蛋白酵素
细胞凋亡
酶
劈理(地质)
细胞生物学
蛋白质水解
生物
生物化学
化学
古生物学
断裂(地质)
作者
Nancy J. Bump,Maria Hackett,Margaret Hugunin,Somasekar Seshagiri,Kenneth D. Brady,Patrick Chen,Catherine R. Ferenz,Simon Franklin,Tariq Ghayur,Ping Li,Peter Licari,John A. Mankovich,Lianfa Shi,Arnold H. Greenberg,Lois K. Miller,Winnie W. Wong
出处
期刊:Science
[American Association for the Advancement of Science]
日期:1995-09-29
卷期号:269 (5232): 1885-1888
被引量:646
标识
DOI:10.1126/science.7569933
摘要
The baculovirus antiapoptotic protein p35 inhibited the proteolytic activity of human interleukin-1β converting enzyme (ICE) and three of its homologs in enzymatic assays. Coexpression of p35 prevented the autoproteolytic activation of ICE from its precursor form and blocked ICE-induced apoptosis. Inhibition of enzymatic activity correlated with the cleavage of p35 and the formation of a stable ICE-p35 complex. The ability of p35 to block apoptosis in different pathways and in distantly related organisms suggests a central and conserved role for ICE-like proteases in the induction of apoptosis.
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