Mass Spectrometry-Based Analysis of Time-Resolved Proteome Quantification

被引:2
|
作者
Valdes, Alberto [1 ]
Bergstroem Lind, Sara [2 ]
机构
[1] Univ Alcala De Henares, Dept Analyt Chem Phys Chem & Chem Engn, Ctra Madrid Barcelona,Km 33-600, Madrid 28871, Spain
[2] Uppsala Univ, Dept Chem BMC, Analyt Chem, Box 599, S-75124 Uppsala, Sweden
基金
奥地利科学基金会; 瑞典研究理事会;
关键词
comparative proteomics; interactomics; mass spectrometry-LC-MS; MS; posttranslational modification analysis; protein dynamics; time-resolved proteomics; TYROSINE PHOSPHORYLATION SITES; IN-VIVO; MOUSE MODEL; PHOSPHOPROTEOMIC ANALYSIS; BIOMARKER DISCOVERY; SIGNALING PATHWAY; NUCLEAR PROTEOME; PLASMA PROTEOME; CELL-CULTURE; AMINO-ACIDS;
D O I
10.1002/pmic.201800425
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The aspect of time is essential in biological processes and thus it is important to be able to monitor signaling molecules through time. Proteins are key players in cellular signaling and they respond to many stimuli and change their expression in many time-dependent processes. Mass spectrometry (MS) is an important tool for studying proteins, including their posttranslational modifications and their interaction partners-both in qualitative and quantitative ways. In order to distinguish the different trends over time, proteins, modification sites, and interacting proteins must be compared between different time points, and therefore relative quantification is preferred. In this review, the progress and challenges for MS-based analysis of time-resolved proteome dynamics are discussed. Further, aspects on model systems, technologies, sampling frequencies, and presentation of the dynamic data are discussed.
引用
收藏
页数:11
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