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dc.contributor.authorBohm, Raphaelen_US
dc.contributor.authorFreiberger, Friedrichen_US
dc.contributor.authorStummeyer, Katharinaen_US
dc.contributor.authorGerardy-Schahn, Ritaen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.contributor.authorHaselhorst, Thomasen_US
dc.date.accessioned2017-05-03T11:47:35Z
dc.date.available2017-05-03T11:47:35Z
dc.date.issued2010en_US
dc.date.modified2011-03-07T08:54:03Z
dc.identifier.issn14394227en_US
dc.identifier.doi10.1002/cbic.200900659en_AU
dc.identifier.urihttp://hdl.handle.net/10072/36880
dc.description.abstractOn the loose: We report an STD NMR spectroscopic study of the polysialyltransferase from Neisseria meningitidis serogroup B (NmB-polyST). The spectra reveal that the cytosine and ribose moiety receive more saturation than the sialic acid residue of CMP-Neu5Ac. This loose binding enables a fast and efficient sialyl transfer to the acceptor substrate. Our analysis offers a view of the structural determinants necessary for binding to NmB-polyST that provide the basis for the development of novel NmB-polyST inhibitors.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherWiley-VCH Verlagen_US
dc.publisher.placeGermanyen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom170en_US
dc.relation.ispartofpageto174en_US
dc.relation.ispartofissue2en_US
dc.relation.ispartofjournalChemBioChemen_US
dc.relation.ispartofvolume11en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchMedical Biochemistry and Metabolomics not elsewhere classifieden_US
dc.subject.fieldofresearchcode110199en_US
dc.titleNeisseria meningitidis Serogroup B Polysialyltransferase: Insights into Substrate Bindingen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomicsen_US
gro.date.issued2010
gro.hasfulltextNo Full Text


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