Objective "The modification of nuclear and cytoplasmic proteins by covalent attachment of N-acetylglucosamine (O-GlcNAc) to serine or threonine residues is emerging as a crucial regulatory posttranslational modification similar to phosphorylation. O-GlcNAc is essential for cell survival and is implicated in key biological processes (e. g., nutrient sensing, protein regulation and gene expression) and human diseases (e. g., diabetes, Alzheimer’s disease and cancer). In contrast to conventional protein glycosylation, O-GlcNAcylation is not further elaborated into complex glycans and occurs on intracellular proteins.Despite its biological importance, the functional roles and molecular details of O-GlcNAc modification remain to be elucidated; furthermore, no consensus sequence has been established for the site of glycosylation.With the goal of answering these questions, we propose herein novel chemical and enzymatic strategies to recapitulate and probe O-GlcNAcylation in vitro and in vivo. On the basis of the ""tag-and-modify"" approach to site-selective protein modification developed in Professor Davis' group, these investigations will be directed to enable the identification of O-GlcNAc-modified proteins and their specific glycosylation sites. Such strategies can be used as a powerful tool for elucidating the, as yet largely unknown, functional significance and molecular mechanisms of this dynamic posttranslational modification.On a professional basis, this multidisciplinary project will surely contribute significantly to the career development of the researcher, by adding different training and research competences along with complementary skills at an advanced level." Fields of science medical and health sciencesbasic medicineneurologydementiaalzheimernatural sciencesbiological sciencesbiochemistrybiomoleculesproteinsmedical and health sciencesclinical medicineendocrinologydiabetesnatural sciencesbiological sciencesbiochemistrybiomoleculescarbohydratesmedical and health sciencesclinical medicineoncology Programme(s) FP7-PEOPLE - Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013) Topic(s) FP7-PEOPLE-2013-IEF - Marie-Curie Action: "Intra-European fellowships for career development" Call for proposal FP7-PEOPLE-2013-IEF See other projects for this call Funding Scheme MC-IEF - Intra-European Fellowships (IEF) Coordinator THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD EU contribution € 231 283,20 Address WELLINGTON SQUARE UNIVERSITY OFFICES OX1 2JD Oxford United Kingdom See on map Region South East (England) Berkshire, Buckinghamshire and Oxfordshire Oxfordshire Activity type Higher or Secondary Education Establishments Administrative Contact Gill Wells (Ms.) Links Contact the organisation Opens in new window Website Opens in new window Total cost No data
