Linked Life Data

20561791

Source:http://linkedlifedata.com/resource/pubmed/id/20561791

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2010-11-1
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0968-0004
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
643-51
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Zooming into protein oligomerization in neurodegeneration using BiFC.
pubmed:affiliation
Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't