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Last Updated: 2 years ago

Possible Interaction: Interferons and Tyrosine

supplement:

Tyrosine

Research Papers that Mention the Interaction

IFN stimulation results in tyrosine phosphorylation, dimerization, and nuclear import of STATs.
The Journal of Biological Chemistry  •  2001  |  View Paper
Interferon IFN ) treatment induces tyrosine phosphorylation and nuclear translocation of Stat1 (signal transducer and activator of transcription) to activate or repress transcription.
Proceedings of the National Academy of Sciences of the United States of America  •  2001  |  View Paper
Furthermore, LPS plus IFNγ increased the tyrosine phosphorylation of NOS-I, with a concomitant inhibition of its enzyme activity.
The Journal of Biological Chemistry  •  1999  |  View Paper
IFNα also induces tyrosine phosphorylation of IRS-1, the principle substrate of the insulin receptor.
The Journal of Biological Chemistry  •  1996  |  View Paper
IFN induces the expression of the nonreceptor protein tyrosine kinase, hck, and cross-linking the Fc gamma RI receptor in U937IF cells results in the activation of hck kinase as evidenced by the three- to fivefold increased tyrosine phosphorylation of hck.
Journal of immunology  •  1995  |  View Paper
Binding of type I interferons IFNs ) to their receptors induces rapid tyrosine phosphorylation of multiple proteins, including the alpha and beta subunits of the receptor, the polypeptides that form the transcriptional activator ISGF3 alpha (Stat113, Stat84, and Stat91), and the p135tyk2 and Jak-1 tyrosine kinases.
Molecular and cellular biology  •  1994  |  View Paper
Phosphorylation of the 42,000-M(r) protein on tyrosine was observed only after treatment of cells with interferon.
Infection and immunity  •  1994  |  View Paper
We now show that interferon‐γ IFN‐γ ) also decreases constitutive tyrosine phosphorylation of erbB‐2 and inhibits erbB‐2 kinase activity in an ovarian cancer cell line.
International journal of cancer  •  1994  |  View Paper
Immunoblotting analysis demonstrated that IFN gamma induced rapid changes in the tyrosine phosphorylation of several endogenous cytosolic and membranal proteins.
Leukemia research  •  1994  |  View Paper
In mouse livers and bone marrow-derived macrophages, both interferon-γ (IFNγ) and interleukin-6 (IL-6) rapidly induced the tyrosine phosphorylation of signal transducer and activator of transcription-1 (STAT1) and STAT3.
Journal of Biological Chemistry  •  2006  |  View Paper
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