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通过高灵敏度、高分辨率傅里叶变换离子回旋共振质谱法测定蛋白质的翻译后修饰。

Determination of post-translational modifications of proteins by high-sensitivity, high-resolution Fourier transform ion cyclotron resonance mass spectrometry.

作者信息

Emmett Mark R

机构信息

National High Magnetic Field Laboratory, Florida State University, B224 Magnet Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310-3706, USA.

出版信息

J Chromatogr A. 2003 Sep 26;1013(1-2):203-13. doi: 10.1016/s0021-9673(03)01127-0.

Abstract

The response of a cell to its extracellular environment is a multi-step process beginning with signal transduction that is governed by "subtle changes" often resulting in protein expression. Proteomics is the tracking of this protein expression. Post-translational modification (PTM) is a "subtle change" that has a major influence on signal transduction. Phosphorylation and glycosylation propagate signals by sequential, reversible modifications. High-sensitivity, high-resolution and multiple MS capabilities of Fourier transform ion cyclotron resonance mass spectrometry permit localization of the PTM(s) with electron-capture dissociation, and then structural determination of the PTM with infrared multiphoton dissociation.

摘要

细胞对其细胞外环境的反应是一个多步骤过程,始于由“细微变化”控制的信号转导,这些变化通常会导致蛋白质表达。蛋白质组学就是对这种蛋白质表达的追踪。翻译后修饰(PTM)是一种对信号转导有重大影响的“细微变化”。磷酸化和糖基化通过连续的、可逆的修饰来传递信号。傅里叶变换离子回旋共振质谱的高灵敏度、高分辨率和多重质谱能力允许通过电子捕获解离对翻译后修饰进行定位,然后通过红外多光子解离对翻译后修饰进行结构测定。

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