Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0040-4039(02)02724-7
Title: Design and synthesis of an affinity probe that targets caspases in proteomic experiments
Authors: Liau, M.-L.
Panicker, R.C.
Yao, S.Q. 
Issue Date: 27-Jan-2003
Citation: Liau, M.-L., Panicker, R.C., Yao, S.Q. (2003-01-27). Design and synthesis of an affinity probe that targets caspases in proteomic experiments. Tetrahedron Letters 44 (5) : 1043-1046. ScholarBank@NUS Repository. https://doi.org/10.1016/S0040-4039(02)02724-7
Abstract: The field of proteomics aims to study all proteins in the human proteome. This huge task may be accelerated by using active-site directed probes which profile proteins in an activity-dependent manner. Herein, we have developed a fluorescently-labeled affinity probe containing chemical reactivity specific towards caspases. Preliminary assays and proof-of-concept experiments demonstrated that this probe exhibits strong chemical reactivity towards caspase-1 over other enzymes, capable of covalently labeling caspapse-1 over other non-caspase enzymes. This thus demonstrates its selectivity and potential in high-throughput screenings of other unknown caspases in a large-scale proteomics experiment. © 2003 Elsevier Science Ltd. All rights reserved.
Source Title: Tetrahedron Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/75866
ISSN: 00404039
DOI: 10.1016/S0040-4039(02)02724-7
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