Selected article for: "protein function and small fraction"

Author: Ray, Bridgette N.; Kweon, Hye Kyong; Argetsinger, Lawrence S.; Fingar, Diane C.; Andrews, Philip C.; Carter-Su, Christin
Title: Research Resource: Identification of Novel Growth Hormone-Regulated Phosphorylation Sites by Quantitative Phosphoproteomics
  • Document date: 2012_5_8
  • ID: xtj2ywf3_30
    Snippet: newly identified GH-dependent phosphosites are all documented regulatory sites, i.e. sites whose phosphorylation in response to some stimulus has been reported to regulate the function of the protein (Table 1 and Supplemental Table 1 ), suggesting that GH-promoted phosphorylation at these phosphosites regulates function and is physiologically relevant. The 15 proteins in these four KEGG categories include only a small fraction of the 95 GHregula.....
    Document: newly identified GH-dependent phosphosites are all documented regulatory sites, i.e. sites whose phosphorylation in response to some stimulus has been reported to regulate the function of the protein (Table 1 and Supplemental Table 1 ), suggesting that GH-promoted phosphorylation at these phosphosites regulates function and is physiologically relevant. The 15 proteins in these four KEGG categories include only a small fraction of the 95 GHregulated proteins identified in our SILAC/MS-based phosphoproteomic study that exhibit GH-dependent increases in phosphorylation. Future analysis of these latter proteins, most of whose GH-dependent phosphosites have no known function, stands to further increase our understanding of the physiological actions of GH.

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