 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12429019 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:12429019 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12429019 | pubmed:author | pubmed-author:DulhuntyAngel... | lld:pubmed |
| pubmed-article:12429019 | pubmed:author | pubmed-author:GreenDanielD | lld:pubmed |
| pubmed-article:12429019 | pubmed:author | pubmed-author:LambGraham... | lld:pubmed |
| pubmed-article:12429019 | pubmed:author | pubmed-author:PaceSuziS | lld:pubmed |
| pubmed-article:12429019 | pubmed:author | pubmed-author:CurtisSuzanne... | lld:pubmed |
| pubmed-article:12429019 | pubmed:author | pubmed-author:SakowskaMagda... | lld:pubmed |
| pubmed-article:12429019 | pubmed:author | pubmed-author:CasarottoMarc... | lld:pubmed |
| pubmed-article:12429019 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12429019 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12429019 | pubmed:volume | 370 | lld:pubmed |
| pubmed-article:12429019 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12429019 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12429019 | pubmed:pagination | 517-27 | lld:pubmed |
| pubmed-article:12429019 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:meshHeading | pubmed-meshheading:12429019... | lld:pubmed |
| pubmed-article:12429019 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12429019 | pubmed:articleTitle | The three-dimensional structural surface of two beta-sheet scorpion toxins mimics that of an alpha-helical dihydropyridine receptor segment. | lld:pubmed |
| pubmed-article:12429019 | pubmed:affiliation | Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, ACT, 2601, Australia. | lld:pubmed |
| pubmed-article:12429019 | pubmed:publicationType | Journal Article | lld:pubmed |
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