Proteomic analysis of post-translational modifications

被引：1570

作者：

Mann, M

Jensen, ON

机构：

[1] Univ So Denmark, CEBI, Dept Biochem & Mol Biol, DK-5230 Odense M, Denmark

[2] Univ So Denmark, Prot Res Grp, Dept Biochem & Mol Biol, DK-5230 Odense M, Denmark

来源：

NATURE BIOTECHNOLOGY | 2003年 / 21卷 / 03期

关键词：

D O I：

10.1038/nbt0303-255

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Post-translational modifications modulate the activity of most eukaryote proteins. Analysis of these modifications presents formidable challenges but their determination generates indispensable insight into biological function. Strategies developed to characterize individual proteins are now systematically applied to protein populations. The combination of function- or structure-based purification of modified 'subproteomes', such as phosphorylated proteins or modified membrane proteins, with mass spectrometry is proving particularly successful. To map modification sites in molecular detail, novel mass spectrometric peptide sequencing and analysis technologies hold tremendous potential. Finally, stable isotope labeling strategies in combination with mass spectrometry have been applied successfully to study the dynamics of modifications.

引用

页码：255 / 261

页数：7

共 69 条

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