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Article

Transcription factor ISGF-3 formation requires phosphorylated Stat91 protein, but Stat113 protein is phosphorylated independently of Stat91 protein.

Proceedings of the National Academy of Sciences of the United States of America - 24 May 1994

Improta T, Schindler C, Horvath C M, Kerr I M, Stark G R, Darnell J E

Abstract excerpt

Transcription factor ISGF-3 is a multiprotein, interferon alpha-activated transcription complex consisting of a 48-kDa DNA-binding protein and two proteins termed Stats (for signal transducers and activators of transcription) that become phosphorylated on tyrosine in the cell cytoplasm, a 113-kDa and either a 91- or 84-kDa polypeptide, the latter two of which arise from differentially spliced mRNAs. Using cell...

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Identifiers

PMID: 8197134
DOI: 10.1073/pnas.91.11.4776
PMCID: PMC43871

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Transcription factor ISGF-3 formation requires phosphorylated Stat91 protein, but Stat113 protein is phosphorylated independently of Stat91 protein.PMID 8197134Read ↗

Ras-independent growth factor signaling by transcription factor tyrosine phosphorylation.Semantic proximity Read ↗

Proteins of transcription factor ISGF-3: one gene encodes the 91-and 84-kDa ISGF-3 proteins that are activated by interferon alpha.Semantic proximity Read ↗

Stat3 isoforms, alpha and beta, demonstrate distinct intracellular dynamics with prolonged nuclear retention of Stat3beta mapping to its unique C-terminal end.Semantic proximity Read ↗

Complementation of a mutant cell line: central role of the 91 kDa polypeptide of ISGF3 in the interferon-alpha and -gamma signal transduction pathways.Semantic proximity Read ↗

Interferon regulatory factor subcellular localization is determined by a bipartite nuclear localization signal in the DNA-binding domain and interaction with cytoplasmic retention factorsSemantic proximity Read ↗

Direct Association of STAT3 with the IFNAR-1 Chain of the Human Type I Interferon ReceptorSemantic proximity Read ↗

STAT-phosphorylation-independent induction of interferon regulatory factor-9 by interferon-beta.Semantic proximity Read ↗

Clinically relevant dimer interface mutants of STAT1 transcription factor exhibit differential gene expression.Semantic proximity Read ↗

Implications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation-inactivation cycle.Semantic proximity Read ↗

Structural bases of unphosphorylated STAT1 association and receptor binding.Semantic proximity Read ↗

c-Src activates the DNA binding and transcriptional activity of Stat3 molecules: serine 727 is not required for transcriptional activation under certain circumstances.Semantic proximity Read ↗

Multiple reasons for an inefficient STAT1 response upon IL-6-type cytokine stimulation.Semantic proximity Read ↗

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