Source:http://linkedlifedata.com/resource/pubmed/id/11400335
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2001-6-12
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pubmed:abstractText |
Experimental protocols that allow confident assignment of signaling proteins to specific subdomains of the plasma membrane are essential for a full understanding of the complexities of signal transduction. This is especially relevant for Ras proteins, where the different membrane anchors of the Ras isoforms target them to functionally distinct microdomains that in turn allow quantitatively different signal outputs from otherwise highly homologous proteins. The methods outlined in this chapter, in addition to being invaluable in addressing Ras function, should also have wide utility in the study of many mammalian signal transduction pathways.
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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 |
0076-6879
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
333
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
172-83
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11400335-Animals,
pubmed-meshheading:11400335-Caveolin 1,
pubmed-meshheading:11400335-Caveolins,
pubmed-meshheading:11400335-Cell Membrane,
pubmed-meshheading:11400335-Cells, Cultured,
pubmed-meshheading:11400335-Cricetinae,
pubmed-meshheading:11400335-Immunohistochemistry,
pubmed-meshheading:11400335-Microscopy, Electron,
pubmed-meshheading:11400335-Mutation,
pubmed-meshheading:11400335-Protein Structure, Tertiary,
pubmed-meshheading:11400335-Transfection,
pubmed-meshheading:11400335-ras Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Caveolin and Ras function.
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pubmed:affiliation |
Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Institute of Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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