Mammals express seven different catalytically active proteasome subunits. In order to determine the roles of the different proteolytically active subunits in antigen presentation and other cellular processes, highly specific inhibitors and activity-based probes that selectively target specific active sites are needed. In this work we present the development of fluorescent activity-based probes that selectively target the β1 and β5 sites of the constitutive proteasome.
To meet the increasing clinical demand for the diagnostic agent (4′‐deoxychitobiosyl)‐4‐methylumbelliferone, a flexible and scalable route of synthesis is needed. In this paper such a route is presented. The key to the route is the use of a partially protected thiophenyl glucosamine as starting material for the preparation of both the reducing and nonreducing end building blocks of the 4′‐deoxychitobiose disaccharide.
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