Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:19673097rdf:typepubmed:Citationlld:pubmed
pubmed-article:19673097lifeskim:mentionsumls-concept:C0327441lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C0031676lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C1179435lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C0012590lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C0441655lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C0026377lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C1705248lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C1548799lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C1524073lld:lifeskim
pubmed-article:19673097lifeskim:mentionsumls-concept:C0449432lld:lifeskim
pubmed-article:19673097pubmed:issue5lld:pubmed
pubmed-article:19673097pubmed:dateCreated2009-8-12lld:pubmed
pubmed-article:19673097pubmed:abstractTextMembrane-damaging activity of Naja naja atra cardiotoxin 3 (CTX3) on 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC)/1,2-dimyristoyl-phosphatidic acid (DMPA) vesicles was approximately 3-fold that of N. naja atra cardiotoxin 4 (CTX4), while CTX3 and CTX4 displayed insignificantly permeabilizing activity in 1,2-dipalmitoyl-phosphatidylcholine (DPPC)/DMPA vesicles. Phospholipid-binding capability and oligomeric assembly upon binding with lipid vesicles did not closely correlate with membrane-damaging potency of CTX3 and CTX4. Geometrical arrangement of CTX3 in contact with POPC/DMPA vesicles was different from that noted with CTX4, and binding forces between CTX3 and POPC/DMPA were stronger than those between CTX4 and POPC/DMPA. Unlike POPC/DMPA, the interaction between CTXs and DPPC/DMPA was drastically reduced by increasing salt concentration. Color transformation of phospholipid/polydiacetylene membrane assay and FTIR spectra analyses revealed that CTX3 and CTX4 adopted different conformationsand modes upon absorption on POPC/DMPA and DPPC/DMPA vesicles. Taken together, our data show that, in addition to membrane packing density and phospholipid-binding capability, membrane-bound conformation of CTXs plays a vital role in displaying membrane-damaging activity.lld:pubmed
pubmed-article:19673097pubmed:languageenglld:pubmed
pubmed-article:19673097pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:citationSubsetIMlld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19673097pubmed:statusMEDLINElld:pubmed
pubmed-article:19673097pubmed:monthAprlld:pubmed
pubmed-article:19673097pubmed:issn0041-0101lld:pubmed
pubmed-article:19673097pubmed:authorpubmed-author:LinShinne-Ren...lld:pubmed
pubmed-article:19673097pubmed:authorpubmed-author:ChangLong-Sen...lld:pubmed
pubmed-article:19673097pubmed:authorpubmed-author:WuMing-JungMJlld:pubmed
pubmed-article:19673097pubmed:authorpubmed-author:KaoPei-HsiuPHlld:pubmed
pubmed-article:19673097pubmed:issnTypePrintlld:pubmed
pubmed-article:19673097pubmed:volume53lld:pubmed
pubmed-article:19673097pubmed:ownerNLMlld:pubmed
pubmed-article:19673097pubmed:authorsCompleteYlld:pubmed
pubmed-article:19673097pubmed:pagination512-8lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:meshHeadingpubmed-meshheading:19673097...lld:pubmed
pubmed-article:19673097pubmed:year2009lld:pubmed
pubmed-article:19673097pubmed:articleTitleMembrane-bound conformation and phospholipid components modulate membrane-damaging activity of Taiwan cobra cardiotoxins.lld:pubmed
pubmed-article:19673097pubmed:affiliationInstitute of Biomedical Sciences, National Sun Yat-Sen University-Kaohsiung Medical University Joint Research Center, National Sun Yat-Sen University, No. 70, Lien-Hai Road, Kaohsiung 804, Taiwan.lld:pubmed
pubmed-article:19673097pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19673097pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed