青云英语翻译

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翻译结果1翻译结果2 翻译结果3翻译结果4翻译结果5

翻译结果1复制译文编辑译文朗读译文返回顶部

这表明, ATXN1和RBM17在大的蛋白质复合物相互作用。

翻译结果2复制译文编辑译文朗读译文返回顶部

这建议 ATXN1 和 RBM17 在大蛋白质的建筑群互相影响。进到大蛋白质的建筑群的 RBM17 和 ATXN1 的结合没有在 S776 由 ATXN1 的不同的 phosphorylation 造成 ( 附助的无花果。S9 ).

翻译结果3复制译文编辑译文朗读译文返回顶部

这表明,ATXN1 和 RBM17 在大型蛋白质复合物进行交互。将 RBM17 和 ATXN1 纳入大蛋白复合体不造成的鉴别磷酸化在 S776 ATXN1 (补充图。S9)。

翻译结果4复制译文编辑译文朗读译文返回顶部

这建议ATXN1和RBM17在大蛋白质复合体互动。RBM17和ATXN1的并网到大蛋白质复合体里未由ATXN1的有差别的磷酸化造成在S776 (补充Fig. S9)。

翻译结果5复制译文编辑译文朗读译文返回顶部

这建议ATXN1和RBM17在大蛋白质复合体互动。 RBM17和ATXN1的并网到大蛋白质复合体里未由ATXN1的有差别的磷酸化造成在S776 (补充。 S9).
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aGiven that the proteins showed broadly overlapping elution profiles, we sought to establish the fractions in which ATXN1 and RBM17 interact. 假设蛋白质显示了宽广地重叠的洗提外形,我们寻求建立ATXN1和RBM17互动的分数。 [translate] 
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aWe found that ATXN1[82Q] immunoprecipitated endogenous RBM17 proteins from the large protein complexes (peak fraction 9, red box at the bottom panel), but not from the small protein complexes (peak fractions 12–13, blue box at the bottom panel). 正在翻译,请等待... [translate] 
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aThis suggests that ATXN1 and RBM17 interact in the large protein complexes. Incorporation of RBM17 and ATXN1 into large protein complexes was not caused by differential phosphorylation of ATXN1 at S776 (Supplementary Fig. S9). 这建议ATXN1和RBM17在大蛋白质复合体互动。 RBM17和ATXN1的并网到大蛋白质复合体里未由ATXN1的有差别的磷酸化造成在S776 (补充。 S9). [translate]