Developments in quantitative mass spectrometry for the analysis of proteome dynamics
Two of the primary responses in a cell when perturbed are modulation of the dynamics of its constituent gene expression and protein abundance to restore steady-state homeostasis. To obtain a detailed model of the restoration of this balance, it is necessary to examine the kinetics of transcription a...
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| Main Authors: | , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
27 October 2012
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| In: |
Trends in biotechnology
Year: 2012, Volume: 30, Issue: 12, Pages: 668-676 |
| ISSN: | 1879-3096 |
| DOI: | 10.1016/j.tibtech.2012.09.007 |
| Online Access: | Verlag, Volltext: http://dx.doi.org/10.1016/j.tibtech.2012.09.007 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S016777991200162X 
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| Author Notes: | Christopher Hughes, Jeroen Krijgsveld |
| Summary: | Two of the primary responses in a cell when perturbed are modulation of the dynamics of its constituent gene expression and protein abundance to restore steady-state homeostasis. To obtain a detailed model of the restoration of this balance, it is necessary to examine the kinetics of transcription and translation, thus going beyond establishing mere abundance levels of transcripts and proteins. In this review we discuss proteomic approaches that utilize genomic tagging and metabolic labeling to reveal turnover kinetics for cellular proteins in a high-throughput manner. Novel metabolic and multiplexed labeling techniques coupled to mass spectrometry, in combination with next-generation sequencing approaches, provide tools for studying the principles of cellular adaptation and dynamics in unprecedented detail. |
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| Item Description: | Gesehen am 02.10.2018 |
| Physical Description: | Online Resource |
| ISSN: | 1879-3096 |
| DOI: | 10.1016/j.tibtech.2012.09.007 |