title: The characterization of protein post-translational modifications by mass spectrometry.
abstract: Most biological processes are regulated by post-translational modifications of proteins, and conditions that disrupt the regulation of such events can lead to disease. In the past decade, the identification and characterization of covalent modifications have been driven by advances in mass spectrometry. Here, we discuss current mass spectrometric and proteomic approaches for the identification of proteins and their covalent modifications, and we highlight high-throughput strategies for comprehensive analysis of cell proteomes.
authors.affiliation: Department of Chemistry and Biochemistry and Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado 80309, USA.
authors.forename: Rebecca E
authors.initials: RE
authors.lastname: Schweppe
authors.forename: Claire E
authors.initials: CE
authors.lastname: Haydon
authors.forename: Timothy S
authors.initials: TS
authors.lastname: Lewis
authors.forename: Katheryn A
authors.initials: KA
authors.lastname: Resing
authors.forename: Natalie G
authors.initials: NG
authors.lastname: Ahn
mesh_terms: D000595:Amino Acid Sequence; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D020539:Sequence Analysis, Protein / Q000379:methods
chemical_list: D011506:Proteins