Linked Life Data

15910781

Source:http://linkedlifedata.com/resource/pubmed/id/15910781

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2005-5-24
pubmed:abstractText
We examined the ultrastructural localization of oligomeric proteins, Abeta42, and flotillin-1 in Tg2576 mouse brains by triple immunoelectron microscopy. Oligomer-specific immunoreactions localized to cell processes, especially to axon terminals with higher density in Tg than in nonTg mouse brains. The oligomer was less frequently colocalized to flotillin-1-immunoreactive rafts than Abeta42, suggesting that rafts are one of the sites of polymeric Abeta deposition, but not of oligomeric proteins including Abeta.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-8993
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
1045
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
224-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain.
pubmed:affiliation
Gunma University School of Health Sciences, 3-39-15 Showa-machi, Maebashi 371-8514, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't