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首页> 外文期刊>Proteomics >A large set of estrogen receptor beta-interacting proteins identified by tandem affinity purification in hormone-responsive human breast cancer cell nuclei.
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A large set of estrogen receptor beta-interacting proteins identified by tandem affinity purification in hormone-responsive human breast cancer cell nuclei.

机译:通过串联亲和纯化在激素反应性人乳腺癌细胞核中鉴定出大量的雌激素受体β相互作用蛋白。

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摘要

Estrogen receptors alpha (ER-alpha) and beta (ER-beta) play distinct biological roles in onset and progression of hormone-responsive breast cancer, with ER-beta exerting a modulatory activity on ER-alpha-mediated estrogen signaling and stimulation of cell proliferation by mechanisms still not fully understood. We stably expressed human ER-beta fused to a tandem affinity purification-tag in estrogen-responsive MCF-7 cells and applied tandem affinity purification and nanoLC-MS/MS to identify the ER-beta interactome of this cell type. Functional annotation by bioinformatics analyses of the 303 proteins that co-purify with ER-beta from nuclear extracts identify several new molecular partners of this receptor subtype that represents nodal points of a large protein network controlling multiple processes and functions in breast cancer cells.
机译:雌激素受体α(ER-alpha)和β(ER-beta)在激素反应性乳腺癌的发生和发展中起着独特的生物学作用,其中ER-beta对ER-alpha介导的雌激素信号传导和细胞刺激具有调节作用扩散机制尚不完全清楚。我们在雌激素反应性MCF-7细胞中稳定表达与串联亲和纯化标签融合的人ER-β,并应用串联亲和纯化和nanoLC-MS / MS来鉴定这种细胞类型的ER-β相互作用组。通过生物信息学分析,对从核提取物中与ER-β共纯化的303种蛋白质进行功能注释,鉴定出该受体亚型的几个新分子伴侣,它们代表控制乳腺癌细胞中多个过程和功能的大型蛋白质网络的节点。

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