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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Hauptverfasser: Hughes, Christopher (VerfasserIn) , Krijgsveld, Jeroen (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 27 October 2012
In: Trends in biotechnology
Year: 2012, Jahrgang: 30, Heft: 12, Pages: 668-676
ISSN:1879-3096
DOI:10.1016/j.tibtech.2012.09.007
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1016/j.tibtech.2012.09.007
Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S016777991200162X
Volltext
Verfasserangaben:Christopher Hughes, Jeroen Krijgsveld
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 02.10.2018
Beschreibung:Online Resource
ISSN:1879-3096
DOI:10.1016/j.tibtech.2012.09.007