72304-24-6Relevant academic research and scientific papers
Profiling of glycosidase activities using coumarin-conjugated glycoside cocktails
Park, Sungjin,Shin, Injae
, p. 619 - 622 (2007/10/03)
Glycosidases are a large subgroup of carbohydrate-processing enzymes that hydrolytically cleave the glycosidic bond. Glycans formed by the action of glycosidases are involved in various biological processes. Genetic abnormalities in glycosidases are associated with inherited diseases. Thus, characterization of the catalytic activities of glycosidases is of great importance. Herein, we describe a simple and rapid approach for determining glycosidase activity profiles using coumarin-conjugated glycoside cocktails.
Site-specific labelling of proteins
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, (2008/06/13)
An in vivo method for labelling a protein having an N-terminal cysteine is disclosed. A probe comprising a thioester group and a detectable label is introduced into a cell expressing the N-terminal cysteine protein, allowing for the N-terminal cysteine to cleave the thioester bond and resulting in the label being covalently attached to the N-terminus of the protein by an amide bond.
Cell-permeable small molecule probes for site-specific labeling of proteins.
Yeo, Dawn S Y,Srinivasan, Rajavel,Uttamchandani, Mahesh,Chen, Grace Y J,Zhu, Qing,Yao, Shao Q
, p. 2870 - 2871 (2007/10/03)
We have successfully synthesized a number of small molecule probes designed for site-specific labeling of N-terminal cysteine-containing proteins expressed in live cells. Their utility for site-specific, covalent modifications of proteins was successfully demonstrated with purified proteins in vitro, and with live bacterial cells in vivo.
