Mutant cell lines unresponsive to alpha/beta and gamma interferon are defective in tyrosine phosphorylation of ISGF-3 alpha components.

The 84-, 91-, and 113-kDa proteins of the ISGF-3 alpha complex are phosphorylated on tyrosine residues upon alpha interferon (IFN-alpha) treatment and subsequently translocate to the nucleus together with a 48-kDa subunit. In this study, we investigated the presence and the functional status of ISGF...

詳細記述

書誌詳細

出版年:	Mol Cell Biol
主要な著者:	Loh, J E, Schindler, C, Ziemiecki, A, Harpur, A G, Wilks, A F, Flavell, R A
フォーマット:	Artigo
言語:	Inglês
出版事項:	Taylor & Francis 1994
主題:	Research Article
オンライン･アクセス:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC358577/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8114747/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.14.3.2170-2179.1994
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