Affiliation: Hokkaido University
- Systematic characterization by mass spectrometric analysis of phosphorylation sites in IRF-3 regulatory domain activated by IKK-iKiyonaga Fujii
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N 12, W 6, Kita ku, Sapporo 060 0812, Japan
J Proteomics 73:1196-203. 2010..Thus, we demonstrated that Ser-386, -396 and -402 are directly phosphorylated by IKK-i in the co-expression system. These results will help provide new insights into the IRF-3 activation mechanism...
- Ser386 phosphorylation of transcription factor IRF-3 induces dimerization and association with CBP/p300 without overall conformational changeKiyohiro Takahasi
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N 12W 6 Kita ku, Sapporo 060 0812, Japan
Genes Cells 15:901-10. 2010..Thus, we conclude that the phosphorylation of Ser386 is essential for activation of IRF-3...
- Differential LC-MS-based proteomics of surgical human cholangiocarcinoma tissuesHiroshi Kawase
Department of Surgical Oncology, Hokkaido University Graduate School of Medicine, Kita ku, Sapporo, Japan
J Proteome Res 8:4092-103. 2009..Thus, we successfully identified several proteins up-regulated in cholangiocarcinoma. These proteins are candidate biomarkers and may also help to provide new insights into our understanding of the disease...