Source:http://linkedlifedata.com/resource/pubmed/id/20936947
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2011-1-7
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pubmed:abstractText |
Low molecular weight ("small") GTPases are key regulators of a number of signaling cascades. Each GTPase is regulated by numerous guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and each GTPase binds to numerous effector proteins in a GTP-dependent manner. In many instances, individual regulators activate more than one GTPase, and each effector binds to one or more GTPases belonging to the same family. To untangle these complex networks, probes based on the principle of Förster resonance energy transfer (FRET) are widely used. Here, we provide an overview of the probes based on FRET and examples of discoveries achieved with them. In the process, we attempt to delineate the merits, current limitations, and future applications of this technique to pharmacological studies.
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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:month |
Feb
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pubmed:issn |
1545-4304
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
10
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pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
337-58
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pubmed:meshHeading |
pubmed-meshheading:20936947-Animals,
pubmed-meshheading:20936947-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:20936947-GTPase-Activating Proteins,
pubmed-meshheading:20936947-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:20936947-Humans,
pubmed-meshheading:20936947-Monomeric GTP-Binding Proteins,
pubmed-meshheading:20936947-Signal Transduction
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pubmed:year |
2011
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pubmed:articleTitle |
Spatiotemporal regulation of small GTPases as revealed by probes based on the principle of Förster Resonance Energy Transfer (FRET): Implications for signaling and pharmacology.
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pubmed:affiliation |
Department of Pathology and Biology of Diseases, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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