TOPIC

TOPIC: Targeting Cytotoxic Protein Oligomers

 Coordinatore AARHUS UNIVERSITET 

 Organization address address: Nordre Ringgade 1
city: AARHUS C
postcode: 8000

contact info
Titolo: Mrs.
Nome: Anne Marie
Cognome: Marcussen
Email: send email
Telefono: +45 20353887

 Nazionalità Coordinatore Denmark [DK]
 Totale costo 586˙111 €
 EC contributo 586˙111 €
 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-ITN
 Funding Scheme MC-ITN
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-09-01   -   2017-08-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    AARHUS UNIVERSITET

 Organization address address: Nordre Ringgade 1
city: AARHUS C
postcode: 8000

contact info
Titolo: Mrs.
Nome: Anne Marie
Cognome: Marcussen
Email: send email
Telefono: +45 20353887

DK (AARHUS C) coordinator 553˙875.50
2    CROSSBETA BIOSCIENCES BV

 Organization address address: PADUALAAN 8
city: UTRECHT
postcode: 3584 CH

contact info
Titolo: Dr.
Nome: Martijn
Cognome: Gebbink
Email: send email
Telefono: +31 302532483

NL (UTRECHT) participant 32˙235.50

Mappa


 Word cloud

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

proteins    strategy    cytotoxic    biophysical    protein    parkinson    disease    techniques    interactions    therapeutic    diseases    esrs    mass    small    cellular    oligomers    oligomeric    huntington    eid    amyloid   

 Obiettivo del progetto (Objective)

'Parkinson's disease and Huntington's disease are highly debilitating diseases for which no disease modifying treatment is available. This EID proposal, called TOPIC (Targeting Cytotoxic Protein Oligomers), will train 2 ESRs to target the oligomeric protein aggregate which accumulates in these diseases. These oligomers occur under conditions which eventually lead to the accumulation of fibrillar amyloid deposits. However, there is increasing consensus that the amyloid state is biologically inert and the cytotoxic species is the oligomeric structure. Our approach rests on the working hypothesis that the cytotoxic oligomers engage in a number of unwanted interactions with proteins and membranes. The 2 ESRs will combine proprietary technology to stabilize these oligomers with state-of-the-art mass spectrometry and biophysical techniques to identify, quantitate and rank these interactions within the context of the cellular interactome. The next goal (building directly on the EID outcome but outside its present scope) is to develop small-molecule inhibitors of these interactions as a therapeutic strategy to eliminate cell death and disease progression. This training programme offers a unique opportunity for the 2 ESRs to carry out central parts of translational research in both an academic and SME setting, spanning a multitude of different cellular, biophysical and mass spectrometric techniques of general use in the life sciences. Our target oligomeric proteins are α-synuclein (Parkinson’s Disease) and the N-terminal part of exon 1 of huntingtin (Huntington’s Disease). By analysing two different proteins in parallel projects, we will be able to validate the robustness of our approach and potentially identify generic small molecules to target misfolded protein oligomers in general. Our approach will allow the ESRs to develop a general therapeutic strategy that targets a major class of devastating disease affecting the daily lives of millions of people throughout the world.'

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