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MPA-ND SIGNED

Membrane protein aggregation and its links with neurodegenerative diseases

Total Cost €

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EC-Contrib. €

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Partnership

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Project "MPA-ND" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE 

Organization address
address: TRINITY LANE THE OLD SCHOOLS
city: CAMBRIDGE
postcode: CB2 1TN
website: www.cam.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Project website http://www.ch.cam.ac.uk/person/ks741
 Total cost 183˙454 €
 EC max contribution 183˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2015
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2016
 Duration (year-month-day) from 2016-03-01   to  2018-02-28

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE UK (CAMBRIDGE) coordinator 183˙454.00

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 Project objective

Protein aggregation is associated with some of the most prevalent and devastating neurodegenerative disorders in our society, including Alzheimer’s and Parkinson’s diseases. The intricate details of the aggregation process are now beginning to emerge through major efforts for characterizing the associated protein deposits . However, knowledge about the aggregation of membrane proteins, which account for about one third of the human genome , is still almost completely missing despite increasing evidence that implicates in particular the aggregation of those in the respiratory chain and glucose metabolism in pathological pathways. To cover this huge gap, this project is aimed at elucidating the association of membrane protein aggregation with neurodegenerative diseases. The extensive biophysical investigation of the aggregates of two model sugar transporter proteins, galactose (GalP) and lactose (LacY) permeases, is proposed. Initially, controlled ways to promote the aggregation of these two proteins will be investigated in detail. The use of a range of biophysical spectroscopic methods is proposed to obtain information on the nature of the aggregates and their formation process. Further in vivo experiments will probe bacterial ageing in the presence of these aggregates. This work is expected to lead to new insights into the nature of membrane protein aggregates, characterization of their formation, and determination of their possible roles in neurodegenerative processes.

 Publications

year authors and title journal last update
List of publications.
2017 Karen Stroobants, Janet R. Kumita, Nicola J. Harris, Dimitri Y. Chirgadze, Christopher M. Dobson, Paula J. Booth, Michele Vendruscolo
Amyloid-like Fibrils from an α-Helical Transmembrane Protein
published pages: 3225-3233, ISSN: 0006-2960, DOI: 10.1021/acs.biochem.7b00157
Biochemistry 56/25 2019-06-13

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