title: Modificomics: posttranslational modifications beyond protein phosphorylation and glycosylation.
abstract: Posttranslational modifications of proteins possess key functions in the regulation of various cellular processes. While they facilitate fast, location-specific and transient reactions to changing conditions in the first place they enhance the already high complexity of a cellular proteome by orders of magnitude. Furthermore, they can utterly alter the properties of the modified protein, thus making a timely analysis even more difficult. While several standardized methods for the analysis of protein phosphorylation and glycosylation have been established most other modifications require tailor-made solutions for a comprehensive analysis. Therefore, we will provide guidelines for the analysis of some important posttranslational modifications that are underrepresented in contemporary literature.
authors.affiliation: University of Wuerzburg, Proteomics Group, Pharmaceutical Biology, Julius-von-Sachs-Institute for Biosciences, Julius-von-Sachs-Platz 2, 97082 Wuerzburg, Germany.
authors.forename: Joerg
authors.initials: J
authors.lastname: Reinders
authors.forename: Albert
authors.initials: A
authors.lastname: Sickmann
mesh_terms: D006031:Glycosylation; D008954:Models, Biological; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D020543:Proteome / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D020543:Proteome