Protein Phosphorylation in Health and Disease

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...

Full description

Main Author: Allegra Via
Other Authors: Andreas Zanzoni
Format: eBook
Published: Frontiers Media SA 2016
Subjects:
Online Access:
Collection: Directory of Open Access Books - Collection details see MPG.ReNa
LEADER 03409nmm a2200433 u 4500
001 EB001491047
003 EBX01000000000000000920636
005 00000000000000.0
007 cr|||||||||||||||||||||
008 170612 |||
020 |a 9782889199006 
100 1 |a Allegra Via 
245 0 0 |a Protein Phosphorylation in Health and Disease  |h Elektronische Ressource 
260 |b Frontiers Media SA  |c 2016 
300 |a 1 electronic resource (122 p.) 
653 |a network biology 
653 |a Science (General) 
653 |a Genetics 
653 |a Protein phosphorylation 
653 |a Phosphatases 
653 |a bioinformatics 
653 |a Systems Biology 
653 |a Human Disease 
653 |a evolution 
653 |a kinases 
653 |a protein structure 
700 1 |a Andreas Zanzoni 
989 |b DOAB  |a Directory of Open Access Books 
856 |u http://www.doabooks.org/doab?func=fulltext&rid=18287  |z Description of rights in Directory of Open Access Books (DOAB): Attribution (CC by) 
856 |u http://journal.frontiersin.org/researchtopic/1984/protein-phosphorylation-in-health-and-disease 
082 0 |a 500 
082 0 |a 140 
082 0 |a 610 
082 0 |a 576 
520 |a 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.  
520 |a Protein 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.  
520 |a 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