Cancer Institute A national cancer institute
designated cancer center

Matthew Bogyo

Publication Details

  • Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain BIOORGANIC & MEDICINAL CHEMISTRY LETTERS Sexton, K. B., Witte, M. D., Blum, G., Bogyo, M. 2007; 17 (3): 649-653

    Abstract:

    Asparaginyl endopeptidase (AEP), also known as legumain, is a cysteine protease that has been ascribed roles in antigen presentation yet its exact role in human biology remains poorly understood. We report here, the use of a positional scanning combinatorial library of peptide AOMKs containing a P1 aspartic acid to probe the P2, P3, and P4 subsite specificity of endogenous legumain. Using inhibitor specificity profiles of cathepsin B and legumain, we designed fluorescent ABPs that are highly selective, cell-permeable reagents for monitoring legumain activity in complex proteomes.

    View details for DOI 10.1016/j.bmcl.2006.10.100

    View details for Web of Science ID 000244170700015

    View details for PubMedID 17189693

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