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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2005-6-30
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pubmed:abstractText |
High-throughput screening is used by the pharmaceutical industry for identifying lead compounds that interact with targets of pharmacological interest. Because of the key role that aberrant regulation of protein phosphorylation plays in diseases such as cancer, diabetes and hypertension, kinases have become one of the main drug targets. With the exception of antibody-based assays, methods to screen for specific kinase activity are generally restricted to the use of small synthetic peptides as substrates. However, the use of natural protein substrates has the advantage that potential inhibitors can be detected that affect enzyme activity by binding to a site other than the catalytic site. We have previously reported a non-radioactive and non-antibody-based fluorescence quench assay for detection of phosphorylation or dephosphorylation using synthetic peptide substrates. The aim of this work is to develop an assay for detection of phosphorylation of chemically unmodified proteins based on this polymer superquenching platform.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-10535914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-10720314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-10970784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-11080688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-11742082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-12120282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-12471243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-12895464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-15090152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-15165511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-15165513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-15165514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-15165516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-15494445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-1658551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-8660605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15927069-9451512
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EIF4EBP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/IRAK4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1 Receptor-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Basic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1472-6750
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16
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pubmed:dateRevised |
2010-9-20
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pubmed:meshHeading |
pubmed-meshheading:15927069-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15927069-Animals,
pubmed-meshheading:15927069-Binding Sites,
pubmed-meshheading:15927069-Carrier Proteins,
pubmed-meshheading:15927069-Cattle,
pubmed-meshheading:15927069-Fluorescence Polarization,
pubmed-meshheading:15927069-Fluorescent Dyes,
pubmed-meshheading:15927069-Histones,
pubmed-meshheading:15927069-Humans,
pubmed-meshheading:15927069-Inhibitory Concentration 50,
pubmed-meshheading:15927069-Interleukin-1 Receptor-Associated Kinases,
pubmed-meshheading:15927069-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:15927069-Ions,
pubmed-meshheading:15927069-Myelin Basic Proteins,
pubmed-meshheading:15927069-Peptide Library,
pubmed-meshheading:15927069-Peptides,
pubmed-meshheading:15927069-Phosphoproteins,
pubmed-meshheading:15927069-Phosphorylation,
pubmed-meshheading:15927069-Phosphotransferases,
pubmed-meshheading:15927069-Polymers,
pubmed-meshheading:15927069-Protein Array Analysis,
pubmed-meshheading:15927069-Protein Kinase C-alpha,
pubmed-meshheading:15927069-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15927069-Proteins,
pubmed-meshheading:15927069-Quantitative Trait Loci,
pubmed-meshheading:15927069-Sequence Analysis, Protein
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pubmed:year |
2005
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pubmed:articleTitle |
High-throughput kinase assays with protein substrates using fluorescent polymer superquenching.
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pubmed:affiliation |
QTL Biosystems, 2778 Agua Fria Street, Santa Fe, NM 87507, USA. frauke@qtlbio.com
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pubmed:publicationType |
Journal Article
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