Source:http://linkedlifedata.com/resource/pubmed/id/17649968
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2007-7-25
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pubmed:abstractText |
Chemical modification of proteins with bifunctional reagents has become a widely used technique for analyzing protein structure and dynamics. A new era is emerging, and scientists can now actually control the function of proteins by tethering molecular switches at a desired position. In a new paper, researchers stretch the technique a bit further by using a reactive derivative of a peptide toxin to probe the subunit composition of a voltage-gated K+ channel.
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pubmed:commentsCorrections | |
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 |
Jul
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pubmed:issn |
1554-8937
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
451-3
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pubmed:meshHeading | |
pubmed:year |
2007
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pubmed:articleTitle |
Staples, tape measures, and bungee cords: a variety of bifunctional reagents for understanding and controlling ion channels.
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pubmed:affiliation |
Department of Molecular and Cell Biology, University of California-Berkeley, Berkeley, California 94720-3200, USA.
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pubmed:publicationType |
Journal Article,
Comment
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