GLCNAC-PROBE

Novel chemical and enzymatic strategies for probing O-GlcNAc glycosylation

 Coordinatore THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD 

 Organization address address: University Offices, Wellington Square
city: OXFORD
postcode: OX1 2JD

contact info
Titolo: Ms.
Nome: Gill
Cognome: Wells
Email: send email
Telefono: +44 1865 289800
Fax: +44 1865 289801

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 231˙283 €
 EC contributo 231˙283 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-2013-IEF
 Funding Scheme MC-IEF
 Anno di inizio 2015
 Periodo (anno-mese-giorno) 2015-09-01   -   2017-08-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD

 Organization address address: University Offices, Wellington Square
city: OXFORD
postcode: OX1 2JD

contact info
Titolo: Ms.
Nome: Gill
Cognome: Wells
Email: send email
Telefono: +44 1865 289800
Fax: +44 1865 289801

UK (OXFORD) coordinator 231˙283.20

Mappa


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modification    proteins    molecular    glcnac    glycosylation    functional    basis    strategies    biological    posttranslational    protein    glcnacylation    site   

 Obiettivo del progetto (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.'

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