期刊
SCIENCE
卷 305, 期 5689, 页码 1471-1474出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1098231
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资金
- NCI NIH HHS [P01 CA95471] Funding Source: Medline
We describe the synthesis and properties of a small molecule mimic of Smac, a pro-apoptotic protein that functions by relieving inhibitor-of-apoptosis protein (IAP)-mediated suppression of caspase activity. The compound binds to X chromosome-encoded IAP (XIAP), cellular IAP 1 (clAP-1), and cellular IAP 2 (clAP-2) and synergizes with both tumor necrosis factor alpha (TNFalpha.) and TNF-related apoptosis-inducing ligand (TRAIL) to potently induce caspase activation and apoptosis in human cancer cells. The molecule has allowed a temporal, unbiased evaluation of the roles that IAP proteins play during signaling from TRAIL and TNF receptors. The compound is also a lead structure for the development of IAP antagonists potentially useful as therapy for cancer and inflammatory diseases.
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