Linked Life Data

16092089

Source:http://linkedlifedata.com/resource/pubmed/id/16092089

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-8-15
pubmed:abstractText
alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Its relevance to Parkinson's disease (PD) is based on mutations found in familial cases of the disease and its presence in filaments of Lewy bodies (LB) and Lewy neurites (LN) in sporadic cases where it is packed in a beta-sheet configuration. This structural plasticity of alpha-synuclein has raised the possibility that neurodegeneration may be a consequence of abnormal protein folding. The extent to which abnormal folding and aggregation of neuronal proteins is directly toxic to the cell, an inert biochemical marker of an underlying harmful metabolic defect, or a protective reaction remains to be seen. We review the function of alpha-synuclein and recent studies that have shed light on the mechanisms by which it aggregates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0885-3185
pubmed:author
pubmed:copyrightInfo
Copyright 2005 Movement Disorder Society.
pubmed:issnType
Print
pubmed:volume
20 Suppl 12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S37-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Alpha-synuclein dysfunction in Lewy body diseases.
pubmed:affiliation
Cambridge Centre for Brain Repair, University of Cambridge, UK.
pubmed:publicationType
Journal Article, In Vitro