Title : Protein kinase IKKβ-catalyzed phosphorylation of IRF5 at Ser462 induces its dimerization and nuclear translocation in myeloid cells.

Pub. Date : 2014 Dec 9

PMID : 25326418






4 Functional Relationships(s)
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1 CL097 also stimulated the phosphorylation of IRF5 at Ser462 and stimulated the nuclear translocation of wild-type IRF5, but not the IRF5[Ser462Ala] mutant. CL097 interferon regulatory factor 5 Homo sapiens
2 CL097 also stimulated the phosphorylation of IRF5 at Ser462 and stimulated the nuclear translocation of wild-type IRF5, but not the IRF5[Ser462Ala] mutant. CL097 interferon regulatory factor 5 Homo sapiens
3 CL097 also stimulated the phosphorylation of IRF5 at Ser462 and stimulated the nuclear translocation of wild-type IRF5, but not the IRF5[Ser462Ala] mutant. CL097 interferon regulatory factor 5 Homo sapiens
4 The CL097-stimulated phosphorylation of IRF5 at Ser462 and its nuclear translocation was prevented by the pharmacological inhibition of protein kinase IKKbeta or the siRNA knockdown of IKKbeta or its "upstream" activator, the protein kinase TAK1. CL097 interferon regulatory factor 5 Homo sapiens