ADP-Specific Sensors Enable Universal Assay of Protein Kinase Activity

Two molecular sensors that specifically recognize ADP in a background of over 100-fold molar excess of ATP are described. These sensors are nucleic-acid based and comprise a general method for monitoring protein kinase activity. The ADP-aptamer scintillation proximity assay is configured in a single...

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Published inChemistry & biology Vol. 11; no. 4; pp. 499 - 508
Main Authors Srinivasan, Jayaram, Cload, Sharon T, Hamaguchi, Nobuko, Kurz, Jeffrey, Keene, Sara, Kurz, Markus, Boomer, Ryan M, Blanchard, Jill, Epstein, David, Wilson, Charles, Diener, John L
Format Journal Article
LanguageEnglish
Published United States Elsevier Ltd 01.04.2004
Subjects
Adenosine Diphosphate - analysis
Adenosine Diphosphate - metabolism
Adenosine Triphosphate - metabolism
Base Sequence
Biosensing Techniques - methods
Fluorescence
Ligands
Molecular Sequence Data
Protein Kinases - analysis
Protein Kinases - metabolism
RNA, Catalytic - chemistry
RNA, Catalytic - metabolism
Signal Transduction
Substrate Specificity
Time Factors
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Summary:Two molecular sensors that specifically recognize ADP in a background of over 100-fold molar excess of ATP are described. These sensors are nucleic-acid based and comprise a general method for monitoring protein kinase activity. The ADP-aptamer scintillation proximity assay is configured in a single-step, homogeneous format while the allosteric ribozyme (RiboReporter) sensor generates a fluorescent signal upon ADP-dependent ribozyme self-cleavage. Both systems perform well when configured for high-throughput screening and have been used to rediscover a known protein kinase inhibitor in a high-throughput screening format.
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ISSN:1074-5521
1879-1301
DOI:10.1016/j.chembiol.2004.03.014