Mapping protein post-translational modifications with mass spectrometry

被引：601

作者：

Witze, Eric S.

Old, William M.

Resing, Katheryn A.

Ahn, Natalie G.

机构：

[1] Univ Colorado, Dept Chem & Biochem, Boulder, CO 80309 USA

[2] Univ Colorado, Howard Hughes Med Inst, Boulder, CO 80309 USA

来源：

NATURE METHODS | 2007年 / 4卷 / 10期

关键词：

D O I：

10.1038/nmeth1100

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Post-translational modifications of proteins control many biological processes, and examining their diversity is critical for understanding mechanisms of cell regulation. Mass spectrometry is a fundamental tool for detecting and mapping covalent modifications and quantifying their changes. Modern approaches have made large-scale experiments possible, screening complex mixtures of proteins for alterations in chemical modifications. By profiling protein chemistries, biologists can gain deeper insight into biological control. The aim of this review is introduce biologists to current strategies in mass spectrometry based proteomics that are used to characterize protein post-translational modifications, noting strengths and shortcomings of various approaches.

引用

收藏

页码：798 / 806

页数：9

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