dc.contributor.author | NOLAN, DEREK | |
dc.date.accessioned | 2010-01-28T17:32:41Z | |
dc.date.available | 2010-01-28T17:32:41Z | |
dc.date.issued | 2005 | |
dc.date.submitted | 2005 | en |
dc.identifier.citation | Perez-Morga D., Vanhollebeke B., Paturiaux-Hanocq F., Nolan D.P., Lins L., Homble F., Vanhamme L., Tebabi P., Pays A., Poelvoorde P., Jacquet A., Brasseur R., Pays E., Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes, Science, 309, 2005, 469, 472 | en |
dc.identifier.other | Y | |
dc.identifier.uri | http://hdl.handle.net/2262/36528 | |
dc.description | PUBLISHED | en |
dc.description.abstract | 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. | en |
dc.format.extent | 469 | en |
dc.format.extent | 472 | en |
dc.format.extent | 387355 bytes | |
dc.format.mimetype | application/pdf | |
dc.language.iso | en | en |
dc.publisher | American Association for the Advancement of Science | en |
dc.relation.ispartofseries | Science | en |
dc.relation.ispartofseries | 309 | en |
dc.rights | Y | en |
dc.subject | Biochemistry | |
dc.title | Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes | en |
dc.type | Journal Article | en |
dc.type.supercollection | scholarly_publications | en |
dc.type.supercollection | refereed_publications | en |
dc.identifier.peoplefinderurl | http://people.tcd.ie/denolan | |
dc.identifier.rssinternalid | 30141 | |
dc.identifier.rssuri | http://dx.doi.org/10.1126/science.1114566 | |