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Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
Published on: July 1, 2014
Quantifying proteomes and their post-translational modifications by stable isotope label-based mass spectrometry
Anna E Merrill1, Joshua J Coon
1Department of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, WI 53706, United States; Genome Center of Wisconsin, University of Wisconsin, 425 Henry Mall, Madison, WI 53706, United States.
Current Opinion in Chemical Biology
|July 10, 2013
Summary
Stable isotope labeling with mass spectrometry enhances protein expression studies. This quantitative proteomics approach reveals biological interactions and aids in building signaling networks for translational science.
Area of Science:
- Proteomics and Mass Spectrometry
- Systems Biology
- Translational Science
Background:
- Stable isotope labeling is a powerful technique in proteomics.
- Label incorporation can be metabolic or chemical, each with unique advantages and limitations.
Purpose of the Study:
- To review the applications of stable isotope labeling in quantitative proteomics.
- To highlight the extension of these methods to post-translational modifications and tissue analysis.
Main Methods:
- Stable isotope labeling (metabolic and chemical).
- Mass spectrometry for quantitative analysis.
- Integration of multiple data types.
Main Results:
- Quantitative proteomics enables identification of protein interactions with nucleic acids and metabolites.
- Label-based methods applied to phosphoproteins allow construction of signaling networks.
- Tissue quantification methods show potential in translational research.
Conclusions:
- Stable isotope labeling coupled with mass spectrometry is revolutionizing protein expression studies.
- The integration of diverse data types provides systems-level biological insights.
- Quantitative mass spectrometry is emerging as a key tool in translational science.
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