pubmed-article:14580560 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14580560 | lifeskim:mentions | umls-concept:C0013227 | lld:lifeskim |
pubmed-article:14580560 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
pubmed-article:14580560 | lifeskim:mentions | umls-concept:C1153198 | lld:lifeskim |
pubmed-article:14580560 | lifeskim:mentions | umls-concept:C0033629 | lld:lifeskim |
pubmed-article:14580560 | lifeskim:mentions | umls-concept:C0205197 | lld:lifeskim |
pubmed-article:14580560 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
pubmed-article:14580560 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:14580560 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:14580560 | pubmed:dateCreated | 2003-10-28 | lld:pubmed |
pubmed-article:14580560 | pubmed:abstractText | The notorious difficulty of elucidating structures of membrane transporters by crystallography has long prevented our understanding of active transport mechanism coupled with ion/proton transport. The determination of the first crystal structure of the drug/H+ antiporter AcrB was a breakthrough for structure-based understanding of drug/H+ antiport. However, although AcrB is a major multidrug exporter in Gram-negative organisms, the majority of bacterial drug exporters are major facilitator superfamily (MFS) drug transporters. As no crystal structures have been solved for MFS transporters, the alternative protein-engineering methods are still very useful for estimating structures and functions of drug/H+ antiporters. This review describes this alternative approach for investigating the structure and function of tetracycline/H+ antiporters. | lld:pubmed |
pubmed-article:14580560 | pubmed:language | eng | lld:pubmed |
pubmed-article:14580560 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14580560 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14580560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14580560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:14580560 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14580560 | pubmed:month | Oct | lld:pubmed |
pubmed-article:14580560 | pubmed:issn | 1367-5931 | lld:pubmed |
pubmed-article:14580560 | pubmed:author | pubmed-author:TamuraNorihis... | lld:pubmed |
pubmed-article:14580560 | pubmed:author | pubmed-author:YamaguchiAkih... | lld:pubmed |
pubmed-article:14580560 | pubmed:author | pubmed-author:KonishiSatoko... | lld:pubmed |
pubmed-article:14580560 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14580560 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:14580560 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14580560 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14580560 | pubmed:pagination | 570-9 | lld:pubmed |
pubmed-article:14580560 | pubmed:dateRevised | 2009-8-25 | lld:pubmed |
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pubmed-article:14580560 | pubmed:meshHeading | pubmed-meshheading:14580560... | lld:pubmed |
pubmed-article:14580560 | pubmed:meshHeading | pubmed-meshheading:14580560... | lld:pubmed |
pubmed-article:14580560 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14580560 | pubmed:articleTitle | Mechanisms of drug/H+ antiport: complete cysteine-scanning mutagenesis and the protein engineering approach. | lld:pubmed |
pubmed-article:14580560 | pubmed:affiliation | Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan. | lld:pubmed |
pubmed-article:14580560 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14580560 | pubmed:publicationType | Review | lld:pubmed |
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