Mass-spectrometric exploration of proteome structure and function

被引:1605
作者
Aebersold, Ruedi [1 ,2 ]
Mann, Matthias [3 ,4 ]
机构
[1] Swiss Fed Inst Technol, Inst Mol Syst Biol, Dept Biol, CH-8093 Zurich, Switzerland
[2] Univ Zurich, Fac Sci, CH-8093 Zurich, Switzerland
[3] Max Planck Inst Biochem, Dept Prote & Signal Transduct, D-82152 Martinsried, Germany
[4] Univ Copenhagen, Fac Hlth & Med Sci, Novo Nordisk Fdn Ctr Prot Res, DK-2200 Copenhagen, Denmark
关键词
CHEMICAL CROSS-LINKING; PHOSPHOPROTEOME REVEALS; QUANTITATIVE-ANALYSIS; LYSINE ACETYLATION; HIGH-RESOLUTION; LIVING CELLS; COPY-NUMBER; DRAFT MAP; IN-VIVO; PEPTIDE;
D O I
10.1038/nature19949
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
070301 [无机化学]; 070403 [天体物理学]; 070507 [自然资源与国土空间规划学]; 090105 [作物生产系统与生态工程];
摘要
Numerous biological processes are concurrently and coordinately active in every living cell. Each of them encompasses synthetic, catalytic and regulatory functions that are, almost always, carried out by proteins organized further into higher-order structures and networks. For decades, the structures and functions of selected proteins have been studied using biochemical and biophysical methods. However, the properties and behaviour of the proteome as an integrated system have largely remained elusive. Powerful mass-spectrometry-based technologies now provide unprecedented insights into the composition, structure, function and control of the proteome, shedding light on complex biological processes and phenotypes.
引用
收藏
页码:347 / 355
页数:9
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