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修饰特异性蛋白质组学:通过质谱对翻译后修饰进行表征

Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry.

作者信息

Jensen Ole Nørregaard

机构信息

Protein Research Group, Department of Biochemistry & Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark.

出版信息

Curr Opin Chem Biol. 2004 Feb;8(1):33-41. doi: 10.1016/j.cbpa.2003.12.009.

DOI:10.1016/j.cbpa.2003.12.009
PMID:15036154
Abstract

Post-translational modifications generate tremendous diversity, complexity and heterogeneity of gene products, and their determination is one of the main challenges in proteomics research. Recent developments in mass spectrometry based approaches for systematic, qualitative and quantitative determination of modified proteins promise to bring new insights on the dynamics and spatio-temporal control of protein activities by post-translational modifications, and reveal their roles in biological processes and pathogenic conditions. Combinations of affinity-based enrichment and extraction methods, multidimensional separation technologies and mass spectrometry are particularly attractive for systematic investigation of post-translationally modified proteins in proteomics.

摘要

翻译后修饰产生了基因产物的巨大多样性、复杂性和异质性,对其进行测定是蛋白质组学研究的主要挑战之一。基于质谱的方法在系统、定性和定量测定修饰蛋白方面的最新进展有望为翻译后修饰对蛋白质活性的动态变化和时空控制带来新的见解,并揭示它们在生物过程和致病条件中的作用。基于亲和的富集和提取方法、多维分离技术和质谱的组合对于蛋白质组学中翻译后修饰蛋白的系统研究特别有吸引力。

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