Source:http://linkedlifedata.com/resource/pubmed/id/16368465
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2005-12-21
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pubmed:abstractText |
The cell membrane is a 2-dimensional non-ideal liquid containing dynamic structures on various time-space scales, and the raft domain is one of them. Existing literature supports the concept that raft dynamics may be important for its formation and function: the raft function may be supported by stimulation-induced raft association/coalescence and recruitment of various raftophilic molecules to coalesced rafts, and, importantly, they both may happen transiently. Thus, one must always consider the limited association time of a raft or a raftophilic molecule with another raft, even when one interprets the results of static experiments, such as immunofluorescence and pull-down assays. Critical considerations on the chemical fixation mechanism and immunocolocalization data suggest that the temporary nature of raft-based molecular interactions may explain why colocalization results are sensitive to subtle variations in experimental conditions employed in different laboratories.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Fixatives,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
1746
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
234-51
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pubmed:meshHeading |
pubmed-meshheading:16368465-Animals,
pubmed-meshheading:16368465-Cell Membrane,
pubmed-meshheading:16368465-Cross-Linking Reagents,
pubmed-meshheading:16368465-Detergents,
pubmed-meshheading:16368465-Diffusion,
pubmed-meshheading:16368465-Fixatives,
pubmed-meshheading:16368465-Fluorescent Antibody Technique,
pubmed-meshheading:16368465-Glycosylphosphatidylinositols,
pubmed-meshheading:16368465-Humans,
pubmed-meshheading:16368465-Membrane Fluidity,
pubmed-meshheading:16368465-Membrane Lipids,
pubmed-meshheading:16368465-Membrane Microdomains,
pubmed-meshheading:16368465-Membrane Proteins,
pubmed-meshheading:16368465-Models, Biological
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pubmed:year |
2005
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pubmed:articleTitle |
Toward understanding the dynamics of membrane-raft-based molecular interactions.
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pubmed:affiliation |
The Institute for Frontier Medical Sciences, Kyoto University, 606-8507, Japan. akusumi@frontier.kyoto-u.ac.jp
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pubmed:publicationType |
Journal Article,
Review
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