CHEMAMP

Chemical AMPylomics: targeting a novel host-pathogen interaction

 Coordinatore IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE 

 Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD
city: LONDON
postcode: SW7 2AZ

contact info
Titolo: Ms.
Nome: Brooke
Cognome: Alasya
Email: send email
Telefono: +44 207 594 1181
Fax: +44 207 594 1418

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 209˙033 €
 EC contributo 209˙033 €
 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-2011-IEF
 Funding Scheme MC-IEF
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-03-01   -   2015-02-28

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE

 Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD
city: LONDON
postcode: SW7 2AZ

contact info
Titolo: Ms.
Nome: Brooke
Cognome: Alasya
Email: send email
Telefono: +44 207 594 1181
Fax: +44 207 594 1418

UK (LONDON) coordinator 209˙033.40

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

transferases    mechanism    translational    interactions    host    tools    ampylation    normal    chemical    signaling    cell    first    bacterial    post    pathogen    proteins    protein    amp   

 Obiettivo del progetto (Objective)

'In 2009 protein AMPylation, the reversible post-translational adenylation of target proteins with adenosine monophosphate (AMP), was first revealed as a novel mechanism for pathogenic bacteria to target and disrupt interactions of host GTPases with their cognate binding partners. Furthermore, there is growing evidence that AMPylation also operates as a general intracellular signaling mechanism in normal cell function. This novel post-translational modification is catalyzed by AMP transferases containing a so-called Fido motif that has been found across prokaryotes and eukaryotes, in over 2700 putative bacterial and mammalian proteins. Consequently, AMPylation is rapidly emerging as a fundamental mechanism to regulate protein-protein interactions and cell signaling in normal cells and in host-pathogen interactions, providing an opportunity for the discovery of new biology and targets for new antibiotics with novel mode of action. However, without robust tools to identify and manipulate both AMP transferases and their AMPylated protein substrates, our understanding of this complex signaling network will remain superficial. This Fellowship project aims to develop and apply chemical probes and technologies that will enable for the first time high-throughput analysis and exploration of the complex biological networks involved in protein AMPylation. These chemical tools will be applied to mapping the changes in AMPylation that occur during bacterial infection in the host and the pathogen, with the ultimate objective of identifying and validating cellular mechanisms that can be targeted for future antimicrobial therapy.'

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