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| pubmed-article:19819701 | lifeskim:mentions | umls-concept:C0162340 | lld:lifeskim |
| pubmed-article:19819701 | lifeskim:mentions | umls-concept:C0242738 | lld:lifeskim |
| pubmed-article:19819701 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
| pubmed-article:19819701 | lifeskim:mentions | umls-concept:C0678679 | lld:lifeskim |
| pubmed-article:19819701 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19819701 | pubmed:dateCreated | 2010-2-3 | lld:pubmed |
| pubmed-article:19819701 | pubmed:abstractText | Multidrug ABC transporters can transport a wide range of drugs from the cell. Ongoing studies of the prototype mammalian multidrug resistance ATP-binding cassette transporter P-glycoprotein (ABCB1) have revealed many intriguing functional and biochemical features. However, a gap remains in our knowledge regarding the molecular basis of its broad specificity for structurally unrelated ligands. Recently, the first crystal structures of ligand-free and ligand-bound ABCB1 showed ligand binding in a cavity between its two membrane domains, and earlier observations on polyspecificity can now be interpreted in a structural context. Comparison of the new ABCB1 crystal structures with structures of bacterial homologs suggests a critical role for an axial rotation of transmembrane helices for high-affinity binding and low-affinity release of ligands during transmembrane transport. | lld:pubmed |
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| pubmed-article:19819701 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19819701 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19819701 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19819701 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19819701 | pubmed:issn | 0968-0004 | lld:pubmed |
| pubmed-article:19819701 | pubmed:author | pubmed-author:WardAndrewA | lld:pubmed |
| pubmed-article:19819701 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:19819701 | pubmed:author | pubmed-author:UrbatschIna... | lld:pubmed |
| pubmed-article:19819701 | pubmed:author | pubmed-author:ChangGeoffrey... | lld:pubmed |
| pubmed-article:19819701 | pubmed:author | pubmed-author:GutmannDaniel... | lld:pubmed |
| pubmed-article:19819701 | pubmed:copyrightInfo | Copyright 2009 Elsevier Ltd. All rights reserved. | lld:pubmed |
| pubmed-article:19819701 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19819701 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:19819701 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19819701 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19819701 | pubmed:pagination | 36-42 | lld:pubmed |
| pubmed-article:19819701 | pubmed:dateRevised | 2011-6-21 | lld:pubmed |
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| pubmed-article:19819701 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19819701 | pubmed:articleTitle | Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1. | lld:pubmed |
| pubmed-article:19819701 | pubmed:affiliation | Department of Pharmacology, University of Cambridge, Cambridge, UK. | lld:pubmed |
| pubmed-article:19819701 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19819701 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19819701 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:19819701 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19819701 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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