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- W1966793808 abstract "We previously demonstrated that testicular zinc-finger protein (TZF) was a corepressor of the androgen receptor (AR). In the present study, we further showed that TZF-L, an alternative spliced variant of TZF, enhanced transactivation function of AR. Deletion analysis of TZF-L revealed that its N-terminus, which almost corresponded to that of TZF, but not its C-terminus was able to interact with AR. Additional analysis suggested that TZF and TZF-L were able to form both homodimers and heterodimers. TZF-L inhibited the homodimer formation of TZF and the intranuclear dot formation of TZF. We propose that in the unique regulation system of AR-mediated transactivation, two spliced isoforms of TZF act as coactivator and corepressor, respectively." @default.
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- W1966793808 date "2006-03-01" @default.
- W1966793808 modified "2023-09-27" @default.
- W1966793808 title "Opposite effects of alternative TZF spliced variants on androgen receptor" @default.
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- W1966793808 doi "https://doi.org/10.1016/j.bbrc.2005.12.213" @default.
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