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dc.contributor.authorZloh, Mire
dc.contributor.authorKaatz, G.W.
dc.contributor.authorGibbons, S.
dc.date.accessioned2013-06-24T15:10:51Z
dc.date.available2013-06-24T15:10:51Z
dc.date.issued2004-02-23
dc.identifier.citationZloh , M , Kaatz , G W & Gibbons , S 2004 , ' Inhibitors of multidrug resistance (MDR) have affinity for MDR substrates ' , Bioorganic and Medicinal Chemistry Letters , vol. 14 , no. 4 , pp. 881-885 . https://doi.org/10.1016/j.bmcl.2003.12.015
dc.identifier.issn0960-894X
dc.identifier.otherPURE: 1448072
dc.identifier.otherPURE UUID: 755460d1-5956-412e-997f-f61f150d357e
dc.identifier.otherScopus: 0842302984
dc.identifier.urihttp://hdl.handle.net/2299/10924
dc.descriptionMEDLINE® is the source for the MeSH terms of this document.
dc.description.abstractMultidrug-resistance (MDR) occurs in many bacterial species and tumour cells. MDR functions by membrane proteins which export drugs from cells, resulting in a low ineffective concentration of the drug. We have shown by molecular modelling that inhibitors of MDR have affinity for substrates of MDR transporters. This affinity may facilitate drug entry into cells and a large inhibitor-drug complex may be a poorer substrate for the MDR mechanism. This complex would effectively 'cloak' the drug rendering it unavailable for efflux.en
dc.format.extent5
dc.language.isoeng
dc.relation.ispartofBioorganic and Medicinal Chemistry Letters
dc.titleInhibitors of multidrug resistance (MDR) have affinity for MDR substratesen
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.description.statusPeer reviewed
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=0842302984&partnerID=8YFLogxK
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted2004-02-23
rioxxterms.versionofrecordhttps://doi.org/10.1016/j.bmcl.2003.12.015
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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