ENDOSIGNAL

Endosignal

 Coordinatore THE UNIVERSITY OF SHEFFIELD 

 Organization address address: FIRTH COURT WESTERN BANK
city: SHEFFIELD
postcode: S10 2TN

contact info
Titolo: Mrs.
Nome: Joanne
Cognome: Watson
Email: send email
Telefono: +44 114 222 4754
Fax: +44 114 222 1455

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 100˙000 €
 EC contributo 100˙000 €
 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-CIG
 Funding Scheme MC-CIG
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-09-01   -   2017-08-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    THE UNIVERSITY OF SHEFFIELD

 Organization address address: FIRTH COURT WESTERN BANK
city: SHEFFIELD
postcode: S10 2TN

contact info
Titolo: Mrs.
Nome: Joanne
Cognome: Watson
Email: send email
Telefono: +44 114 222 4754
Fax: +44 114 222 1455

UK (SHEFFIELD) coordinator 100˙000.00

Mappa


 Word cloud

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

cells    epithelial    domain    protein    membrane    pdz    zebrafish    bowel    molecular    immune    cell    disease    nod    frmpd    model    inflammatory   

 Obiettivo del progetto (Objective)

'Inflammatory bowel disease is a devastating disease affecting several million people in Europe. This proposal addresses the molecular mechanism of inflammatory bowel disease. The multi-PDZ domain protein FRMPD2 (FERM and PDZ domain containing protein 2) has been shown to be an integral part of the immune host defense of epithelial cells by recruiting NOD2 (Nucleotide-binding and oligomerization protein 2), a key player of the innate immune system, to the basolateral membrane in epithelial cells. In addition, FRMPD2 is involved in epithelial cell/cell adhesion regulating tight junction formation. Multi-PDZ domain proteins are scaffolding molecules assembling large protein complexes dedicated to signaling and membrane trafficking. Interaction of NOD2 with FRMPD2 places the NOD2 protein into a novel context being part of a larger protein complex. Using an interdisciplinary approach combining state of the art techniques from cell biology, protein chemistry, membrane physics and developmental genetics, this proposal aims at the identification and functional characterization of novel components of the FRMPD2 protein complex. In particular, this protein complex will be characterized with respect to mechanisms relevant to epithelial cell polarization and inflammatory bowel disease. Finally, the project aims to complement in vitro mechanistic and cell culture data with in vivo results by analyzing the role of the FRMPD2 complex in zebrafish development. Finally, using a Salmonella infection model, a zebrafish animal model for inflammatory bowel disease based on the FRMPD2 complex will be established. The results of this project will lead to a better molecular understanding of the disease opening potentially new avenues of treatments.'

Altri progetti dello stesso programma (FP7-PEOPLE)

HSPB8 AND NEUROPATHY (2009)

Role of the HspB8/Bag3 chaperone complex in neurodegenerative disorders

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SELGIFS (2013)

Study of Emission Line Galaxies with Integral Field Spectroscopy

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SOLAS (2013)

Scalable management Of LArge Scale cloud computing environments using enhanced software-defined networking technologies

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