| pubmed-article:15937493 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15937493 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:15937493 | lifeskim:mentions | umls-concept:C1136174 | lld:lifeskim |
| pubmed-article:15937493 | lifeskim:mentions | umls-concept:C0312418 | lld:lifeskim |
| pubmed-article:15937493 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:15937493 | lifeskim:mentions | umls-concept:C0036667 | lld:lifeskim |
| pubmed-article:15937493 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:15937493 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:15937493 | pubmed:dateCreated | 2005-7-6 | lld:pubmed |
| pubmed-article:15937493 | pubmed:abstractText | Artemisinins are the most important class of antimalarial drugs. They specifically inhibit PfATP6, a SERCA-type ATPase of Plasmodium falciparum. Here we show that a single amino acid in transmembrane segment 3 of SERCAs can determine susceptibility to artemisinin. An L263E replacement of a malarial by a mammalian residue abolishes inhibition by artemisinins. Introducing residues found in other Plasmodium spp. also modulates artemisinin sensitivity, suggesting that artemisinins interact with the thapsigargin-binding cleft of susceptible SERCAs. | lld:pubmed |
| pubmed-article:15937493 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15937493 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15937493 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15937493 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15937493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15937493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15937493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15937493 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15937493 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15937493 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:UhlemannAnne-... | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:HaynesRichard... | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:BradyLeoL | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:FischbargJorg... | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:IserovichPave... | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:ZunigaFelipe... | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:KrishnaSanjee... | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:Eckstein-Ludw... | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:CameronAngusA | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:LeeAnthonyA | lld:pubmed |
| pubmed-article:15937493 | pubmed:author | pubmed-author:EastMalcolmM | lld:pubmed |
| pubmed-article:15937493 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15937493 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:15937493 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15937493 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15937493 | pubmed:pagination | 628-9 | lld:pubmed |
| pubmed-article:15937493 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:15937493 | pubmed:meshHeading | pubmed-meshheading:15937493... | lld:pubmed |
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| pubmed-article:15937493 | pubmed:meshHeading | pubmed-meshheading:15937493... | lld:pubmed |
| pubmed-article:15937493 | pubmed:meshHeading | pubmed-meshheading:15937493... | lld:pubmed |
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| pubmed-article:15937493 | pubmed:meshHeading | pubmed-meshheading:15937493... | lld:pubmed |
| pubmed-article:15937493 | pubmed:meshHeading | pubmed-meshheading:15937493... | lld:pubmed |
| pubmed-article:15937493 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15937493 | pubmed:articleTitle | A single amino acid residue can determine the sensitivity of SERCAs to artemisinins. | lld:pubmed |
| pubmed-article:15937493 | pubmed:affiliation | Department of Cellular and Molecular Medicine, Infectious Diseases, St. George's Hospital Medical School, London SW17 0RE, UK. | lld:pubmed |
| pubmed-article:15937493 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15937493 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15937493 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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