| pubmed-article:19015045 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19015045 | lifeskim:mentions | umls-concept:C1166950 | lld:lifeskim |
| pubmed-article:19015045 | lifeskim:mentions | umls-concept:C0022173 | lld:lifeskim |
| pubmed-article:19015045 | lifeskim:mentions | umls-concept:C0034348 | lld:lifeskim |
| pubmed-article:19015045 | lifeskim:mentions | umls-concept:C0032150 | lld:lifeskim |
| pubmed-article:19015045 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19015045 | pubmed:dateCreated | 2009-2-9 | lld:pubmed |
| pubmed-article:19015045 | pubmed:abstractText | Bioinformatics research on Plasmodium falciparum revealed two isoforms of pyruvate kinase: type-I and type-II enzymes. The type-I enzyme shows typical glycolytic properties, while type-II enzyme is involved in fatty acid type-II biosynthesis and has been predicted to localize to the apicoplast with the targeting signal in its N-terminus. The type-I and type-II isoforms have the same evolutionary origin as Toxoplasma gondii isozymes, TgPyKI and TgPyKII, respectively; however, TgPyKII localizes to both the mitochondrion and the apicoplast. Accordingly, we made a recombinant full length of P. falciparum pyruvate kinase type-II protein using a wheat germ cell-free expression system and obtained a specific antibody against the type-II protein. Fluorescent microscopic analysis revealed that P. falciparum type-II enzyme was localized only to the apicoplast, not to the mitochondrion. The data suggest differences in localization and metabolic pathways between P. falciparum and T. gondii pyruvate kinase isoforms. | lld:pubmed |
| pubmed-article:19015045 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19015045 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19015045 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19015045 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19015045 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19015045 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19015045 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19015045 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19015045 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19015045 | pubmed:issn | 1383-5769 | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:RoosDavid SDS | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:TakeoSatoruS | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:TakeuchiTsuto... | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:HarbOmar SOS | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:AsaiTakashiT | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:MaedaTakuyaT | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:SuzukiHirokoH | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:TsuboiTakafum... | lld:pubmed |
| pubmed-article:19015045 | pubmed:author | pubmed-author:SaitoTomoyaT | lld:pubmed |
| pubmed-article:19015045 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19015045 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:19015045 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19015045 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19015045 | pubmed:pagination | 101-5 | lld:pubmed |
| pubmed-article:19015045 | pubmed:meshHeading | pubmed-meshheading:19015045... | lld:pubmed |
| pubmed-article:19015045 | pubmed:meshHeading | pubmed-meshheading:19015045... | lld:pubmed |
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| pubmed-article:19015045 | pubmed:meshHeading | pubmed-meshheading:19015045... | lld:pubmed |
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| pubmed-article:19015045 | pubmed:meshHeading | pubmed-meshheading:19015045... | lld:pubmed |
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| pubmed-article:19015045 | pubmed:meshHeading | pubmed-meshheading:19015045... | lld:pubmed |
| pubmed-article:19015045 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19015045 | pubmed:articleTitle | Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast. | lld:pubmed |
| pubmed-article:19015045 | pubmed:affiliation | Department of Tropical Medicine and Parasitology, Keio University, Shinjuku-ku, Tokyo 160-8582, Japan. | lld:pubmed |
| pubmed-article:19015045 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19015045 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:810520 | entrezgene:pubmed | pubmed-article:19015045 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19015045 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19015045 | lld:pubmed |
