A Novel Phosphorylation Site-Kinase Network-Based Method for the Accurate Prediction of Kinase-Substrate Relationships.

Protein phosphorylation is catalyzed by kinases which regulate many aspects that control death, movement, and cell growth. Identification of the phosphorylation site-specific kinase-substrate relationships (ssKSRs) is important for understanding cellular dynamics and provides a fundamental basis for...

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Publicado en:BioMed Research International Vol. 2017; pp. 1 - 12
Autores principales: Wang, Minghui, Wang, Tao, Wang, Binghua, Liu, Yu, Li, Ao
Formato: equations & formulas research tables/charts Journal Article
Publicado: Wiley-Blackwell 10/12/2017
Acceso en línea:Ver este registro en EBSCOhost
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      dt: 10/12/2017
      vid: 2017
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      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        10.1155/2017/1826496
        125621965
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        atl: A Novel Phosphorylation Site-Kinase Network-Based Method for the Accurate Prediction of Kinase-Substrate Relationships.
      aug:
        au:
          Wang, Minghui
          Wang, Tao
          Wang, Binghua
          Liu, Yu
          Li, Ao
        affil: School of Information Science and Technology, University of Science and Technology of China, 443 Huangshan Road, Hefei 230027, China
      sug:
        subj:
          Phosphorylation
          Phosphotransferases Analysis
          Human
          Proteins
          Death
          Movement
          Cell Physiology
          Models, Biological
          Models, Statistical
          Data Analysis Software
      ab: Protein phosphorylation is catalyzed by kinases which regulate many aspects that control death, movement, and cell growth. Identification of the phosphorylation site-specific kinase-substrate relationships (ssKSRs) is important for understanding cellular dynamics and provides a fundamental basis for further disease-related research and drug design. Although several computational methods have been developed, most of these methods mainly use local sequence of phosphorylation sites and protein-protein interactions (PPIs) to construct the prediction model. While phosphorylation presents very complicated processes and is usually involved in various biological mechanisms, the aforementioned information is not sufficient for accurate prediction. In this study, we propose a new and powerful computational approach named KSRPred for ssKSRs prediction, by introducing a novel phosphorylation site-kinase network (pSKN) profiles that can efficiently incorporate the relationships between various protein kinases and phosphorylation sites. The experimental results show that the pSKN profiles can efficiently improve the prediction performance in collaboration with local sequence and PPI information. Furthermore, we compare our method with the existing ssKSRs prediction tools and the results demonstrate that KSRPred can significantly improve the prediction performance compared with existing tools.
      pubtype: Academic Journal
      doctype:
        equations & formulas
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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