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| pubmed-article:16020735 | lifeskim:mentions | umls-concept:C0230812 | lld:lifeskim |
| pubmed-article:16020735 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:16020735 | lifeskim:mentions | umls-concept:C0024348 | lld:lifeskim |
| pubmed-article:16020735 | lifeskim:mentions | umls-concept:C1412485 | lld:lifeskim |
| pubmed-article:16020735 | lifeskim:mentions | umls-concept:C0205431 | lld:lifeskim |
| pubmed-article:16020735 | pubmed:issue | 5733 | lld:pubmed |
| pubmed-article:16020735 | pubmed:dateCreated | 2005-7-15 | lld:pubmed |
| pubmed-article:16020735 | pubmed:abstractText | Apolipoprotein L-I is the trypanolytic factor of human serum. Here we show that this protein contains a membrane pore-forming domain functionally similar to that of bacterial colicins, flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein L-I formed anion channels. In Trypanosoma brucei, apolipoprotein L-I was targeted to the lysosomal membrane and triggered depolarization of this membrane, continuous influx of chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed. | lld:pubmed |
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| pubmed-article:16020735 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16020735 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16020735 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16020735 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16020735 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:16020735 | pubmed:author | pubmed-author:LinsLaurenceL | lld:pubmed |
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| pubmed-article:16020735 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16020735 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16020735 | pubmed:volume | 309 | lld:pubmed |
| pubmed-article:16020735 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16020735 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16020735 | pubmed:pagination | 469-72 | lld:pubmed |
| pubmed-article:16020735 | pubmed:dateRevised | 2007-8-13 | lld:pubmed |
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| pubmed-article:16020735 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16020735 | pubmed:articleTitle | Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes. | lld:pubmed |
| pubmed-article:16020735 | pubmed:affiliation | Laboratory of Molecular Parasitology, IBMM, Université Libre de Bruxelles, 12, rue des Profs Jeener et Brachet, B6041 Gosselies, Belgium. | lld:pubmed |
| pubmed-article:16020735 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16020735 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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