LEADER 03304nam 2200409z- 450 001 9910220055803321 005 20231214132942.0 035 $a(CKB)3800000000216220 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/57243 035 $a(EXLCZ)993800000000216220 100 $a20202102d2016 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aProtein Phosphorylation in Health and Disease 210 $cFrontiers Media SA$d2016 215 $a1 electronic resource (122 p.) 225 1 $aFrontiers Research Topics 311 $a2-88919-900-2 330 $aProtein phosphorylation is one of the most abundant reversible post-translational modifications in eukaryotes. It is involved in virtually all cellular processes by regulating protein function, localization and stability and by mediating protein-protein interactions. Furthermore, aberrant protein phosphorylation is implicated in the onset and progression of human diseases such as cancer and neurodegenerative disorders. In the last years, tens of thousands of in vivo phosphorylation events have been identified by large-scale quantitative phospho-proteomics experiment suggesting that a large fraction of the proteome might be regulated by phosphorylation. This data explosion is increasingly enabling the development of computational approaches, often combined with experimental validation, aiming at prioritizing phosphosites and assessing their functional relevance. Some computational approaches also address the inference of specificity determinants of protein kinases/phosphatases and the identification of phosphoresidue recognition domains. In this context, several challenging issues are still open regarding phosphorylation, including a better understanding of the interplay between phosphorylation and allosteric regulation, agents and mechanisms disrupting or promoting abnormal phosphorylation in diseases, the identification and modulation of novel phosphorylation inhibitors, and so forth. Furthermore, the determinants of kinase and phosphatase recognition and binding specificity are still unknown in several cases, as well as the impact of disease mutations on phosphorylation-mediated signaling. The articles included in this Research Topic illustrate the very diverse aspects of phosphorylation, ranging from structural changes induced by phosphorylation to the peculiarities of phosphosite evolution. Some also provide a glimpse into the huge complexity of phosphorylation networks and pathways in health and disease, and underscore that a deeper knowledge of such processes is essential to identify disease biomarkers, on one hand, and design more effective therapeutic strategies, on the other. 610 $aprotein structure 610 $akinases 610 $aPhosphatases 610 $abioinformatics 610 $aevolution 610 $aProtein phosphorylation 610 $anetwork biology 610 $aSystems Biology 610 $aHuman Disease 700 $aAllegra Via$4auth$01328842 702 $aAndreas Zanzoni$4auth 906 $aBOOK 912 $a9910220055803321 996 $aProtein Phosphorylation in Health and Disease$93039020 997 $aUNINA