Connecting 'multi-omics' approaches to endogenous protein complexes

被引：6
作者：
Wu, Di [1 ]
Robinson, Carol V. [1 ]
机构：
[1] Univ Oxford, Dept Chem, Oxford OX1 3QZ, England
来源：
TRENDS IN CHEMISTRY | 2021年 / 3卷 / 06期
基金：
英国医学研究理事会; 欧洲研究理事会; 英国惠康基金;
关键词：
MASS-SPECTROMETRY; V-ATPASE; PHOSPHORYLATION; COMPLEMENT; RESOLUTION; PROTEOFORM; ACTIVATION; DYNAMICS;
D O I：
10.1016/j.trechm.2021.03.007
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Recent progress in mass spectrometry and 'omics' technologies enable links to be made between the incorporation of proteoforms and their impact upon the structure, function, and cellular location of multiprotein assemblies. We focus this review on two of the most prevalent modifications, namely phosphorylation and glycosylation, and relate these to the properties of protein complexes. In so doing, we highlight how native mass spectrometry serves as a hub to connect 'omics' approaches to endogenous protein complexes, thus aiding our understanding of the origin, regulation, and control of multiprotein assemblies.
引用
收藏
页码：445 / 455
页数：11
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