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Mass spectrometry-based proteomics

Abstract

Recent successes illustrate the role of mass spectrometry-based proteomics as an indispensable tool for molecular and cellular biology and for the emerging field of systems biology. These include the study of protein–protein interactions via affinity-based isolations on a small and proteome-wide scale, the mapping of numerous organelles, the concurrent description of the malaria parasite genome and proteome, and the generation of quantitative protein profiles from diverse species. The ability of mass spectrometry to identify and, increasingly, to precisely quantify thousands of proteins from complex samples can be expected to impact broadly on biology and medicine.

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Figure 1: Generic mass spectrometry (MS)-based proteomics experiment.
Figure 2: Mass spectrometers used in proteome research.
Figure 3: Schematic representation of methods for stable-isotope protein labelling for quantitative proteomics.
Figure 4: Organellar proteomics by combined mass spectrometry (MS) and imaging methods.
Figure 5: Schematic representation of the systems biology paradigm.

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Acknowledgements

We thank members of the Institute of Systems Biology (ISB) and the Center for Experimental BioInformatics (CEBI) for critical reading of the manuscript, preparation of figures and fruitful discussions, especially L. Foster, S.-E. Ong, J. Andersen and L. Feltz. CEBI is supported by a grant from the Danish Natural Research Foundation. R.A. is supported by grants from the National Institute of Health and Oxford GlycoSciences, and a contract from the National Heart, Lung, and Blood Institute, National Institutes of Health. The ISB is supported in part by a gift from Merck and Co.

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Aebersold, R., Mann, M. Mass spectrometry-based proteomics. Nature 422, 198–207 (2003). https://doi.org/10.1038/nature01511

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