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dc.contributor.authorHaselhorst, Thomasen_US
dc.contributor.authorOschlies, Melanieen_US
dc.contributor.authorAbu-Izneid, Tareqen_US
dc.contributor.authorKiefel, Miltonen_US
dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorK. Münster-Kühnel, Anjaen_US
dc.contributor.authorGerardy-Schahn, Ritaen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.date.accessioned2017-04-24T07:56:29Z
dc.date.available2017-04-24T07:56:29Z
dc.date.issued2006en_US
dc.date.modified2010-08-26T07:37:35Z
dc.identifier.issn02820080en_US
dc.identifier.doi10.1007/s10719-006-6735-yen_AU
dc.identifier.urihttp://hdl.handle.net/10072/13719
dc.description.abstractCMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and CTP to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PP i . Saturation Transfer Difference (STD) NMR spectroscopy has been employed to investigate the sub-structural requirements of the enzyme's binding domain. Sialylnucleoside mimetics, where the sialic acid moiety has been replaced by a carboxyl group and a hydrophobic moiety, have been used in NMR experiments, to probe the tolerance of the CMP-Kdn synthetase to such replacements. From our data it would appear that unlike another sialylnucleotide-recognising protein, the CMP-Neu5Ac transport protein, either a phosphate group or other functional groups on the sialic acid framework may play important roles in recognition by the synthetase.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherSpringeren_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom371en_US
dc.relation.ispartofpageto375en_US
dc.relation.ispartofissue5/6en_US
dc.relation.ispartofjournalGlycoconjugate Journalen_US
dc.relation.ispartofvolume23en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchcode270108en_US
dc.subject.fieldofresearchcode270199en_US
dc.subject.fieldofresearchcode320302en_US
dc.titleA 1H STD NMR spectroscopic investigation of sialylnucleoside mimetics as probes of CMP-Kdn synthetaseen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2006
gro.hasfulltextNo Full Text


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