Please use this identifier to cite or link to this item:
Title: Zooming into protein oligomerization in neurodegeneration using BiFC
Author: Gonçalves, Susana A.
Matos, Joana E.
Outeiro, Tiago F.
Issue Date: 2010
Publisher: Elsevier
Citation: Trends in Biochemical Sciences, November 2010, Vol. 35, No. 11
Abstract: Several neurodegenerative diseases are characterized by the accumulation of misfolded and aggregated proteins, which lead to neurotoxicity. However, the nature of those toxic species is controversial. Developments in optical microscopy and live-cell imaging are essential in providing crucial insight into the molecular mechanisms involved. In particular, the technique of bimolecular fluorescence complementation (BiFC) represents a remarkable improvement for observing protein protein interactions within living cells. Unlike other techniques, BiFC provides spatial and temporal resolution and can be carried out in a physiological environment. Among other applications, BiFC has been used to study molecular determinants of oligomerization in neurodegenerative disorders, thereby promising to unveil novel targets for therapeutics. We review the applicability of BiFC for investigating the molecular basis of neurodegenerative diseases associated with protein misfolding and aggregation.
Description: © 2010 Elsevier Ltd. All rights reserved.
Peer review: yes
ISSN: 0968-0004
Appears in Collections:IMM - Artigos em Revistas Internacionais

Files in This Item:
File Description SizeFormat 
Artigo.pdf380,38 kBAdobe PDFView/Open    Request a copy

FacebookTwitterDeliciousLinkedInDiggGoogle BookmarksMySpace
Formato BibTex MendeleyEndnote Degois 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.