Literature DB >> 20807952

Focus issue: systems analysis of protein phosphorylation.

Nancy R Gough, John F Foley.   

Abstract

Kinases and phosphatases are key regulatory molecules that participate in most cell signaling pathways. Systems-level analyses are providing new insights into phosphorylation sites and kinase specificity, and phosphoproteomic analyses are creating not just a wealth of data, but are also revealing rich revelations about cellular behavior, cellular responses to changing environmental conditions, and mechanisms of disease. Phosphatases are not merely signal terminators, but play active roles in signal transduction and are especially important in redox signaling. In this Focus Issue, Science Signaling highlights protein phosphorylation as the center of the signaling universe.

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Year:  2010        PMID: 20807952     DOI: 10.1126/scisignal.3137eg6

Source DB:  PubMed          Journal:  Sci Signal        ISSN: 1945-0877            Impact factor:   8.192


  4 in total

1.  Tandem phosphorylation within an intrinsically disordered region regulates ACTN4 function.

Authors:  Timothy Travers; Hanshuang Shao; Brian A Joughin; Douglas A Lauffenburger; Alan Wells; Carlos J Camacho
Journal:  Sci Signal       Date:  2015-05-26       Impact factor: 8.192

2.  Human 14-3-3 paralogs differences uncovered by cross-talk of phosphorylation and lysine acetylation.

Authors:  Marina Uhart; Diego M Bustos
Journal:  PLoS One       Date:  2013-02-13       Impact factor: 3.240

3.  The human phosphotyrosine signaling network: evolution and hotspots of hijacking in cancer.

Authors:  Lei Li; Chabane Tibiche; Cong Fu; Tomonori Kaneko; Michael F Moran; Martin R Schiller; Shawn Shun-Cheng Li; Edwin Wang
Journal:  Genome Res       Date:  2011-12-22       Impact factor: 9.043

Review 4.  Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins.

Authors:  Marina Uhart; Diego M Bustos
Journal:  Front Genet       Date:  2014-02-03       Impact factor: 4.599

  4 in total

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