期刊
CHEMISTRY & BIOLOGY
卷 22, 期 1, 页码 139-147出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2014.11.011
关键词
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资金
- NIH [P30 CA030199, R01-GM09040, R01 CA163743, R01 EB005011, R01 HL11630703]
- Foundation for Polish Science
- Polish Ministry of Science and Higher Education for the Faculty of Chemistry at Wroclaw University of Technology
The human paracaspase mucosa-associated lymphoid tissue lymphoma translocation protein 1 (MALT1) plays a central role in nuclear factor-kappa B (NF-kappa B) signaling as both a protease and scaffolding protein. Knocking out MALT1 leads to impaired NF-kappa B signaling and failure to mount an effective immune response. However, it is unclear to which degree it is the scaffolding function versus the proteolytic activity of MALT1 that is essential. Previous work involving a MALT1 inhibitor with low selectivity suggests that the enzymatic function plays an important role in different cell lines. To help elucidate this proteolytic role of MALT1, we have designed activity-based probes that inhibit its proteolytic activity. The probes selectively label active enzyme and can be used to inhibit MALT1 and trace its activity profile, helping to create a better picture of the significance of the proteolytic function of MALT1.
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