pubmed-article:17150588 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17150588 | lifeskim:mentions | umls-concept:C0020289 | lld:lifeskim |
pubmed-article:17150588 | lifeskim:mentions | umls-concept:C0032150 | lld:lifeskim |
pubmed-article:17150588 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17150588 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
pubmed-article:17150588 | pubmed:issue | 48 | lld:pubmed |
pubmed-article:17150588 | pubmed:dateCreated | 2006-12-7 | lld:pubmed |
pubmed-article:17150588 | pubmed:abstractText | Structural information of Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase (PfSAHH) has been expected to provide new-type chemotherapeutic agents against malaria. Here we report the crystal structure of PfSAHH. The present structure should provide opportunities to design potent and selective PfSAHH inhibitors. | lld:pubmed |
pubmed-article:17150588 | pubmed:language | eng | lld:pubmed |
pubmed-article:17150588 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17150588 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17150588 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17150588 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17150588 | pubmed:issn | 1746-8272 | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:KitadeYukioY | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:NakanishiMasa... | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:TanakaNobutad... | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:NakamuraKazuo... | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:ItoYasutomoY | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:KusakabeYoshi... | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:YabeSaoriS | lld:pubmed |
pubmed-article:17150588 | pubmed:author | pubmed-author:ShiraiwaKatsu... | lld:pubmed |
pubmed-article:17150588 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17150588 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17150588 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17150588 | pubmed:pagination | 281-2 | lld:pubmed |
pubmed-article:17150588 | pubmed:dateRevised | 2007-9-19 | lld:pubmed |
pubmed-article:17150588 | pubmed:meshHeading | pubmed-meshheading:17150588... | lld:pubmed |
pubmed-article:17150588 | pubmed:meshHeading | pubmed-meshheading:17150588... | lld:pubmed |
pubmed-article:17150588 | pubmed:meshHeading | pubmed-meshheading:17150588... | lld:pubmed |
pubmed-article:17150588 | pubmed:meshHeading | pubmed-meshheading:17150588... | lld:pubmed |
pubmed-article:17150588 | pubmed:meshHeading | pubmed-meshheading:17150588... | lld:pubmed |
pubmed-article:17150588 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:17150588 | pubmed:articleTitle | Three-dimensional structure of S-adenosyl-L-homocysteine hydrolase from Plasmodium falciparum. | lld:pubmed |
pubmed-article:17150588 | pubmed:affiliation | School of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, Japan. | lld:pubmed |
pubmed-article:17150588 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17150588 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:813025 | entrezgene:pubmed | pubmed-article:17150588 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17150588 | lld:entrezgene |