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• W1980042348 abstract "Antisense activity against erbB-2 of a variety of sulfur-modified oligonucleotides was examined in a breast cancer cell line which overexpresses this oncogene. Using a 15 base anti-erbB-2 sequence previously shown to be effective, various backbone configurations containing phosphoromonothioate or phosphorodithioate linkages were evaluated for antisense activity by a two-color flow cytometric assay. This sequence was effective in inhibiting the production of erbB-2 protein when it was configured as a monothioate at each linkage and as an alternating dithioate/phosphodiester. Both of these compounds were also able to specifically inhibit erbB-2 mRNA expression, indicative of RNase H-mediated activity. The same sequence protected by either three dithioate or three monothioate linkages at each end was ineffective as an antisense reagent, suggesting that endonuclease activity is a significant determinant of the stability of oligonucleotides. Finally, the erbB-2 sequence target was shifted in an effort to improve antisense activity. A new lead sequence was identified that was significantly more effective in inhibiting erbB-2 protein levels and retained activity at lower concentrations." @default.
• W1980042348 created "2016-06-24" @default.
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• W1980042348 date "1996-11-01" @default.
• W1980042348 modified "2023-09-26" @default.
• W1980042348 title "Inhibition of the erbB-2 Tyrosine Kinase Receptor in Breast Cancer Cells by Phosphoromonothioate and Phosphorodithioate Antisense Oligonucleotides" @default.
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• W1980042348 doi "https://doi.org/10.1093/nar/24.22.4558" @default.
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