ADP-Specific Sensors Enable Universal Assay of Protein Kinase Activity
| Autor: | Jeffrey Kurz, Sara Chesworth Keene, John L. Diener, Ryan M. Boomer, Jayaram Srinivasan, Charles Wilson, David Epstein, Markus Kurz, Jill Blanchard, Nobuko Hamaguchi, Sharon T. Cload |
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| Rok vydání: | 2004 |
| Předmět: |
Time Factors
medicine.drug_class Allosteric regulation Molecular Sequence Data Clinical Biochemistry Biosensing Techniques Ligands Biochemistry Fluorescence Substrate Specificity Adenosine Triphosphate Drug Discovery medicine RNA Catalytic Protein kinase A Molecular Biology Pharmacology biology Base Sequence Ribozyme RNA General Medicine Protein kinase inhibitor Adenosine Diphosphate Scintillation proximity assay biology.protein Molecular Medicine Signal transduction Protein Kinases Signal Transduction |
| Zdroj: | Chemistry & Biology. 11(4):499-508 |
| ISSN: | 1074-5521 |
| DOI: | 10.1016/j.chembiol.2004.03.014 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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