title: Synthetic approaches to protein phosphorylation.
abstract: Reversible protein phosphorylation is critically important in biology and medicine. Hundreds of thousands of sites of protein phosphorylation have been discovered but our understanding of the functions of the vast majority of these post-translational modifications is lacking. This review describes several chemical and biochemical methods that are under development and in current use to install phospho-amino acids and their mimics site-specifically into proteins. The relative merits of total chemical synthesis, semisynthesis, and nonsense suppression strategies for studying protein phosphorylation are discussed in terms of technical simplicity, scope, and versatility.
authors.affiliation: Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, MD 21205, United States.
authors.forename: Zan
authors.initials: Z
authors.lastname: Chen
authors.affiliation: Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, MD 21205, United States. Electronic address: pcole@jhmi.edu.
authors.forename: Philip A
authors.initials: PA
authors.lastname: Cole
mesh_terms: D000818:Animals; D006801:Humans; D016297:Mutagenesis, Site-Directed / Q000379:methods; D010750:Phosphoproteins / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics* / Q000493:pharmacokinetics; D010766:Phosphorylation; D021381:Protein Transport; D011994:Recombinant Proteins / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics / Q000493:pharmacokinetics
chemical_list: D010750:Phosphoproteins; D011994:Recombinant Proteins