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Proteomic dissection of biological pathways/processes through profiling protein-protein interaction networks

Proteomic dissection of biological pathways/processes through profiling protein-protein interaction networks

作     者:CHEN Xian Institutes for Biomedical Sciences, Fudan University, Shanghai 200433, China Department of Biochemistry & Biophysics, School of Medicine, University of North Carolina-Chapel Hill, USA 

作者机构:Institutes for Biomedical Sciences Fudan University Shanghai China Department of Biochemistry & Biophysics School of Medicine University of North Carolina-Chapel Hill Chapel Hill USA 

出 版 物:《Science China Chemistry》 (中国科学(化学英文版))

年 卷 期:2010年第53卷第4期

页      面:737-746页

核心收录:

学科分类:0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 0703[理学-化学] 

基  金:support from the Shanghai Science and Technology Development Program (Grant Nos. 03DZ14024 & 07ZR14010) the 863 High Technology Foundation of China (Grant No. 2006AA02A310) US NIH 1R01AI064806-01A2, 5R21DK082706 U.S. Department of Energy, the Office of Science (BER) (Grant No. DE-FG02- 07ER64422) 

主  题:Chen Proteomic dissection of biological pathways/processes through profiling protein-protein interaction networks 

摘      要:Cellular functions, either under the normal or pathological conditions or under different stresses, are the results of the coordinated action of multiple proteins interacting in macromolecular complexes or assemblies. The precise determination of the specific composition of protein complexes, especially using scalable and high-throughput methods, represents a systematic approach toward revealing particular cellular biological functions. In this regard, the direct profiling protein-protein interactions (PPIs) represent an efficient way to dissect functional pathways for revealing novel protein functions. In this review, we illustrate the technological evolution for the large-scale and precise identification of PPIs toward higher physiologically relevant accuracy. These techniques aim at improving the efficiency of complex pull-down, the signal specificity and accuracy in distinguishing specific PPIs, and the accuracy of identifying physiological relevant PPIs. A newly developed streamline proteomic approach for mapping the binary relationship of PPIs in a protein complex is introduced.

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