pubmed-article:20454456 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20454456 | lifeskim:mentions | umls-concept:C0242738 | lld:lifeskim |
pubmed-article:20454456 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:20454456 | lifeskim:mentions | umls-concept:C1517880 | lld:lifeskim |
pubmed-article:20454456 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:20454456 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:20454456 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:20454456 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:20454456 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:20454456 | pubmed:dateCreated | 2010-5-10 | lld:pubmed |
pubmed-article:20454456 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20454456 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20454456 | pubmed:abstractText | The ABC transporter OpuA from Lactococcus lactis transports glycine betaine upon activation by threshold values of ionic strength. In this study, the ligand binding characteristics of purified OpuA in a detergent-solubilized state and of its substrate-binding domain produced as soluble protein (OpuAC) was characterized. | lld:pubmed |
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pubmed-article:20454456 | pubmed:language | eng | lld:pubmed |
pubmed-article:20454456 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20454456 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20454456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20454456 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20454456 | pubmed:issn | 1932-6203 | lld:pubmed |
pubmed-article:20454456 | pubmed:author | pubmed-author:KarasawaAkira... | lld:pubmed |
pubmed-article:20454456 | pubmed:author | pubmed-author:ThunnissenAnd... | lld:pubmed |
pubmed-article:20454456 | pubmed:author | pubmed-author:PoolmanBertB | lld:pubmed |
pubmed-article:20454456 | pubmed:author | pubmed-author:SlotboomDirk-... | lld:pubmed |
pubmed-article:20454456 | pubmed:author | pubmed-author:WoltersJustin... | lld:pubmed |
pubmed-article:20454456 | pubmed:author | pubmed-author:BerntssonRonn... | lld:pubmed |
pubmed-article:20454456 | pubmed:author | pubmed-author:GulNadiaN | lld:pubmed |
pubmed-article:20454456 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20454456 | pubmed:volume | 5 | lld:pubmed |
pubmed-article:20454456 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20454456 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20454456 | pubmed:pagination | e10361 | lld:pubmed |
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pubmed-article:20454456 | pubmed:meshHeading | pubmed-meshheading:20454456... | lld:pubmed |
pubmed-article:20454456 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20454456 | pubmed:articleTitle | Ligand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA. | lld:pubmed |
pubmed-article:20454456 | pubmed:affiliation | Biochemistry Department, Groningen Biomolecular Sciences and Biotechnology Institute, Netherlands Proteomics Centre, University of Groningen, Groningen, The Netherlands. | lld:pubmed |
pubmed-article:20454456 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20454456 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20454456 | lld:entrezgene |