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dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorSchauer, Rolanden_US
dc.contributor.editorKen-ichi Kasai (Kanagawa)en_US
dc.date.accessioned2017-04-24T11:32:11Z
dc.date.available2017-04-24T11:32:11Z
dc.date.issued2004en_US
dc.date.modified2009-09-01T06:00:38Z
dc.identifier.issn09157352en_US
dc.identifier.doihttp://www.gak.co.jp/TIGG/87pdf/87e.htmlen_AU
dc.identifier.urihttp://hdl.handle.net/10072/5053
dc.description.abstractNaturally occurring sialic acids can be O-acetylated at any one of four hydroxyl groups, located at position C-4, -7, -8, and -9. This modification, which is found in nearly all animals expressing sialic acids and certain bacteria, is known to be involved in regulating a variety of biological events. One of the more important processes that appear to be heavily influenced by O-acetylation is cancer development. The present review outlines some of the more recent advances towards understanding the role and regulation of sialic acid O-acetylation in human colorectal cancer, basalioma and melanoma. Even though great strides have been made towards identifying and characterising the biological role of O-acetylated sialic acids, detailed information concerning the transferase activity responsible for this modification remains vague. The 7(9)-O- and 4-O-specific acetyltransferases were identified in bovine and horse submandibular glands, respectively, over 30 years ago, however despite the efforts of a number of groups these enzymes have stubbornly escaped purification and cloning, remaining elusive. Here we will attempt to summarise the available data gathered over several decades, as well as detailing recent advances towards understanding the mechanism and regulation of this enigmatic enzyme.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherGakushin Publishing Co.en_US
dc.publisher.placeJapanen_US
dc.publisher.urihttp://www.gak.co.jp/TIGG/index.htmlen_AU
dc.relation.ispartofpagefrom1en_US
dc.relation.ispartofpageto15en_US
dc.relation.ispartofissue87en_US
dc.relation.ispartofjournalTrends in Glycoscience and Glycotechnologyen_US
dc.relation.ispartofvolume16en_US
dc.subject.fieldofresearchcode320302en_US
dc.titleThe Enigma of Enzymatic Sialic Acid O-Acetylationen_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.issued2004
gro.hasfulltextNo Full Text


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