title: [Ananlysis of phosphoproteins and signalling pathways by quantitative proteomics].
abstract: Protein phosphorylation is a key regulator in cellular signaling pathways. It is involved in most cellular events in which interplay between phosphatases and kinases strictly controls bio-logical processes, such as differentiation, proliferation and apoptosis. Altered or defective signaling pathways often result in various diseases, emphasizing the importance of studying the phosphoproteome. The abundance of phosphoproteins in the proteome is often very low, which requires specific and highly sensitive approaches. By using quantitative proteomics methods, we are able to analyze changes in abundance of proteins and their posttranslational modifications and then changes in signaling pathways. In this review, we describe quantitative proteomics methods, which could be used for study of phosphoproteins and their connection in signaling pathways.
authors.forename: M
authors.initials: M
authors.lastname: Pjechová
authors.forename: L
authors.initials: L
authors.lastname: Hernychova
authors.forename: P
authors.initials: P
authors.lastname: Tomašec
authors.forename: G W
authors.initials: GW
authors.lastname: Wilkinson
authors.forename: B
authors.initials: B
authors.lastname: Vojtěšek
mesh_terms: D006801:Humans; D010750:Phosphoproteins / Q000032:analysis* / Q000378:metabolism; D010766:Phosphorylation; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction / Q000502:physiology
chemical_list: D010750:Phosphoproteins