| pubmed-article:21246053 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21246053 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:21246053 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:21246053 | lifeskim:mentions | umls-concept:C1420193 | lld:lifeskim |
| pubmed-article:21246053 | lifeskim:mentions | umls-concept:C1333652 | lld:lifeskim |
| pubmed-article:21246053 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:21246053 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:21246053 | lifeskim:mentions | umls-concept:C0181586 | lld:lifeskim |
| pubmed-article:21246053 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:21246053 | pubmed:dateCreated | 2011-1-19 | lld:pubmed |
| pubmed-article:21246053 | pubmed:abstractText | While G6PD deficiency is one of the major causes of acute hemolytic anemia, the membrane changes leading to red cell lysis have not been extensively studied. New findings concerning the mechanisms of G6PD deficient red cell destruction may facilitate our understanding of the large individual variations in susceptibility to pro-oxidant compounds and aid the prediction of the hemolytic activity of new drugs. | lld:pubmed |
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| pubmed-article:21246053 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:21246053 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21246053 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21246053 | pubmed:issn | 1932-6203 | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:CartaFrancoF | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:PippiaProtoP | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:MannuFrancaF | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:TurriniFrance... | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:PantaleoAnton... | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:FerruEmanuela... | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:SimulaLuigi... | lld:pubmed |
| pubmed-article:21246053 | pubmed:author | pubmed-author:KhadjaviAmina... | lld:pubmed |
| pubmed-article:21246053 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21246053 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:21246053 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21246053 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21246053 | pubmed:pagination | e15847 | lld:pubmed |
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| pubmed-article:21246053 | pubmed:meshHeading | pubmed-meshheading:21246053... | lld:pubmed |
| pubmed-article:21246053 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21246053 | pubmed:articleTitle | Irreversible AE1 tyrosine phosphorylation leads to membrane vesiculation in G6PD deficient red cells. | lld:pubmed |
| pubmed-article:21246053 | pubmed:affiliation | Department of Genetics, Biology and Biochemistry, University of Turin, Turin, Italy. | lld:pubmed |
| pubmed-article:21246053 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21246053 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:6521 | entrezgene:pubmed | pubmed-article:21246053 | lld:entrezgene |
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