Source:http://linkedlifedata.com/resource/pubmed/id/20967581
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2010-10-22
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pubmed:abstractText |
Recent data suggest that soluble, non-fibrillar assemblies of the amyloid ?-protein (A?) may mediate the synaptic deficits that characterize the early stages of Alzheimer's disease. Consequently, much effort has been expended in isolating and studying a variety of different A? assemblies. Here, we describe the use of immunoprecipitation/western blotting and size exclusion chromatography/western blotting to characterize A? present in conditioned medium from cultured cells, human cerebrospinal fluid, and human cortex extracted with aqueous buffer, detergent, and formic acid.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1940-6029
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
670
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33-44
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pubmed:meshHeading |
pubmed-meshheading:20967581-Amyloid beta-Peptides,
pubmed-meshheading:20967581-Blotting, Western,
pubmed-meshheading:20967581-Brain,
pubmed-meshheading:20967581-Cell Line,
pubmed-meshheading:20967581-Cells, Cultured,
pubmed-meshheading:20967581-Chromatography, Gel,
pubmed-meshheading:20967581-Culture Media, Conditioned,
pubmed-meshheading:20967581-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:20967581-Humans,
pubmed-meshheading:20967581-Immunoprecipitation
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pubmed:year |
2011
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pubmed:articleTitle |
Isolation of low-n amyloid ?-protein oligomers from cultured cells, CSF, and brain.
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pubmed:affiliation |
Center for Neurologic Diseases, Brigham & Women's Hospital, Harvard Medical School, Boston, MA, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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