Source:http://linkedlifedata.com/resource/pubmed/id/21078554
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-12-24
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pubmed:abstractText |
Affinity reagents that target protein kinases are powerful tools for signal transduction research. Here, we describe a general set of kinase ligands based on a 5-aminoindazole scaffold. This scaffold can readily be derivatized with diverse binding elements and immobilized analogs allow selective enrichment of protein kinases from complex mixtures.
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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:month |
Jan
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pubmed:issn |
1464-3405
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
550-4
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:21078554-Chromatography, High Pressure Liquid,
pubmed-meshheading:21078554-Indazoles,
pubmed-meshheading:21078554-Protein Binding,
pubmed-meshheading:21078554-Protein Kinases,
pubmed-meshheading:21078554-Signal Transduction,
pubmed-meshheading:21078554-Structure-Activity Relationship
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pubmed:year |
2011
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pubmed:articleTitle |
Protein kinase affinity reagents based on a 5-aminoindazole scaffold.
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pubmed:affiliation |
Department of Chemistry, Box 351700, University of Washington, Seattle, WA 98195-1700, United States.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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