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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/21552
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dc.contributor.authorDaines, R. A.en
dc.contributor.authorPendrak, I.en
dc.contributor.authorSham, K.en
dc.contributor.authorVan Aller, G. S.en
dc.contributor.authorKonstantinidis, A. K.en
dc.contributor.authorLonsdale, J. T.en
dc.contributor.authorJanson, C. A.en
dc.contributor.authorQiu, X.en
dc.contributor.authorBrandt, M.en
dc.contributor.authorKhandekar, S. S.en
dc.contributor.authorSilverman, C.en
dc.contributor.authorHead, M. S.en
dc.date.accessioned2015-11-24T19:15:44Z-
dc.date.available2015-11-24T19:15:44Z-
dc.identifier.issn0022-2623-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21552-
dc.rightsDefault Licence-
dc.subject3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/antagonists & inhibitors/*chemistryen
dc.subjectCrystallography, X-Rayen
dc.subjectDrug Designen
dc.subjectEnzyme Inhibitors/*chemical synthesis/chemistryen
dc.subjectIndoles/*chemical synthesis/chemistryen
dc.subjectModels, Molecularen
dc.subjectMolecular Structureen
dc.subjectStreptococcus pneumoniae/chemistryen
dc.titleFirst X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modelingen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1021/jm025571b-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/12502353-
heal.identifier.secondaryhttp://pubs.acs.org/doi/pdfplus/10.1021/jm025571b-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2003-
heal.abstractThe first cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor is reported. The inhibitor was obtained by rational modification of a high throughput screening lead with the aid of a S. pneumoniae FabH homology model. This homology model was used to design analogues that would have both high affinity for the enzyme and appropriate aqueous solubility to facilitate cocrystallization studies.en
heal.journalNameJ Med Chemen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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