By Bruce C Baguley; David J Kerr
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Extra info for Anticancer drug development
1999). A number of antisense approaches have also been used to implicate c-Src as an important facilitator of tumor cell proliferation in vitro and in vivo. , 1999). B. c-Src Interactions with Proliferative and Survival Signaling Pathways The mechanism by which c-Src influences tumor cell proliferation has been the subject of intense study. Although only limited evidence exists for the direct, single-agent, causative participation of overexpressed or overactive c-Src kinase in transforming events, many data support the participation of this kinase with other oncogenic signaling proteins and pathways (Fig.
And Prives, C. (2000). The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites. Genes Dev. 14, 289–300. 30 POMMIER, YU, AND KOHN Shieh, S. , and Prives, C. (1997). DNA damageinduced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91, 325–334. , and Terakawa, N. (2000). Mechanism of the combination effect of wild-type TP53 gene transfection and cisplatin treatment for ovarian cancer xenografts. Eur. J. Cancer 36, 1869–1875.
Cancer Res. 55, 3250–3253. , and Pommier, Y. (1999). Apoptotic response to camptothecin and 7-hydroxystaurosporine (UCN-01) in the eight human breast cancer cell lines of the NCI anticancer drug screen: multifactorial relationship with topoisomerase I, protein kinase C, bcl-2 and caspase pathways. Int. J. Cancer 82, 396–404. , and Hoffmann, I. (2000). Cell cycle regulation by the Cdc25 phosphatase family. Prog. Cell. Cycle Res. 4, 107–114. Noble, M. E. and Endicott, J. A. (1999). Chemical inhibitors of cyclindependent kinases: Insights into design from X-ray crystallographic studies.
Anticancer drug development by Bruce C Baguley; David J Kerr