Proteolytic Post-translational Modification of Proteins: Proteomic Tools and Methodology

被引:110
作者
Rogers, Lindsay D. [1 ,2 ]
Overall, Christopher M. [1 ,2 ]
机构
[1] Univ British Columbia, Dept Biochem & Mol Biol, Dept Oral Biol & Med Sci, Life Sci Inst 4 401, Vancouver, BC V6T 1Z3, Canada
[2] Univ British Columbia, Ctr Blood Res, Life Sci Inst 4 401, Vancouver, BC V6T 1Z3, Canada
基金
加拿大健康研究院;
关键词
N-TERMINAL PEPTIDES; POSITIONAL PROTEOMICS; SELECTIVE ISOLATION; MASS-SPECTROMETRY; CLEAVAGE SITES; IDENTIFICATION; DATABASE; PROTEASES; REVEALS; ACETYLATION;
D O I
10.1074/mcp.M113.031310
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Proteolytic processing is a ubiquitous and irreversible post-translational modification involving limited and highly specific hydrolysis of peptide and isopeptide bonds of a protein by a protease. Cleavage generates shorter protein chains displaying neo-N and -C termini, often with new or modified biological activities. Within the past decade, degradomics and terminomics have emerged as significant proteomics subfields dedicated to characterizing proteolysis products as well as natural protein N and C termini. Here we provide an overview of contemporary proteomics-based methods, including specific quantitation, data analysis, and curation considerations, and highlight exciting new and emerging applications within these fields enabling in vivo analysis of proteolytic events. Molecular & Cellular Proteomics 12: 10.1074/ mcp.M113.031310, 3532-3542, 2013. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
引用
收藏
页码:3532 / 3542
页数:11
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