Suppr超能文献

HMGA1与雌激素受体之间的功能相互作用需要受体的N端或C端结构域。

The functional interaction between HMGA1 and the estrogen receptor requires either the N- or the C-terminal domain of the receptor.

作者信息

Massaad-Massade Liliane, Tacine Rachida, Dulauroy Sophie, Reeves Raymond, Barouki Robert

机构信息

Université René Descartes, Laboratoire de Toxicologie Moléculaire, U-490 INSERM, 45 rue des Saints-Pères, 75270 Paris Cedex, France.

出版信息

FEBS Lett. 2004 Feb 13;559(1-3):89-95. doi: 10.1016/S0014-5793(04)00032-8.

Abstract

We have previously shown that HMGA1 enhances the transcriptional activity of promoters containing the estrogen response element (ERE) and increases binding of the estrogen receptor (ER) to ERE. Herein, we have assessed the transcriptional activity and ERE-binding ability of deleted ER fragments in absence or in presence of HMGA1. The HMGA1 protein stimulated binding and transcriptional activity by a factor of about 2-fold compared to the wild-type ER and both the N- and C-terminal ER deleted domains, but had no effect when both domains were deleted. These data show that HMGA1 cooperates with either the N- or the C-terminal transcriptional activation domain of the ER.

摘要

我们之前已经表明,HMGA1增强了含有雌激素反应元件(ERE)的启动子的转录活性,并增加了雌激素受体(ER)与ERE的结合。在此,我们评估了在不存在或存在HMGA1的情况下缺失的ER片段的转录活性和ERE结合能力。与野生型ER以及N端和C端ER缺失结构域相比,HMGA1蛋白刺激结合和转录活性的倍数约为2倍,但当两个结构域都缺失时则没有影响。这些数据表明,HMGA1与ER的N端或C端转录激活结构域协同作用。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验