Linked Life Data

14655766

Source:http://linkedlifedata.com/resource/pubmed/id/14655766

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-12-5
pubmed:abstractText
Protein aggregation and misfolding characterize most age-related neurodegenerative diseases including Alzheimer, Parkinson and Huntington diseases. Protein aggregation has generally been assumed to be responsible for neurodegeneration in these disorders due to association and genetics. However, protein aggregation may, in fact, be an attempt to protect neurons from the stress resulting from the disease etiology. In this review, we weigh the evidence of whether removal of amyloids, aggregates and neuronal inclusions represent a reasonable strategy for protecting neurons.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1015-6305
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
630-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Will preventing protein aggregates live up to its promise as prophylaxis against neurodegenerative diseases?
pubmed:affiliation
Institute of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
pubmed:publicationType
Journal Article, Review