pubmed-article:19673097 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C0327441 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C0012590 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
pubmed-article:19673097 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:19673097 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:19673097 | pubmed:dateCreated | 2009-8-12 | lld:pubmed |
pubmed-article:19673097 | pubmed:abstractText | Membrane-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:19673097 | pubmed:language | eng | lld:pubmed |
pubmed-article:19673097 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19673097 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19673097 | pubmed:month | Apr | lld:pubmed |
pubmed-article:19673097 | pubmed:issn | 0041-0101 | lld:pubmed |
pubmed-article:19673097 | pubmed:author | pubmed-author:LinShinne-Ren... | lld:pubmed |
pubmed-article:19673097 | pubmed:author | pubmed-author:ChangLong-Sen... | lld:pubmed |
pubmed-article:19673097 | pubmed:author | pubmed-author:WuMing-JungMJ | lld:pubmed |
pubmed-article:19673097 | pubmed:author | pubmed-author:KaoPei-HsiuPH | lld:pubmed |
pubmed-article:19673097 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:19673097 | pubmed:volume | 53 | lld:pubmed |
pubmed-article:19673097 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19673097 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19673097 | pubmed:pagination | 512-8 | lld:pubmed |
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pubmed-article:19673097 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19673097 | pubmed:articleTitle | Membrane-bound conformation and phospholipid components modulate membrane-damaging activity of Taiwan cobra cardiotoxins. | lld:pubmed |
pubmed-article:19673097 | pubmed:affiliation | Institute 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:19673097 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19673097 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |