title: Quantifying proteomes and their post-translational modifications by stable isotope label-based mass spectrometry.
abstract: Stable isotope labeling coupled with mass spectrometry has revolutionized the scope and impact of protein expression studies. Label incorporation can occur metabolically or chemically, and each method bears specific strengths and weaknesses. Quantitative proteomics confidently identifies specific interactions between proteins and other biological species, such as nucleic acids and metabolites. Extending label-based methods to phosphorylation-modified forms of proteins enables the construction of signaling networks and their temporal responses to stimuli. The integration of multiple data types offers systems-level insight on coordinated biological processes. Finally, the development of methods applicable to tissue quantification suggests the emerging role of label-based, quantitative mass spectrometry in translational science.
authors.affiliation: Department 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.
authors.forename: Anna E
authors.initials: AE
authors.lastname: Merrill
authors.forename: Joshua J
authors.initials: JJ
authors.lastname: Coon
mesh_terms: D000818:Animals; D006801:Humans; D007553:Isotope Labeling; D013058:Mass Spectrometry / Q000379:methods*; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*
chemical_list: D020543:Proteome