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STAT1 — TYR

Text-mined interactions from Literome

Aittomäki et al., J Immunol 2000 : The cooperation required phosphorylation of Tyr701 , DNA binding, and the trans-activation domain of Stat1, but did not involve Ser727 phosphorylation of Stat1 or physical interaction between GR and Stat1
Mazière et al., Free Radic Biol Med 2001 : Genistein, a nonspecific Tyr-kinase inhibitor, and AG490, a specific inhibitor of JAKs, markedly prevented the CuLDL induced enhancement of STAT1 and STAT3 Tyr-phosphorylation and DNA binding activity, suggesting that JAKs are the main kinases involved in STATs ' activation by oxidized LDL
Qing et al., J Biol Chem 2005 : Here we show that Tyr ( 441 ) is required to attenuate STAT1 activation in response to IFNgamma
Zhang et al., J Biol Chem 2005 (Inflammation) : Moreover, Stat1-CC still required ligand dependent Tyr-701 phosphorylation for function and exhibited hyperresponsiveness to IFN-beta ( that depends on Stat1/Stat2 heterodimerization ) as well as IFN-gamma ( that depends on Stat1/Stat1 homodimerization )