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Paul Domanski

Researcher at University of Tennessee Health Science Center

Publications -  16
Citations -  1616

Paul Domanski is an academic researcher from University of Tennessee Health Science Center. The author has contributed to research in topics: Interleukin 10 receptor, alpha subunit & Interleukin 5 receptor alpha subunit. The author has an hindex of 15, co-authored 16 publications receiving 1571 citations. Previous affiliations of Paul Domanski include University of Tennessee.

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Vaccinia Virus B18R Gene Encodes a Type I Interferon-binding Protein That Blocks Interferon α Transmembrane Signaling

TL;DR: Among viral host response modifiers, the B18R protein is unique inasmuch as it exists as a soluble extracellular as well as a cell surface protein and thus should effectively block both autocrine and paracrine functions of IFN.
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Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling.

TL;DR: Only expression of the α and long form of the human β subunits in mouse L-929 cells reconstitutes the activation of the Jak kinases and the Stat factors, as well as the antiviral response to human type I IFNs.
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Direct binding to and tyrosine phosphorylation of the alpha subunit of the type i interferon receptor by p135tyk2 tyrosine kinase

TL;DR: The hypothesis that the Tyk2 protein functions as part of a receptor complex to initiate intracellular signaling in response to type I IFNs is supported.
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p135tyk2, an interferon-alpha-activated tyrosine kinase, is physically associated with an interferon-alpha receptor.

TL;DR: In this paper, biochemical evidence is presented which supports this proposed function for the tyk2 tyrosine kinase and further defines its role in the interferon-alpha signaling cascade.
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The type-I interferon receptor. The long and short of it.

TL;DR: New advances in the production of specific monoclonal antibodies against the receptor and the cloning of different receptor subunits are analyzed and the role of the different receptors subunits in type-I interferon signaling is analyzed.