title: Chemical methods for the proteome-wide identification of posttranslationally modified proteins.
abstract: Thousands of proteins are subjected to posttranslational modifications that can have dramatic effects on their functions. Traditional biological methods have struggled to address some of the challenges inherit in the unbiased identification of certain posttranslational modifications. As with many areas of biological discovery, the development of chemoselective and bioorthogonal reactions and chemical probes has transformed our ability to selectively label and enrich a wide variety of posttranslational modifications. Collectively, these efforts are making significant contributions to the goal of mapping the protein modification landscape.
authors.affiliation: Department of Chemistry, University of Southern California, Los Angeles, CA 90089-0744, United States.
authors.forename: Kelly N
authors.initials: KN
authors.lastname: Chuh
authors.affiliation: Department of Chemistry, University of Southern California, Los Angeles, CA 90089-0744, United States; Department of Molecular and Computational Biology, University of Southern California, Los Angeles, CA 90089-0744, United States. Electronic address: matthew.pratt@usc.edu.
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Pratt
mesh_terms: D000107:Acetylation; D000246:Adenosine Diphosphate Ribose / Q000032:analysis / Q000378:metabolism; D000818:Animals; D006031:Glycosylation; D006801:Humans; D008055:Lipids / Q000032:analysis; D008745:Methylation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D020543:Proteome / Q000737:chemistry / Q000378:metabolism; D040901:Proteomics / Q000379:methods*
chemical_list: D008055:Lipids; D011506:Proteins; D020543:Proteome; D000246:Adenosine Diphosphate Ribose