Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 11, Issue 12, Pages 1551-1565Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.O112.022186
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Funding
- Biotechnology and Biological Sciences Research Council [BB/G009112/1]
- Natural Environment Research Council [NE/I013008/1]
- Biotechnology and Biological Sciences Research Council [BB/G009112/1] Funding Source: researchfish
- Natural Environment Research Council [NE/I013008/1] Funding Source: researchfish
- BBSRC [BB/G009112/1] Funding Source: UKRI
- NERC [NE/I013008/1] Funding Source: UKRI
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Although bulk protein turnover has been measured with the use of stable isotope labeled tracers for over half a century, it is only recently that the same approach has become applicable to the level of the proteome, permitting analysis of the turnover of many proteins instead of single proteins or an aggregated protein pool. The optimal experimental design for turnover studies is dependent on the nature of the biological system under study, which dictates the choice of precursor label, protein pool sampling strategy, and treatment of data. In this review we discuss different approaches and, in particular, explore how complexity in experimental design and data processing increases as we shift from unicellular to multicellular systems, in particular animals. Molecular & Cellular Proteomics 11: 10.1074/mcp.O112.022186, 1551-1565, 2012.
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