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https://doi.org/10.1002/qsar.200740064
Title: | Click chemistry as a high-throughput amenable platform in catalomics | Authors: | Kalesh, K.A. Yang, P.-Y. Srinivasan, R. Shao, Q.Y. |
Keywords: | Activity-based probes Catalomics Click chemistry Enzyme inhibitors Fragment-based assembly Inhibitor fingerprinting |
Issue Date: | Dec-2007 | Citation: | Kalesh, K.A., Yang, P.-Y., Srinivasan, R., Shao, Q.Y. (2007-12). Click chemistry as a high-throughput amenable platform in catalomics. QSAR and Combinatorial Science 26 (11-12) : 1135-1144. ScholarBank@NUS Repository. https://doi.org/10.1002/qsar.200740064 | Abstract: | Click chemistry is emerging as a powerful tool to elucidate the complex catalytic functions that enzymes perform in the biological system. Recent advances in proteomics heavily rely on the robust, modular and high-throughput platform offered by click chemistry. This minireview focuses on the central role click chemistry has played on the most recent advances in the chemical proteomic research involving the discovery of enzyme inhibitors and enzyme profiling using Activity-Based Probes (ABPs). The strength and benefit of click chemistry and its novel variants, such as the so-called in situ screening using click chemistry have been even more evident recently when this novel chemistry is coupled with high-throughput assay technologies such as microarrays and characterization techniques such as Liquid Chromatography-Mass Spectrometry in Selected Ion Mode (LCMS-SIM) and multidimensional LC-MS. The invaluable contribution of click chemistry in the emerging field of "Catalomics" is thus firmly established. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA. | Source Title: | QSAR and Combinatorial Science | URI: | http://scholarbank.nus.edu.sg/handle/10635/77518 | ISSN: | 1611020X | DOI: | 10.1002/qsar.200740064 |
Appears in Collections: | Staff Publications |
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