title: Exploring the phosphoproteome with mass spectrometry.
abstract: Protein phosphorylation is a reversible post-translational modification crucial in the control of numerous regulatory pathways. Understanding the highly interconnected nature of such networks requires new broader-scale analysis techniques. This report summarizes recent advances in the use of mass spectrometry to assess phosphorylation events in ever more complex systems.
authors.affiliation: Genomics Institute of the Novartis Research Foundation, 10675 John Jay Hopkins Drive, San Diego, CA 92121, USA. epeters@gnf.org
authors.forename: Eric C
authors.initials: EC
authors.lastname: Peters
authors.forename: Ansgar
authors.initials: A
authors.lastname: Brock
authors.forename: Scott B
authors.initials: SB
authors.lastname: Ficarro
mesh_terms: D000818:Animals; D006801:Humans; D013058:Mass Spectrometry; D010750:Phosphoproteins / Q000032:analysis*; D010766:Phosphorylation; D020543:Proteome / Q000032:analysis* / Q000737:chemistry; D015398:Signal Transduction
chemical_list: D010750:Phosphoproteins; D020543:Proteome