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Title: Current chemical biology tools for studying protein phosphorylation and dephosphorylation
Authors: H.s. Lu, C.
Liu, K.
Tan, L.P. 
Yao, S.Q. 
Keywords: activity-based protein profiling
small-molecule microarray
Issue Date: 2-Jan-2012
Source: H.s. Lu, C., Liu, K., Tan, L.P., Yao, S.Q. (2012-01-02). Current chemical biology tools for studying protein phosphorylation and dephosphorylation. Chemistry - A European Journal 18 (1) : 28-39. ScholarBank@NUS Repository.
Abstract: Amongst different posttranslational events involved in cellular-signaling pathways, phosphorylation and dephosphorylation of proteins are the most prevalent. Aberrant regulations in the cellular phosphoproteome network are implicated in most major human diseases. Consequently, kinases and phosphatases are two of the most important groups of drug targets in medicinal research today. A major challenge in the understanding of protein phosphorylation and dephosphorylation is the sheer complexity of the phosphoproteome network and the lack of tools capable of studying protein phosphorylation and dephosphorylation as they occur in cells. We highlight herein various chemical biology tools that have emerged in the last decade for such studies. First, we discuss the use of small-molecule mimics of phosphoamino acids and their use in elucidating the function of protein phosphorylation and dephosphorylation. We also introduce recent advances in the field of activity-based protein profiling (ABPP) for proteome-wide detection of protein phosphorylation and dephosphorylation. We next discuss the key concepts in the design of peptide-and protein-based biosensors capable of real-time reporting of phosphorylation/dephosphorylation events. Finally, we highlight the application of peptide and small-molecule microarrays (SMMs), and their applications in high-throughput screening and discovery of new compounds related to phosphorylation/dephosphorylation. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Source Title: Chemistry - A European Journal
ISSN: 09476539
DOI: 10.1002/chem.201103206
Appears in Collections:Staff Publications

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