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首页> 外文期刊>The Journal of biological chemistry >Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.
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Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.

机译:微管相关蛋白2c(MAP2c)磷酸化和调节蛋白14-3-3ζ结合位点的定量定位揭示了MAP2c及其同系物Tau之间的关键差异。

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There was an error in Fig. 6. Panels A and B were inadvertently exchanged. The correct legend should read as follows. Microscale thermophoretic analysis of interaction between 5 μm E52C/C348S MAP2c and 14-3-3ζ in 50 mm Tris buffer. A, phosphorylated MAP2c; B, unphosphorylated MAP2c. The plots show interactions in the 14-3-3ζ monomer concentration range from 36.6 nm to 1.2 mm. The mean values ± S.D. for each concentration point were calculated from triplicate measurements.
机译:图6中有一个错误。面板A和B被无意间交换了。正确的图例应如下所示。微量热泳分析在50 mm Tris缓冲液中5μmE52C / C348S MAP2c和14-3-3ζ之间的相互作用。 A,磷酸化的MAP2c; B,未磷酸化的MAP2c。该图显示了14-3-3ζ单体浓度范围为36.6 nm至1.2 mm的相互作用。平均值±标准差从三个重复测量中计算出每个浓度点的浓度。

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