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- W2017482875 abstract "Heat shock proteins (HSPs) are known to protect cells from heat, oxidative stress, and the cytotoxic effects of drugs, and thus can enhance cancer cell survival. As a result, HSPs are a newly emerging class of protein targets for chemotherapy. Among the various HSPs, the HSP70 family is the most highly conserved and prevalent. Herein we describe the development of a β-alanine rich linear polyamide that binds the GGA heat shock elements (HSEs) 3 and 4 in the HSP70 promoter in an unusual 1:1 mode and inhibits heat shock transcription factor 1 (HSF1) binding in vitro." @default.
- W2017482875 created "2016-06-24" @default.
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- W2017482875 date "2011-12-01" @default.
- W2017482875 modified "2023-09-25" @default.
- W2017482875 title "Inhibition of Heat Shock Transcription Factor Binding by a Linear Polyamide Binding in an Unusual 1:1 Mode" @default.
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- W2017482875 doi "https://doi.org/10.1002/cbic.201100524" @default.
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