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• W2001124847 abstract "Mammalian asparaginyl endopeptidase (AEP) or legumain is a recently identified lysosomal cysteine protease belonging to clan CD. To date it has been shown to be involved in antigen presentation within class II MHC positive cells and in pro-protein processing. Further elucidation of the biological functions of the enzyme will require potent and selective inhibitors and thus we describe here new acyloxymethylketone inhibitors of AEP. The most potent of the series is 2,6-dimethyl-benzoic acid 3-benzyloxycarbonylamino-4-carbamoyl-2-oxo-butyl ester (MV026630) with a kobs/[I] value of 1.09 x 10(5) M(-1) s(-1). At low microM concentrations this compound is able to enter living cells and irreversibly inactivate AEP. We show that this results in inhibition of AEP autoactivation and in perturbation of the processing and presentation of T cell epitopes from both tetanus toxin and myelin basic protein." @default.
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• W2001124847 date "2003-01-20" @default.
• W2001124847 modified "2023-09-25" @default.
• W2001124847 title "Novel Cell-Permeable Acyloxymethylketone Inhibitors of Asparaginyl Endopeptidase" @default.
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• W2001124847 doi "https://doi.org/10.1515/bc.2003.136" @default.
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