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dc.contributor.advisorDavey, Gavin
dc.contributor.authorGluchowska, Sonia Agnieszka
dc.date.accessioned2019-11-06T14:34:58Z
dc.date.available2019-11-06T14:34:58Z
dc.date.issued2011
dc.identifier.citationSonia Agnieszka Gluchowska, 'GlcNAc transferases and glycoengineering in Chinese hamster ovary cells', [thesis], Trinity College (Dublin, Ireland). School of Biochemistry and Immunology, 2011, pp 272
dc.identifier.otherTHESIS 9146
dc.description.abstractGlycosylation constitutes one of the most important post-translational modifications of proteins, with over 60% of proteins known to be glycosylated. GlcNAc transferases (GnTs) belong to a large subfamily of glycosyltransferases residing in the Golgi apparatus and play a key role in the synthesis of mature A-linked glycan structures attached to proteins. In forming multi-antennary A-glycan structures in Chinese hamster ovary cells (CHO), GlcNAc residues may be added to the trimannosyl core by four different GlcNAc transferases (I, II, IV and V).
dc.format1 volume
dc.language.isoen
dc.publisherTrinity College (Dublin, Ireland). School of Biochemistry and Immunology
dc.relation.isversionofhttp://stella.catalogue.tcd.ie/iii/encore/record/C__Rb14633201
dc.subjectBiochemistry, Ph.D.
dc.subjectPh.D. Trinity College Dublin.
dc.titleGlcNAc transferases and glycoengineering in Chinese hamster ovary cells
dc.typethesis
dc.type.supercollectionthesis_dissertations
dc.type.supercollectionrefereed_publications
dc.type.qualificationlevelDoctoral
dc.type.qualificationnameDoctor of Philosophy (Ph.D.)
dc.rights.ecaccessrightsopenAccess
dc.format.extentpaginationpp 272
dc.description.noteTARA (Trinity’s Access to Research Archive) has a robust takedown policy. Please contact us if you have any concerns: rssadmin@tcd.ie
dc.identifier.urihttp://hdl.handle.net/2262/90186


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