PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28498306-0 2017 A Conserved Residue, Tyrosine (Y) 84, in H5N1 Influenza A Virus NS1 Regulates IFN Signaling Responses to Enhance Viral Infection. Tyrosine 21-29 interferon alpha 1 Homo sapiens 78-81 29886262-7 2018 Consequently, NSs inhibited IFN-alpha-stimulated tyrosine phosphorylation and nuclear translocation of STAT2. Tyrosine 49-57 interferon alpha 1 Homo sapiens 28-37 28498306-2 2017 In this report, we provide evidence that the conserved residue, tyrosine (Y) 84, in a conserved putative SH2-binding domain in A/Duck/Hubei/2004/L-1 [H5N1] NS1 is critical for limiting an interferon (IFN) response to infection. Tyrosine 64-72 interferon alpha 1 Homo sapiens 200-203 21968657-11 2012 Since phosphorylation of tyrosine 701 on STAT-1 is sufficient to induce interferon (IFN)-dependent genes, constitutive activity of this phosphorylation site may lead to the overexpression of IFN-dependent genes, as well as other STAT-1-dependent genes, in HLA-B27 monocyte/macrophages. Tyrosine 25-33 interferon alpha 1 Homo sapiens 84-87 26481041-6 2016 We also evaluated the synergistic efficacy of IFN-alpha-incorporated HA-Tyr hydrogels+sorafenib in this model. Tyrosine 72-75 interferon alpha 1 Homo sapiens 46-55 26481041-9 2016 Our results suggest a possibility that HA-Tyr hydrogel drug delivery system prolongs the biological half-life of natural human IFN-alpha and enhances its anticancer effects on human RCC cells. Tyrosine 42-45 interferon alpha 1 Homo sapiens 127-136 26481041-12 2016 We also evaluated the synergistic efficacy of natural human IFN-alpha-incorporated HA-Tyr hydrogels+sorafenib. Tyrosine 86-89 interferon alpha 1 Homo sapiens 60-69 26481041-14 2016 In addition, we suggested that IFN-alpha-incorporated HA-Tyr hydrogels+sorafenib exhibited most effectively anticancer effects. Tyrosine 57-60 interferon alpha 1 Homo sapiens 31-40 25247291-4 2015 In this study, we demonstrate that type 1 interferon (IFN) production by CpG-challenged monocytes can be suppressed by C1q through activating leukocyte-associated Ig-like receptor-1 (LAIR-1), which contains immunoreceptor tyrosine-based inhibition motifs (ITIMs). Tyrosine 222-230 interferon alpha 1 Homo sapiens 35-58 27802159-5 2016 IFN-alpha-induced S734-STAT2 phosphorylation displayed different kinetics to that of tyrosine phosphorylation. Tyrosine 85-93 interferon alpha 1 Homo sapiens 0-9 24131713-5 2014 Here we report that RV inhibits IFN-mediated STAT1 tyrosine 701 phosphorylation in human IECs in vitro and identify RV NSP1 as a direct inhibitor of the pathway. Tyrosine 51-59 interferon alpha 1 Homo sapiens 32-35 23910645-0 2013 Protein phosphatase 2A impairs IFNalpha-induced antiviral activity against the hepatitis C virus through the inhibition of STAT1 tyrosine phosphorylation. Tyrosine 129-137 interferon alpha 1 Homo sapiens 31-39 23072726-8 2013 These results indicate that IFN-alpha is associated with decreased peripheral conversion of Phen to Tyr, which in turn is associated with reduced DA in the brain as well as fatigue. Tyrosine 100-103 interferon alpha 1 Homo sapiens 28-37 22191466-8 2012 The increase of Phe concentrations and of Phe/Tyr in HCV infected individuals is caused by IFN-alpha therapy. Tyrosine 46-49 interferon alpha 1 Homo sapiens 91-100 21968657-11 2012 Since phosphorylation of tyrosine 701 on STAT-1 is sufficient to induce interferon (IFN)-dependent genes, constitutive activity of this phosphorylation site may lead to the overexpression of IFN-dependent genes, as well as other STAT-1-dependent genes, in HLA-B27 monocyte/macrophages. Tyrosine 25-33 interferon alpha 1 Homo sapiens 191-194 21129804-10 2011 ACK1 expression enhanced the IFN-stimulated response element (ISRE) and interferon-gamma-activated site (GAS) promoter activity through tyrosine phosphorylation of signal transducers and activators of transcription (STAT) 1. Tyrosine 136-144 interferon alpha 1 Homo sapiens 29-32 22036215-5 2012 IFN responses in PBMNC were assessed by in vitro IFN-beta-induced activation of phospho-tyrosine-STAT1 and phospho-serine-STAT1 transcription factors, and MxA proteins using Western blots. Tyrosine 88-96 interferon alpha 1 Homo sapiens 0-3 22312113-5 2012 However, the unmodified, 5"-unphosphorylated in vitro transcript of tRNA(Tyr) induced IFN-alpha, thus revealing posttranscriptional modifications as a factor suppressing immunostimulation. Tyrosine 73-76 interferon alpha 1 Homo sapiens 86-95 21865166-5 2011 PKD2 undergoes IFNalpha-inducible tyrosine phosphorylation on specific phospho-acceptor site (Tyr-438) within the plekstrin homology domain. Tyrosine 34-42 interferon alpha 1 Homo sapiens 15-23 21865166-5 2011 PKD2 undergoes IFNalpha-inducible tyrosine phosphorylation on specific phospho-acceptor site (Tyr-438) within the plekstrin homology domain. Tyrosine 94-97 interferon alpha 1 Homo sapiens 15-23 21865166-7 2011 Tyrosine phosphorylation of PKD2 is required for IFNalpha-stimulated activation of this kinase as well as for efficient serine phosphorylation and degradation of IFNAR1 and ensuing restriction of the extent of cellular responses to IFNalpha. Tyrosine 0-8 interferon alpha 1 Homo sapiens 49-57 21865166-7 2011 Tyrosine phosphorylation of PKD2 is required for IFNalpha-stimulated activation of this kinase as well as for efficient serine phosphorylation and degradation of IFNAR1 and ensuing restriction of the extent of cellular responses to IFNalpha. Tyrosine 0-8 interferon alpha 1 Homo sapiens 232-240 21593149-1 2011 Tyrosine phosphorylation and nuclear translocation of STAT1 indicate activation of interferon (IFN) signal transduction pathways. Tyrosine 0-8 interferon alpha 1 Homo sapiens 83-93 21593149-1 2011 Tyrosine phosphorylation and nuclear translocation of STAT1 indicate activation of interferon (IFN) signal transduction pathways. Tyrosine 0-8 interferon alpha 1 Homo sapiens 95-98 21593149-3 2011 Ad is known to suppress IFN-inducible gene expression; however, we observed that Ad infection prolongs the tyrosine phosphorylation of STAT1 induced by alpha IFN in infected cells. Tyrosine 107-115 interferon alpha 1 Homo sapiens 158-161 19085955-11 2009 Furthermore, HDV blocked the IFN-alpha-stimulated tyrosine phosphorylation of IFN receptor-associated JAK kinase Tyk2, without affecting either the tyrosine phosphorylation of Jak1 or the expression of type I IFN receptor subunits. Tyrosine 50-58 interferon alpha 1 Homo sapiens 29-38 19396596-4 2009 Flow cytometric and immunoblot analyses indicated that the enhanced direct actions of IFN-alpha on melanoma cells were the result of prolonged phosphorylation of STAT1 (P-STAT1) on both the Tyrosine(701) and Serine(727) residues. Tyrosine 190-198 interferon alpha 1 Homo sapiens 86-95 19254804-5 2009 In this study we show that when type I IFN is added to primary human fibroblasts following MV infection, the tyrosine phosphorylation of the Janus kinase Tyk2 is specifically blocked, thereby preventing the subsequent activation of downstream STAT1 and STAT2. Tyrosine 109-117 interferon alpha 1 Homo sapiens 39-42 20937272-4 2011 Inhibition of STAT1 tyrosine phosphorylation and DNA binding by a naturally occurring rotenoid deguelin also rescued U266 myeloma cell lines from IFNalpha-induced apoptosis. Tyrosine 20-28 interferon alpha 1 Homo sapiens 146-154 19515782-2 2009 P, V, and W, have in common an amino-terminal domain sufficient to bind STAT1, inhibiting its interferon (IFN)-induced tyrosine phosphorylation. Tyrosine 119-127 interferon alpha 1 Homo sapiens 94-104 19515782-2 2009 P, V, and W, have in common an amino-terminal domain sufficient to bind STAT1, inhibiting its interferon (IFN)-induced tyrosine phosphorylation. Tyrosine 119-127 interferon alpha 1 Homo sapiens 106-109 19345260-5 2009 Our data demonstrate that nontoxic concentrations of acrolein significantly inhibited IFNalpha-induced tyrosine phosphorylation of both cytoplasmic and nuclear STAT1 and STAT2, without altering the total levels. Tyrosine 103-111 interferon alpha 1 Homo sapiens 86-94 18725457-9 2008 SOCS1 mutants with loss of nuclear localization were still effective in suppressing IFN-alpha-mediated STAT1 tyrosine phosphorylation. Tyrosine 109-117 interferon alpha 1 Homo sapiens 84-93 19014879-8 2009 Finally, IFNalpha induced the binding of PEA3 to JAK1, as well as PEA3 tyrosine and serine phosphorylation. Tyrosine 71-79 interferon alpha 1 Homo sapiens 9-17 19014879-9 2009 CONCLUSIONS: IFNalpha determines the binding of PEA3 to JAK1 and its tyrosine phosphorylation. Tyrosine 69-77 interferon alpha 1 Homo sapiens 13-21 18306331-7 2008 In pretreated Tac, but not CyA, the levels of IFN-alpha-induced tyrosine phosphorylated STAT-1 and -2 were clearly lower than those induced by IFN-alpha alone. Tyrosine 64-72 interferon alpha 1 Homo sapiens 46-55 18474601-2 2008 We previously hypothesized that, in the absence of its cognate ligand, type I interferon (IFN), the IFNalpha receptor chain 1 (IFNAR1) receptor chain is protected from basal endocytosis by a hypothetical masking complex that prevents the Tyr-based endocytic motif within IFNAR1 from interacting with components of the adaptin protein complex 2 (AP2). Tyrosine 238-241 interferon alpha 1 Homo sapiens 71-94 18287094-5 2008 Such effects are associated with impaired IFN-dependent phosphorylation of Stat1 on Tyr(701) and Stat3 on Tyr(705) and defective binding of Stat complexes to ISRE or GAS elements. Tyrosine 84-87 interferon alpha 1 Homo sapiens 42-45 18287094-5 2008 Such effects are associated with impaired IFN-dependent phosphorylation of Stat1 on Tyr(701) and Stat3 on Tyr(705) and defective binding of Stat complexes to ISRE or GAS elements. Tyrosine 106-109 interferon alpha 1 Homo sapiens 42-45 17785772-2 2007 In this article we show that the small dual-specificity phosphatase VHR selectively dephosphorylates IFN-alpha- and beta-activated, tyrosine-phosphorylated STAT5, leading to the subsequent inhibition of STAT5 function. Tyrosine 132-140 interferon alpha 1 Homo sapiens 101-110 17880940-5 2007 IFNalpha promoted sustained accumulation of tyrosine phosphorylated STAT3C in the nucleus and a prolonged DNA binding of the STAT3/3 homodimers in EMSA. Tyrosine 44-52 interferon alpha 1 Homo sapiens 0-8 16595158-5 2006 This was accomplished by preventing the IFN-alpha-induced tyrosine phosphorylation of STAT-1 and STAT-2 through the inactivation of the upstream receptor associated tyrosine kinases, JAK-1 and Tyk-2. Tyrosine 58-66 interferon alpha 1 Homo sapiens 40-49 17785551-3 2007 EXPERIMENTAL DESIGN: Tyr(701)-phosphorylated STAT1 (P-STAT1) was measured by flow cytometry in IFN-alpha-stimulated human melanoma cell lines, melanoma cells derived from patient tumors, and peripheral blood mononuclear cells (PBMC). Tyrosine 21-24 interferon alpha 1 Homo sapiens 95-104 17442890-0 2007 A Mutation in the SH2 domain of STAT2 prolongs tyrosine phosphorylation of STAT1 and promotes type I IFN-induced apoptosis. Tyrosine 47-55 interferon alpha 1 Homo sapiens 101-104 17442890-6 2007 This prolonged IFN response was associated with sustained tyrosine phosphorylation of STAT1 and STAT2 and their mutual association as heterodimers, which resulted from resistance to dephosphorylation by the nuclear tyrosine phosphatase TcPTP. Tyrosine 58-66 interferon alpha 1 Homo sapiens 15-18 17095088-7 2007 Deletion of this region within the hIFNAR2 completely abolishes IFN-alpha/beta-dependent STAT4 tyrosine phosphorylation when expressed in human IFNAR2-deficient fibroblasts. Tyrosine 95-103 interferon alpha 1 Homo sapiens 64-73 17290288-5 2007 Moreover, we provide strong evidence that both the induction of eIF2alpha phosphorylation and inhibition of protein synthesis by IFN are impaired in cells lacking Jak1 or Tyk2, which corresponds to a lack of induction of PKR tyrosine phosphorylation. Tyrosine 225-233 interferon alpha 1 Homo sapiens 129-132 17290288-6 2007 We conclude that PKR tyrosine phosphorylation provides an important link between IFN signalling and translational control through the regulation of eIF2alpha phosphorylation. Tyrosine 21-29 interferon alpha 1 Homo sapiens 81-84 16987558-6 2006 STAT1 tyrosine phosphorylation was elevated by IFN combination treatment, however, only the hyper-transactivation of GAS but not ISRE was observed. Tyrosine 6-14 interferon alpha 1 Homo sapiens 47-50 16324217-17 2005 When IFN-alpha binds its receptor, two receptor associated tyrosine kinases, Tyk2 and Jak1 become activated by phosphorylation, and phosphorylate Stat1 and Stat2 on conserved tyrosine residues 13. Tyrosine 59-67 interferon alpha 1 Homo sapiens 5-14 16731929-1 2006 Japanese encephalitis virus (JEV), a mosquito-borne flavivirus that causes severe human disease, has been shown to block the interferon (IFN)-induced Janus kinase signal transducer and activation of transcription (Jak-Stat) signaling cascade by preventing Tyk2 tyrosine phosphorylation and Stat activation. Tyrosine 261-269 interferon alpha 1 Homo sapiens 125-142 16324217-4 2005 In contrast, when combined with exogenously applied IFN-alpha, ethanol inhibited the antiviral actions of IFN against HCV replication, involving inhibition of IFN-induced Stat1 tyrosine phosphorylation. Tyrosine 177-185 interferon alpha 1 Homo sapiens 52-61 15845643-4 2005 Stimulation of neutrophils with IFN-alpha or IFN-gamma resulted in tyrosine phosphorylation of STAT1 and STAT3 but not phosphorylation of STAT5, Akt, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase. Tyrosine 67-75 interferon alpha 1 Homo sapiens 32-41 16324217-4 2005 In contrast, when combined with exogenously applied IFN-alpha, ethanol inhibited the antiviral actions of IFN against HCV replication, involving inhibition of IFN-induced Stat1 tyrosine phosphorylation. Tyrosine 177-185 interferon alpha 1 Homo sapiens 52-55 16324217-4 2005 In contrast, when combined with exogenously applied IFN-alpha, ethanol inhibited the antiviral actions of IFN against HCV replication, involving inhibition of IFN-induced Stat1 tyrosine phosphorylation. Tyrosine 177-185 interferon alpha 1 Homo sapiens 106-109 15944325-9 2005 Such a selective antagonism on antiviral effect of IFN-alpha, but not IFN-gamma, correlated with down-regulated tyrosine-phosphorylation and DNA-binding activities of STAT1 and STAT3 transcription factors by DV. Tyrosine 112-120 interferon alpha 1 Homo sapiens 51-60 15944325-10 2005 Furthermore, subsequent studies into the underlying mechanisms revealed that DV attenuated IFN-alpha-induced tyrosine-phosphorylation of Tyk2, an upstream molecule of STAT activation, but had no effect on expression of both IFN-alpha receptor 1 and IFN-alpha receptor 2. Tyrosine 109-117 interferon alpha 1 Homo sapiens 91-100 15720527-5 2005 We established stable transfectants of SOCS-1 in a human hepatoma cell line, PLC/PRF/5 and analysed the effects of SOCS-1 on the phosphorylation of IFN-alpha-induced STAT-1 tyrosine by immunoblotting and the expression of antiviral genes by Northern blot. Tyrosine 173-181 interferon alpha 1 Homo sapiens 148-157 15659558-7 2005 We observed induced phosphorylation on several well documented as well as novel tyrosine phosphorylation sites on proteins involved in IFNalpha signal transduction, such as Tyk2, JAK1, and IFNAR subunits. Tyrosine 80-88 interferon alpha 1 Homo sapiens 135-143 15795279-10 2005 Finally, the blocking of the IFN-alpha and IFN-gamma by neutralizing antibodies led to the complete inhibition of tyrosine phosphorylation of STAT1. Tyrosine 114-122 interferon alpha 1 Homo sapiens 29-38 15767445-7 2005 In MuV-infected cells, nuclear translocation and phosphorylation of STAT1 and STAT2 tyrosine residue (Y) at 701 and 689, respectively, by IFN-beta were significantly inhibited but the phosphorylation of Jak1 and Tyk2 was not inhibited. Tyrosine 84-92 interferon alpha 1 Homo sapiens 138-141 16000854-4 2005 IFN-receptor interactions invoke Janus kinase activation via phosphorylation events, which in turn leads to the recruitment and phosphorylation of STAT proteins on tyrosine residues. Tyrosine 164-172 interferon alpha 1 Homo sapiens 0-3 15611255-4 2005 H9 and SKW6.4 cell lines responded to 10,000 IU/ml IFN-alpha-2a, as evidenced by decreased cell proliferation and tyrosine phosphorylation of Stat1 and Stat3 proteins without significant cytotoxicity. Tyrosine 114-122 interferon alpha 1 Homo sapiens 51-60 15302890-6 2004 Both IFN-alpha and IFN-gamma induced strong tyrosine phosphorylation of STAT1 in mature but not in immature neutrophils. Tyrosine 44-52 interferon alpha 1 Homo sapiens 5-14 15542633-7 2004 The lack of cPKC activity leads to a broad reduction of IFN-alpha-stimulated gene expression due to a significant impairment of STAT1 and STAT3 tyrosine phosphorylation. Tyrosine 144-152 interferon alpha 1 Homo sapiens 56-65 16059651-8 2005 In contrast, STAT 1 phosphorylation response at Tyr 701 after IFNalpha occurred in 13 (29.5%) and after IFNgamma in 32 (73%) patients. Tyrosine 48-51 interferon alpha 1 Homo sapiens 62-70 15467722-3 2004 Enhanced IFN-alpha signaling and proinflammatory function were dependent on the tyrosine kinase Syk and on adaptor proteins that activate Syk through immunoreceptor tyrosine activation motifs. Tyrosine 80-88 interferon alpha 1 Homo sapiens 9-18 15467722-5 2004 These results identify a mechanism by which crosstalk between cytokine and immune cell-specific immunoreceptor tyrosine activation motif-dependent signaling pathways regulates macrophage responses to IFN-alpha. Tyrosine 111-119 interferon alpha 1 Homo sapiens 200-209 14647450-7 2004 However, inhibition of Jak1 expression also decreased IFN-alpha-induced tyrosine phosphorylation of ErbB3. Tyrosine 72-80 interferon alpha 1 Homo sapiens 54-63 14690454-5 2004 This STAT1-mediated inhibition does not require STAT1 tyrosine phosphorylation because overexpression of dominant-negative STAT1 with a mutation on tyrosine residue 701 also blocks IFN-alpha activation of STAT1, STAT2 and STAT3. Tyrosine 148-156 interferon alpha 1 Homo sapiens 181-190 14722125-5 2004 One of these clones (Clone 8) is defective in its responses to IFNalpha with regard to activation of genes that require tyrosine phosphorylation of Stat2. Tyrosine 120-128 interferon alpha 1 Homo sapiens 63-71 14722125-6 2004 Stimulation of Clone 8 cells with IFNalpha induces normal tyrosine phosphorylation of Stat1 and Stat3. Tyrosine 58-66 interferon alpha 1 Homo sapiens 34-42 15175343-2 2004 STAT2 resides primarily in the cytoplasm and is tyrosine-phosphorylated after IFNalpha binds to cell surface receptors. Tyrosine 48-56 interferon alpha 1 Homo sapiens 78-86 15166220-5 2004 We found that IFN-lambda 1-induced STAT2 tyrosine phosphorylation is mediated through tyrosines 343 and 517 of the receptor, which showed some similarities with tyrosines from type I IFN receptors involved in STAT2 activation. Tyrosine 41-49 interferon alpha 1 Homo sapiens 14-17 15166220-5 2004 We found that IFN-lambda 1-induced STAT2 tyrosine phosphorylation is mediated through tyrosines 343 and 517 of the receptor, which showed some similarities with tyrosines from type I IFN receptors involved in STAT2 activation. Tyrosine 86-95 interferon alpha 1 Homo sapiens 14-17 15166220-5 2004 We found that IFN-lambda 1-induced STAT2 tyrosine phosphorylation is mediated through tyrosines 343 and 517 of the receptor, which showed some similarities with tyrosines from type I IFN receptors involved in STAT2 activation. Tyrosine 161-170 interferon alpha 1 Homo sapiens 14-17 15296650-5 2004 In the presence of IFN-alpha, core expression was associated with increased IFN-stimulated gene factor 3 (ISGF3) binding to the IFN-stimulated response element (ISRE) and tyrosine phosphorylation of Stat1. Tyrosine 171-179 interferon alpha 1 Homo sapiens 19-28 15087447-4 2004 Cultured human umbilical vein EC (HUVEC) express low levels of STAT4, which may be tyrosine-phosphorylated by treatment with IFNalpha but not IL12. Tyrosine 83-91 interferon alpha 1 Homo sapiens 125-133 12883649-4 2003 To further explore cancer-associated impaired STAT 1 response to IFNs, the inducibility of serine (S 727) and tyrosine (Y 701) phosphorylation by IFN-alpha/-gamma was assessed in 21 melanoma cell lines and in 35 primary cultures derived from melanoma patients. Tyrosine 110-118 interferon alpha 1 Homo sapiens 146-155 12804067-8 2003 In support of this hypothesis, IFN treatment resulted in differential induction of Stat1 phosphorylation at Tyr 701. Tyrosine 108-111 interferon alpha 1 Homo sapiens 31-34 12792788-7 2003 Lovastatin and IFN-alpha 2b in combination led to cell cycle arrest and resulted in significant reduction of phosphorylation on tyrosine, serine, and threonine protein residues. Tyrosine 128-136 interferon alpha 1 Homo sapiens 15-24 12789268-2 2003 Here we report the ability of IFN-alpha to induce tyrosine phosphorylation of a 180 kDa band in the KAS-6/1 MM cell line, which is growth responsive to IFN-alpha. Tyrosine 50-58 interferon alpha 1 Homo sapiens 30-39 12789268-2 2003 Here we report the ability of IFN-alpha to induce tyrosine phosphorylation of a 180 kDa band in the KAS-6/1 MM cell line, which is growth responsive to IFN-alpha. Tyrosine 50-58 interferon alpha 1 Homo sapiens 152-161 12421984-3 2002 SSG enhanced IFN-alpha-induced Stat1 tyrosine phosphorylation, inactivated intracellular SHP-1 and SHP-2 that negatively regulate IFN signaling, and induced cellular protein tyrosine phosphorylation in cancer cell lines. Tyrosine 37-45 interferon alpha 1 Homo sapiens 13-22 12610111-6 2003 In contrast, the C mutant proteins retaining the STAT1-binding capacity suppressed IFN-alpha-stimulated tyrosine phosphorylation of both STAT2 and STAT1 to various degrees. Tyrosine 104-112 interferon alpha 1 Homo sapiens 83-92 12600939-3 2003 Most importantly, in UBP43-deficient cells, IFN-beta induces a prolonged Stat1 tyrosine phosphorylation, DNA binding, and IFN-mediated gene activation. Tyrosine 79-87 interferon alpha 1 Homo sapiens 44-47 12421984-3 2002 SSG enhanced IFN-alpha-induced Stat1 tyrosine phosphorylation, inactivated intracellular SHP-1 and SHP-2 that negatively regulate IFN signaling, and induced cellular protein tyrosine phosphorylation in cancer cell lines. Tyrosine 174-182 interferon alpha 1 Homo sapiens 13-22 11821064-2 2002 We previously reported suppression of IFN-stimulated tyrosine phosphorylation of signal transducers and activators of transcription (Stats) in infected cells. Tyrosine 53-61 interferon alpha 1 Homo sapiens 38-41 12105218-10 2002 We show here that in addition to IFN-dependent tyrosine phosphorylation of STAT3, activation using a STAT3-dependent electrophoretic mobility shift assay and a STAT3-specific reporter can also be demonstrated. Tyrosine 47-55 interferon alpha 1 Homo sapiens 33-36 12105218-11 2002 Furthermore, we demonstrate that type I IFN-dependent activation of STAT3 proceeds through a novel mechanism that is dependent on two tyrosines, Tyr(337) and Tyr(512), present in IFNAR2c and contained within a conserved six-amino acid residue motif, GxGYxM. Tyrosine 134-143 interferon alpha 1 Homo sapiens 40-43 12105218-11 2002 Furthermore, we demonstrate that type I IFN-dependent activation of STAT3 proceeds through a novel mechanism that is dependent on two tyrosines, Tyr(337) and Tyr(512), present in IFNAR2c and contained within a conserved six-amino acid residue motif, GxGYxM. Tyrosine 145-148 interferon alpha 1 Homo sapiens 40-43 12105218-11 2002 Furthermore, we demonstrate that type I IFN-dependent activation of STAT3 proceeds through a novel mechanism that is dependent on two tyrosines, Tyr(337) and Tyr(512), present in IFNAR2c and contained within a conserved six-amino acid residue motif, GxGYxM. Tyrosine 158-161 interferon alpha 1 Homo sapiens 40-43 12105218-12 2002 Surprisingly, both tyrosines were previously shown to be required for type I IFN-dependent STAT1 and STAT2 activation. Tyrosine 19-28 interferon alpha 1 Homo sapiens 77-80 12040445-2 2002 Treatment of freshly isolated (day 0), highly purified (>95% pure) CD34+ cells with recombinant IFN-alpha resulted in rapid tyrosine phosphorylation and activation of STAT1, Tyk2 and JAK1 as shown by Western immunoblotting. Tyrosine 127-135 interferon alpha 1 Homo sapiens 99-108 11886239-3 2002 STAT1 was continuously phosphorylated at tyrosine 701 by IFN signaling; however, its serine phosphorylation was suppressed. Tyrosine 41-49 interferon alpha 1 Homo sapiens 57-60 12051728-4 2002 With regard to IFN-alpha signaling, IL-1beta enhanced both tyrosine and serine phosphorylation of STAT1 through p38 mitogen-activated protein kinase activation. Tyrosine 59-67 interferon alpha 1 Homo sapiens 15-24 12051728-5 2002 In contrast, IL-10 inhibited IFN-alpha-mediated tyrosine phosphorylation of STAT1 by induction of a Janus kinase inhibitor, JAB. Tyrosine 48-56 interferon alpha 1 Homo sapiens 29-38 11886239-0 2002 Dephosphorylation failure of tyrosine-phosphorylated STAT1 in IFN-stimulated Sendai virus C protein-expressing cells. Tyrosine 29-37 interferon alpha 1 Homo sapiens 62-65 11802163-1 2002 Type I interferon (IFN) stimulates transcription through a heteromeric transcription factor that contains tyrosine-phosphorylated STAT2. Tyrosine 106-114 interferon alpha 1 Homo sapiens 0-23 11821064-5 2002 IFN-stimulated tyrosine phosphorylation of Stat1 was doubtlessly suppressed early in infection, but the suppression was incomplete, suggesting the importance of the unknown blocking mechanism that inactivates the tyrosine-phosphorylated (pY)-Stat1 generated as the signaling leak. Tyrosine 15-23 interferon alpha 1 Homo sapiens 0-3 11821064-5 2002 IFN-stimulated tyrosine phosphorylation of Stat1 was doubtlessly suppressed early in infection, but the suppression was incomplete, suggesting the importance of the unknown blocking mechanism that inactivates the tyrosine-phosphorylated (pY)-Stat1 generated as the signaling leak. Tyrosine 213-221 interferon alpha 1 Homo sapiens 0-3 11476770-11 2001 Tyrosine phosphorylation of STAT 1 in capacitated sperm was enhanced by IFN-alpha and IFN-gamma, and that of STAT 4 was enhanced by IL-12. Tyrosine 0-8 interferon alpha 1 Homo sapiens 72-81 11513540-6 2001 Using different polyclonal antibodies that recognize either total STAT-4 protein or tyrosine-phosphorylated STAT-4, we can easily detect IL-12 and IFNalpha signaling in PHA/IL-2 blasts derived from peripheral blood lymphocytes. Tyrosine 84-92 interferon alpha 1 Homo sapiens 147-155 11162588-1 2001 We have previously shown that interferon-alpha (IFN alpha)-dependent tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) is impaired by serine phosphorylation of IRS-1 due to the reduced ability of serine phosphorylated IRS-1 to serve as a substrate for Janus kinase 1 (JAK1). Tyrosine 69-77 interferon alpha 1 Homo sapiens 48-57 11473581-6 2001 We provide evidence that the cytoplasmic tyrosine residues of IFNAR-1, which remains phosphorylated by a weak IFN-alpha/beta stimulation, provide docking sites for Stat1 and Stat3 to form homo- or heterodimers following IL-6 stimulation. Tyrosine 41-49 interferon alpha 1 Homo sapiens 110-119 11277596-2 2001 We ever reported that there exist distinct domains in IFNalpha molecule that mediate immune and analgesic effects respectively and inferred that the analgesic domain locates around the 122nd Tyr residue of IFNalpha molecule in the tertiary structure. Tyrosine 191-194 interferon alpha 1 Homo sapiens 54-62 11277596-2 2001 We ever reported that there exist distinct domains in IFNalpha molecule that mediate immune and analgesic effects respectively and inferred that the analgesic domain locates around the 122nd Tyr residue of IFNalpha molecule in the tertiary structure. Tyrosine 191-194 interferon alpha 1 Homo sapiens 206-214 11277596-4 2001 The results suggest that the 36th Phe residue is one of the constituent for the analgesic domain of IFNalpha and inferred that the analgesic domain of IFNalpha consists of the 122nd Tyr and the residues around the 122nd in the tertiary structure, which include the 36th Phe. Tyrosine 182-185 interferon alpha 1 Homo sapiens 100-108 11277596-4 2001 The results suggest that the 36th Phe residue is one of the constituent for the analgesic domain of IFNalpha and inferred that the analgesic domain of IFNalpha consists of the 122nd Tyr and the residues around the 122nd in the tertiary structure, which include the 36th Phe. Tyrosine 182-185 interferon alpha 1 Homo sapiens 151-159 11301323-5 2001 Disruption of the IFNalpha receptor-RACK1 interaction abolishes not only IFNalpha-induced tyrosine phosphorylation of STAT1 but also activation of STAT2, indicating that RACK1 plays a central role in early signaling through the Jak-STAT pathway. Tyrosine 90-98 interferon alpha 1 Homo sapiens 18-26 11301323-5 2001 Disruption of the IFNalpha receptor-RACK1 interaction abolishes not only IFNalpha-induced tyrosine phosphorylation of STAT1 but also activation of STAT2, indicating that RACK1 plays a central role in early signaling through the Jak-STAT pathway. Tyrosine 90-98 interferon alpha 1 Homo sapiens 73-81 11150296-2 2001 IFN stimulation results in tyrosine phosphorylation, dimerization, and nuclear import of STATs. Tyrosine 27-35 interferon alpha 1 Homo sapiens 0-3 11248056-1 2001 Interferon (IFN) treatment induces tyrosine phosphorylation and nuclear translocation of Stat1 (signal transducer and activator of transcription) to activate or repress transcription. Tyrosine 35-43 interferon alpha 1 Homo sapiens 0-10 11248056-1 2001 Interferon (IFN) treatment induces tyrosine phosphorylation and nuclear translocation of Stat1 (signal transducer and activator of transcription) to activate or repress transcription. Tyrosine 35-43 interferon alpha 1 Homo sapiens 12-15 11162588-5 2001 Furthermore, treatment of U266 cells with the FRAP inhibitor rapamycin increased IFN alpha-dependent tyrosine phosphorylation by twofold while reducing constitutive IRS-1 serine phosphorylation within S/T-P motifs by 80%. Tyrosine 101-109 interferon alpha 1 Homo sapiens 81-90 10900338-3 2000 After the 129th Tyr residue of human IFNalpha was mutated to Ser, the antiviral activity almost disappeared, but there still remained a strong analgesic activity that could be blocked by naloxone. Tyrosine 16-19 interferon alpha 1 Homo sapiens 37-45 11408801-11 2001 Furthermore, IFN-alpha enhanced tyrosine phosphorylation of Stat1 and Stat2. Tyrosine 32-40 interferon alpha 1 Homo sapiens 13-22 10982828-5 2000 Mutation of the N domain at tryptophan residue W37, predicted to interrupt N domain dimer formation, unexpectedly prevented IFN-alpha-induced tyrosine phosphorylation of the Stat4 monomer, blocking dimer formation and nuclear translocation. Tyrosine 142-150 interferon alpha 1 Homo sapiens 124-133 10900338-5 2000 However, although the antiviral activity of IFNalpha decreased to 34.1% of wild type IFNalpha after the 122nd Tyr residue was changed to Ser, the analgesic activity of this mutant was lost completely. Tyrosine 110-113 interferon alpha 1 Homo sapiens 44-52 10900338-5 2000 However, although the antiviral activity of IFNalpha decreased to 34.1% of wild type IFNalpha after the 122nd Tyr residue was changed to Ser, the analgesic activity of this mutant was lost completely. Tyrosine 110-113 interferon alpha 1 Homo sapiens 85-93 10900338-7 2000 These studies show strong structural and functional similarities between INFalpha and opioid peptides, and inferred that the analgesic domain locates around the 122nd Tyr residue of IFNalpha molecule in tertiary structure. Tyrosine 167-170 interferon alpha 1 Homo sapiens 182-190 10777558-7 2000 Thus, our results not only demonstrate that the IFNalpha/beta receptor utilizes distinct mechanisms to trigger the tyrosine phosphorylation of specific STAT proteins, but they also indicate a diverging pathway that leads to the serine phosphorylation of STAT1 and STAT3. Tyrosine 115-123 interferon alpha 1 Homo sapiens 48-56 10918594-3 2000 Analysis of the early signals triggered by IFN-alpha and IFN-beta demonstrated that the two IFNs were similarly effective in inducing tyrosine phosphorylation of the Jak-1 and Tyk-2 kinases and the transcription factors Stat-1 and Stat-2. Tyrosine 134-142 interferon alpha 1 Homo sapiens 43-52 11956564-4 2000 When the 129th Tyr residue of human IFNalpha was mutated to Ser, the immunoactivity of the mutant almost disappeared, while the strong analgesic activity still persisted, which could be blocked by naloxone. Tyrosine 15-18 interferon alpha 1 Homo sapiens 36-44 10777558-5 2000 This inhibition is paralleled by the loss of Jak1 and IFNAR1 tyrosine phosphorylation in response to IFNalpha, whereas Tyk2 and IFNAR2 tyrosine phosphorylation is unaffected. Tyrosine 61-69 interferon alpha 1 Homo sapiens 101-109 10803933-5 2000 Therefore, we studied the effect of recombinant IFNalpha on tyrosine phosphorylation and proliferation of cytosolic proteins in human cell lines and in freshly isolated B-CLL cells in order to test the potential value of these events as a pretreatment test for IFNalpha in CLL. Tyrosine 60-68 interferon alpha 1 Homo sapiens 48-56 10753717-9 2000 Indeed, in SeV- and hPIV3-infected cells STAT1 was phosphorylated on tyrosine 701 (Y701), a characteristic of IFN receptor activation. Tyrosine 69-77 interferon alpha 1 Homo sapiens 110-113 10803933-6 2000 In human lymphoid cell lines, IFNalpha induced tyrosine phosphorylation of multiple cytosolic proteins in a time- and concentration-dependent manner. Tyrosine 47-55 interferon alpha 1 Homo sapiens 30-38 10803933-8 2000 In marked contrast, in freshly isolated B-CLL cells IFNalpha seemed to have both stimulatory and inhibitory effects on proliferation, but it consistently stimulated tyrosine phosphorylation. Tyrosine 165-173 interferon alpha 1 Homo sapiens 52-60 10803933-10 2000 Therefore, the assessment of IFNalpha-induced tyrosine phosphorylation of cytosolic phospho-proteins does not allow to predict the treatment response to IFNalpha in CLL patients. Tyrosine 46-54 interferon alpha 1 Homo sapiens 29-37 10666284-2 2000 IFN-alpha-stimulated tyrosine phosphorylation of STATs and subsequent formation of the IFN-stimulated gene factor 3 transcription complex were inhibited in SeV-infected cells, resulting in inefficient induction of IFN-stimulated gene products. Tyrosine 21-29 interferon alpha 1 Homo sapiens 0-9 10666284-4 2000 Moreover, tyrosine phosphorylation of Jak1 in response to IFN-alpha was unaffected at the early phase of infection, suggesting that oligomerization of the receptor subunits proceeded normally. Tyrosine 10-18 interferon alpha 1 Homo sapiens 58-67 10666284-5 2000 In contrast to Jak1, IFN-alpha-stimulated tyrosine phosphorylation of Tyk2 was partially inhibited. Tyrosine 42-50 interferon alpha 1 Homo sapiens 21-30 10657627-1 2000 IFN-gamma transduces signals by activating the IFN-gamma receptor-associated Jak-1 and Jak-2 kinases and by inducing tyrosine phosphorylation and activation of the Stat-1 transcriptional activator. Tyrosine 117-125 interferon alpha 1 Homo sapiens 0-3 10488146-2 1999 Here, we report that serine phosphorylation of IRS-1 induced by either okadaic acid (OA) or chronic insulin stimulation prevents interferon-alpha (IFN-alpha)-dependent IRS-1 tyrosine phosphorylation and IFN-alpha-dependent IRS-1/phosphatidylinositol 3"-kinase (PI3K) association. Tyrosine 174-182 interferon alpha 1 Homo sapiens 147-156 10586107-5 1999 Type I IFN induces the phosphorylation of STAT1 and STAT2 proteins by tyrosine phosphorylation involving the type I IFN receptor-associated tyrosine kinases TYK2 and JAK1. Tyrosine 70-78 interferon alpha 1 Homo sapiens 7-10 10586107-5 1999 Type I IFN induces the phosphorylation of STAT1 and STAT2 proteins by tyrosine phosphorylation involving the type I IFN receptor-associated tyrosine kinases TYK2 and JAK1. Tyrosine 70-78 interferon alpha 1 Homo sapiens 116-119 10490982-6 1999 Induction of Stat6 complexes by IFN-alpha appears to be cell type specific, given that tyrosine phosphorylation of Stat6 in response to IFN-alpha is predominantly detected in B cells. Tyrosine 87-95 interferon alpha 1 Homo sapiens 32-41 10490982-6 1999 Induction of Stat6 complexes by IFN-alpha appears to be cell type specific, given that tyrosine phosphorylation of Stat6 in response to IFN-alpha is predominantly detected in B cells. Tyrosine 87-95 interferon alpha 1 Homo sapiens 136-145 10488146-2 1999 Here, we report that serine phosphorylation of IRS-1 induced by either okadaic acid (OA) or chronic insulin stimulation prevents interferon-alpha (IFN-alpha)-dependent IRS-1 tyrosine phosphorylation and IFN-alpha-dependent IRS-1/phosphatidylinositol 3"-kinase (PI3K) association. Tyrosine 174-182 interferon alpha 1 Homo sapiens 203-212 10488146-4 1999 We found that treatment of U266 cells with OA induced serine phosphorylation of IRS-1 and completely blocked IFN-alpha-dependent tyrosine phosphorylation of IRS-1 and IFN-alpha-dependent IRS-1/PI3K association. Tyrosine 129-137 interferon alpha 1 Homo sapiens 109-118 10488146-6 1999 Chronic treatment of U266 cells with insulin led to a 50% reduction in IFN-alpha-dependent tyrosine phosphorylation of IRS-1 and IRS-1/PI3K association. Tyrosine 91-99 interferon alpha 1 Homo sapiens 71-80 10098730-6 1999 The ability of leukaemic cells to exhibit the S phase accumulation after stimulation by IFN-alpha plus sodium butyrate correlated well with persistent tyrosine phosphorylation of cdc2, whereas treatment with IFN-gamma plus sodium butyrate did not affect its phosphorylation levels. Tyrosine 151-159 interferon alpha 1 Homo sapiens 88-97 10068671-9 1999 IFN-alpha enhanced tyrosine phosphorylation of STAT1, STAT3, STAT4, STAT5a, and STAT5b. Tyrosine 19-27 interferon alpha 1 Homo sapiens 0-9 10029571-7 1999 This was accomplished by preventing the IFN-induced tyrosine phosphorylation of STAT1, a component of both IFNalpha- and IFNgamma-induced DNA binding complexes. Tyrosine 52-60 interferon alpha 1 Homo sapiens 40-43 10029571-7 1999 This was accomplished by preventing the IFN-induced tyrosine phosphorylation of STAT1, a component of both IFNalpha- and IFNgamma-induced DNA binding complexes. Tyrosine 52-60 interferon alpha 1 Homo sapiens 107-115 10029571-8 1999 Therefore, IL-10 can directly inhibit STAT-dependent early response gene expression induced by both IFNalpha and IFNgamma in monocytes by suppressing the tyrosine phosphorylation of STAT1. Tyrosine 154-162 interferon alpha 1 Homo sapiens 100-108 10428508-3 1999 In the present study, we provide evidence that the related CrkII protein is also rapidly phosphorylated on tyrosine during treatment of U-266 and Daudi cells with IFNalpha or IFNbeta. Tyrosine 107-115 interferon alpha 1 Homo sapiens 163-171 10098730-7 1999 Considering that dephosphorylation of cdc2 leads to entry to the M phase, the persistent tyrosine phosphorylation of cdc2 may be associated with the S phase accumulation induced by IFN-alpha and sodium butyrate. Tyrosine 89-97 interferon alpha 1 Homo sapiens 181-190 9872990-1 1999 Type I interferons (IFNalpha and IFNbeta) transduce signals by inducing tyrosine phosphorylation of Jaks and Stats, as well as the CrkL adapter, an SH2/SH3-containing protein which provides a link to downstream pathways that mediate growth inhibition. Tyrosine 72-80 interferon alpha 1 Homo sapiens 20-40 9872990-2 1999 We report that Stat5 interacts constitutively with the IFN receptor-associated Tyk-2 kinase, and during IFNalpha stimulation its tyrosine-phosphorylated form acts as a docking site for the SH2 domain of CrkL. Tyrosine 129-137 interferon alpha 1 Homo sapiens 104-112 9501047-4 1998 Removal of the conserved membrane distal 16-amino-acid IRTAM (Interferon Receptor Tyrosine Activation Motif) sequence: (1) increased sensitivity to IFN alpha"s antiviral activity, (2) increased the rapid IFN alpha-dependent formation of STAT-containing DNA-binding complexes, (3) prolonged tyrosine phosphorylation kinetics of the JAK-STAT pathway, and (4) blocked the IFN-dependent down-regulation of the IFNAR1 chain. Tyrosine 82-90 interferon alpha 1 Homo sapiens 148-157 9804758-2 1998 Activation of STAT1 by IFNalpha or IFNgamma through its tyrosine phosphorylation involves members of the Jak tyrosine kinases. Tyrosine 56-64 interferon alpha 1 Homo sapiens 23-31 9677371-3 1998 Upon treatment of cells with interferon alpha (IFNalpha), the IFNaR1 subunit of the IFNalpha receptor becomes tyrosine phosphorylated at position 466. Tyrosine 110-118 interferon alpha 1 Homo sapiens 47-55 9677371-3 1998 Upon treatment of cells with interferon alpha (IFNalpha), the IFNaR1 subunit of the IFNalpha receptor becomes tyrosine phosphorylated at position 466. Tyrosine 110-118 interferon alpha 1 Homo sapiens 84-92 9677371-4 1998 The region surrounding phosphorylated tyrosine 466 subsequently acts as a docking site for the SH2 domain of Stat2, facilitating phosphorylation of the latter and, thus, the transduction of the IFNalpha signal. Tyrosine 38-46 interferon alpha 1 Homo sapiens 194-202 9581833-8 1998 By analyzing the effect of PRL on IFN alpha/beta-induced tyrosine phosphorylation of Stat proteins and their binding to IFN-regulated genes, we now report that costimulation of PRL receptors did not interfere with IFN alpha/beta signals in several human breast cancer cell lines, including T47D, MCF-7, and BT-20. Tyrosine 57-65 interferon alpha 1 Homo sapiens 34-43 9581833-8 1998 By analyzing the effect of PRL on IFN alpha/beta-induced tyrosine phosphorylation of Stat proteins and their binding to IFN-regulated genes, we now report that costimulation of PRL receptors did not interfere with IFN alpha/beta signals in several human breast cancer cell lines, including T47D, MCF-7, and BT-20. Tyrosine 57-65 interferon alpha 1 Homo sapiens 34-37 9581833-10 1998 Instead, IFN alpha/beta- and PRL-induced tyrosine phosphorylation of Stat1 was additive and occurred without evidence of competition for limited concentrations of cytoplasmic Stat1. Tyrosine 41-49 interferon alpha 1 Homo sapiens 9-18 9581833-11 1998 A similar additive relationship was observed on IFN alpha/beta- and PRL-induced Stat3 tyrosine phosphorylation. Tyrosine 86-94 interferon alpha 1 Homo sapiens 48-57 9531615-1 1998 Multiple biologic effects of interferon-alpha (IFN-alpha), including cell growth inhibition and antiviral protection, are initiated by tyrosine phosphorylation of STAT proteins. Tyrosine 135-143 interferon alpha 1 Homo sapiens 47-56 9769120-2 1998 Both IFNalpha and IFNgamma have been shown to exert their effects via a recently discovered signalling pathway by inducing tyrosine phosphorylation of their receptors. Tyrosine 123-131 interferon alpha 1 Homo sapiens 5-13 9501047-4 1998 Removal of the conserved membrane distal 16-amino-acid IRTAM (Interferon Receptor Tyrosine Activation Motif) sequence: (1) increased sensitivity to IFN alpha"s antiviral activity, (2) increased the rapid IFN alpha-dependent formation of STAT-containing DNA-binding complexes, (3) prolonged tyrosine phosphorylation kinetics of the JAK-STAT pathway, and (4) blocked the IFN-dependent down-regulation of the IFNAR1 chain. Tyrosine 82-90 interferon alpha 1 Homo sapiens 204-213 9501047-4 1998 Removal of the conserved membrane distal 16-amino-acid IRTAM (Interferon Receptor Tyrosine Activation Motif) sequence: (1) increased sensitivity to IFN alpha"s antiviral activity, (2) increased the rapid IFN alpha-dependent formation of STAT-containing DNA-binding complexes, (3) prolonged tyrosine phosphorylation kinetics of the JAK-STAT pathway, and (4) blocked the IFN-dependent down-regulation of the IFNAR1 chain. Tyrosine 290-298 interferon alpha 1 Homo sapiens 148-157 9501047-4 1998 Removal of the conserved membrane distal 16-amino-acid IRTAM (Interferon Receptor Tyrosine Activation Motif) sequence: (1) increased sensitivity to IFN alpha"s antiviral activity, (2) increased the rapid IFN alpha-dependent formation of STAT-containing DNA-binding complexes, (3) prolonged tyrosine phosphorylation kinetics of the JAK-STAT pathway, and (4) blocked the IFN-dependent down-regulation of the IFNAR1 chain. Tyrosine 290-298 interferon alpha 1 Homo sapiens 204-213 9374471-1 1997 Interferon (IFN) alpha induces rapid and transient tyrosine phosphorylation of the Src homology 2/Src homology 3 (SH2/SH3)-containing CrkL adaptor protein in a time- and dose-dependent manner. Tyrosine 51-59 interferon alpha 1 Homo sapiens 0-22 9249040-2 1997 IFN alpha treatment of cells induces the rapid tyrosine phosphorylation of these two kinases, two subunits of the IFN alpha receptor, and two members of the signal transducer and activator of transcription (STAT) family of latent transcription factors. Tyrosine 47-55 interferon alpha 1 Homo sapiens 0-9 9242679-3 1997 STAT1 and STAT2 are activated by tyrosine phosphorylation in response to type I interferons-alpha/beta (IFN-alpha/beta) and subsequently form a multimeric transcription factor designated the IFN-alpha-stimulated gene factor 3 (ISGF3). Tyrosine 33-41 interferon alpha 1 Homo sapiens 104-113 9218843-7 1997 IFN-alpha/beta specifically induced tyrosine phosphorylation and translocation into nucleus of signal transducers and activators of transcription (STAT) 2 protein in the T cell clones. Tyrosine 36-44 interferon alpha 1 Homo sapiens 0-9 9249040-2 1997 IFN alpha treatment of cells induces the rapid tyrosine phosphorylation of these two kinases, two subunits of the IFN alpha receptor, and two members of the signal transducer and activator of transcription (STAT) family of latent transcription factors. Tyrosine 47-55 interferon alpha 1 Homo sapiens 114-123 9020188-1 1997 Transcriptional responses to interferon (IFN) are mediated by tyrosine phosphorylation and nuclear translocation of transcription factors of the signal transducer and activator of transcription (Stat) family. Tyrosine 62-70 interferon alpha 1 Homo sapiens 29-39 9121453-1 1997 Two members of the STAT signal transducer and activator of transcription family, STAT1 and STAT2, are rapidly phosphorylated on tyrosine in response to alpha interferon (IFN-alpha). Tyrosine 128-136 interferon alpha 1 Homo sapiens 170-179 9020188-1 1997 Transcriptional responses to interferon (IFN) are mediated by tyrosine phosphorylation and nuclear translocation of transcription factors of the signal transducer and activator of transcription (Stat) family. Tyrosine 62-70 interferon alpha 1 Homo sapiens 41-44 8780896-6 1996 Coprecipitation experiments demonstrated an association of constitutively tyrosine-phosphorylated TYK2 with the IFN-alpha receptor 1 chain. Tyrosine 74-82 interferon alpha 1 Homo sapiens 112-121 9038355-2 1997 During engagement of the type I IFN receptor, p95vav is phosphorylated on tyrosine residues, but the kinase regulating its phosphorylation has not been identified to date. Tyrosine 74-82 interferon alpha 1 Homo sapiens 32-35 9038355-3 1997 Our studies demonstrate that p95vav forms a stable complex with the IFN-receptor-associated Tyk-2 kinase in vivo, and strongly suggest that this kinase regulates its phosphorylation on tyrosine. Tyrosine 185-193 interferon alpha 1 Homo sapiens 68-71 8969169-5 1996 Both IFNAR1 and IFNAR2.2 undergo tyrosine phosphorylation upon induction by either IFN-alpha or IFN-beta. Tyrosine 33-41 interferon alpha 1 Homo sapiens 83-92 8943379-6 1996 In this study, we demonstrated that STAT4 activation by IL-12 is not unique; IL-12 and IFN-alpha, but not IFN-gamma, induced tyrosine phosphorylation and DNA binding of STAT4. Tyrosine 125-133 interferon alpha 1 Homo sapiens 87-96 8943379-10 1996 Thus, STAT4 activation was not IL-12 specific, and IL-12 and IFN-alpha activated STAT4 through both tyrosine and serine phosphorylation. Tyrosine 100-108 interferon alpha 1 Homo sapiens 61-70 8910507-1 1996 Interferon-alpha (IFN-alpha)-mediated intracellular signaling is initiated by ligand-induced receptor dimerization, tyrosine phosphorylation of the Tyk2 and Jak1 tyrosine kinases, and subsequent phosphorylation of the Stat1 and Stat2 proteins. Tyrosine 116-124 interferon alpha 1 Homo sapiens 18-27 8910507-7 1996 IFN-alpha-induced receptor tyrosine phosphorylation was not critical for signaling because mutation of Tyr residues to Phe did not prevent the biological response to IFN-alpha. Tyrosine 27-35 interferon alpha 1 Homo sapiens 0-9 8917387-4 1996 We report that the treatment of cells with vanadate selectively potentiated (2-3 fold) the levels of IFN-stimulated tyrosine phosphorylation of p91 (and not of p113) as compared to the levels of p91 activated by IFN alone and that this was associated with the increased accumulation of phosphorylated p91 in the nucleus, and the activation of protein tyrosine kinases that phosphorylate p91. Tyrosine 116-124 interferon alpha 1 Homo sapiens 101-104 8943349-9 1996 By contrast, IFN-alpha caused tyrosine phosphorylation and DNA binding of exclusively the b isoform of Stat5, and activated Stat5b formed a DNA binding activity previously found in HeLa cells and designated IFN-alpha activation factor 2. Tyrosine 30-38 interferon alpha 1 Homo sapiens 13-22 8780698-2 1996 In U-266 myeloma and 293T embryonic kidney cells, p120cbl is rapidly phosphorylated on tyrosine in an IFN alpha-dependent manner. Tyrosine 87-95 interferon alpha 1 Homo sapiens 102-111 8780896-7 1996 TYK2 activity led to an IFN-alpha-independent appearance of tyrosine-phosphorylated STAT1 but not STAT2 or JAK1 proteins. Tyrosine 60-68 interferon alpha 1 Homo sapiens 24-33 8780896-8 1996 Consistent with this, TYK2 activity also caused constitutive activation of the IFN-alpha-responsive transcription factor IFN-alpha activation factor, a dimer of tyrosine-phosphorylated STAT1, but not of the IFN-alpha-responsive transcription factor IFN-stimulated gene factor 3, a heterotrimer of tyrosine-phosphorylated STAT1 and STAT2 in association with a M(r) 48,000 DNA-binding subunit. Tyrosine 161-169 interferon alpha 1 Homo sapiens 79-88 8780896-8 1996 Consistent with this, TYK2 activity also caused constitutive activation of the IFN-alpha-responsive transcription factor IFN-alpha activation factor, a dimer of tyrosine-phosphorylated STAT1, but not of the IFN-alpha-responsive transcription factor IFN-stimulated gene factor 3, a heterotrimer of tyrosine-phosphorylated STAT1 and STAT2 in association with a M(r) 48,000 DNA-binding subunit. Tyrosine 161-169 interferon alpha 1 Homo sapiens 121-130 8780896-8 1996 Consistent with this, TYK2 activity also caused constitutive activation of the IFN-alpha-responsive transcription factor IFN-alpha activation factor, a dimer of tyrosine-phosphorylated STAT1, but not of the IFN-alpha-responsive transcription factor IFN-stimulated gene factor 3, a heterotrimer of tyrosine-phosphorylated STAT1 and STAT2 in association with a M(r) 48,000 DNA-binding subunit. Tyrosine 161-169 interferon alpha 1 Homo sapiens 121-130 8780896-8 1996 Consistent with this, TYK2 activity also caused constitutive activation of the IFN-alpha-responsive transcription factor IFN-alpha activation factor, a dimer of tyrosine-phosphorylated STAT1, but not of the IFN-alpha-responsive transcription factor IFN-stimulated gene factor 3, a heterotrimer of tyrosine-phosphorylated STAT1 and STAT2 in association with a M(r) 48,000 DNA-binding subunit. Tyrosine 297-305 interferon alpha 1 Homo sapiens 79-88 8780896-8 1996 Consistent with this, TYK2 activity also caused constitutive activation of the IFN-alpha-responsive transcription factor IFN-alpha activation factor, a dimer of tyrosine-phosphorylated STAT1, but not of the IFN-alpha-responsive transcription factor IFN-stimulated gene factor 3, a heterotrimer of tyrosine-phosphorylated STAT1 and STAT2 in association with a M(r) 48,000 DNA-binding subunit. Tyrosine 297-305 interferon alpha 1 Homo sapiens 121-130 8780896-8 1996 Consistent with this, TYK2 activity also caused constitutive activation of the IFN-alpha-responsive transcription factor IFN-alpha activation factor, a dimer of tyrosine-phosphorylated STAT1, but not of the IFN-alpha-responsive transcription factor IFN-stimulated gene factor 3, a heterotrimer of tyrosine-phosphorylated STAT1 and STAT2 in association with a M(r) 48,000 DNA-binding subunit. Tyrosine 297-305 interferon alpha 1 Homo sapiens 121-130 8780896-10 1996 Our results suggest that in addition to activated TYK2, there is a requirement for additional, IFN-alpha-dependent signals for the phosphorylation of STAT2 and the generation of IFN-stimulated gene factor 3 as well as for the conversion of tyrosine-phosphorylated STAT1 into transcriptionally active IFN-alpha activation factor. Tyrosine 240-248 interferon alpha 1 Homo sapiens 95-104 8628273-1 1996 Binding of alpha interferon (IFNalpha) to its receptors induces rapid tyrosine phosphorylation of the receptor subunits IFNaR1 and IFNaR2, the TYK2 and JAK1 tyrosine kinases, and the Stat1 and Stat2 transcription factors. Tyrosine 70-78 interferon alpha 1 Homo sapiens 11-38 8628273-9 1996 Specifically, mutations in the binding domain act in a dominant-negative fashion to inhibit the IFNalpha-induced tyrosine phosphorylation of TYK2 and Stat2. Tyrosine 113-121 interferon alpha 1 Homo sapiens 96-104 8605876-1 1996 Interferon-alpha (IFN alpha) induces rapid tyrosine phosphorylation of its receptors, two JAK kinases and three STAT transcription factors. Tyrosine 43-51 interferon alpha 1 Homo sapiens 18-27 8626489-2 1996 We show that STAT3 undergoes IFNalpha-dependent tyrosine phosphorylation and IFNalpha treatment induces protein-DNA complexes that contain STAT3. Tyrosine 48-56 interferon alpha 1 Homo sapiens 29-37 8626489-3 1996 In addition, STAT3 associates with the IFNAR-1 chain of the type I receptor in a tyrosine phosphorylation-dependent manner upon IFNalpha addition. Tyrosine 81-89 interferon alpha 1 Homo sapiens 128-136 8657115-4 1996 Phorbol ester treatment of monocytes inhibited IFN alpha-stimulated tyrosine phosphorylation of the transcription factors Stat1alpha, Stat2, and Stat3 and of the tyrosine kinase Tyk2 but had no effect on IFN-gamma activation of Stat1alpha. Tyrosine 68-76 interferon alpha 1 Homo sapiens 47-56 8657115-5 1996 IFNalpha-stimulated tyrosine phosphorylation of Jak1 and the alpha subunit of the IFN-alpha receptor were unaffected by phorbol 12-myristate 13-acetate (PMA). Tyrosine 20-28 interferon alpha 1 Homo sapiens 0-8 8657115-5 1996 IFNalpha-stimulated tyrosine phosphorylation of Jak1 and the alpha subunit of the IFN-alpha receptor were unaffected by phorbol 12-myristate 13-acetate (PMA). Tyrosine 20-28 interferon alpha 1 Homo sapiens 0-3 8605876-6 1996 When this phosphopeptide is introduced into permeabilized cells, the IFN alpha-dependent tyrosine phosphorylation of both STATs is blocked. Tyrosine 89-97 interferon alpha 1 Homo sapiens 69-78 8524306-1 1996 Alpha interferon (IFN-alpha)-induced transcriptional activation requires the induction of a complex of DNA-binding proteins, including tyrosine-phosphorylated Stat1 and Stat2, and of p48, a protein which is not phosphorylated on tyrosine and which comes from a separate family of DNA-binding proteins. Tyrosine 135-143 interferon alpha 1 Homo sapiens 0-27 8650265-1 1996 IRS-signalling proteins are engaged and phosphorylated on tyrosine residues by the receptors for insulin and IGF-1, and various classes of cytokine receptors, including IL-4, IL-9, and IL-13; IFN alpha/beta and IFN gamma; and growth hormone and LIF. Tyrosine 58-66 interferon alpha 1 Homo sapiens 192-201 8550573-1 1996 Binding of interferon alpha (IFN alpha) to its receptor induces activation of the Tyk-2 and Jak-1 tyrosine kinases and tyrosine phosphorylation of multiple downstream signaling elements, including the Stat components of the interferon-stimulated gene factor 3 (ISGF-3). Tyrosine 98-106 interferon alpha 1 Homo sapiens 29-38 8550573-2 1996 IFN alpha also induces tyrosine phosphorylation of IRS-1, the principle substrate of the insulin receptor. Tyrosine 23-31 interferon alpha 1 Homo sapiens 0-9 8524306-1 1996 Alpha interferon (IFN-alpha)-induced transcriptional activation requires the induction of a complex of DNA-binding proteins, including tyrosine-phosphorylated Stat1 and Stat2, and of p48, a protein which is not phosphorylated on tyrosine and which comes from a separate family of DNA-binding proteins. Tyrosine 229-237 interferon alpha 1 Homo sapiens 0-27 8524306-3 1996 As reported earlier, Stat1, which is the second target of tyrosine phosphorylation in IFN-alpha-treated cells, is not phosphorylated in the absence of Stat2. Tyrosine 58-66 interferon alpha 1 Homo sapiens 86-95 7479825-1 1995 The IFNAR chain of the type I interferon (IFN) receptor (IFNIR) undergoes rapid ligand-dependent tyrosine phosphorylation and acts as a species-specific transducer for type I IFN action. Tyrosine 97-105 interferon alpha 1 Homo sapiens 4-7 7479825-1 1995 The IFNAR chain of the type I interferon (IFN) receptor (IFNIR) undergoes rapid ligand-dependent tyrosine phosphorylation and acts as a species-specific transducer for type I IFN action. Tyrosine 97-105 interferon alpha 1 Homo sapiens 42-45 7479825-8 1995 The tyrosine phosphorylation and down-regulation of the IFNAR chain were induced by type I IFN in several human cell lines of diverse origins but not in HEC1B cells. Tyrosine 4-12 interferon alpha 1 Homo sapiens 56-59 7479825-9 1995 However, of type I IFNs, IFN-beta uniquely induced the tyrosine phosphorylation of a 105-kDa protein associated with the IFNAR chain in two lymphoblastoid cell lines (Daudi and U266), demonstrating the specificity of transmembrane signaling for IFN-beta and IFN-alpha through the IFNAR chain. Tyrosine 55-63 interferon alpha 1 Homo sapiens 258-267 21552922-1 1995 Upon binding of interferon (IFN) and epidermal growth factor (EGF) to their cell surface receptors, tyrosine phosphorylation of latent cytoplasmic Stat91 (Ras-independent signal transducer and activator of transcription, Stat1 alpha) protein is promptly induced and translocate from the cytoplasm to the nucleus to transduce the signal. Tyrosine 100-108 interferon alpha 1 Homo sapiens 16-26 7559568-1 1995 Binding of interferon-alpha (IFN alpha) to the multisubunit type I IFN receptor (IFNR) induces activation of the Tyk-2 and Jak-1 kinases and tyrosine phosphorylation of multiple signaling elements, including the Stat proteins that form the ISGF3 alpha complex. Tyrosine 141-149 interferon alpha 1 Homo sapiens 29-38 21552922-1 1995 Upon binding of interferon (IFN) and epidermal growth factor (EGF) to their cell surface receptors, tyrosine phosphorylation of latent cytoplasmic Stat91 (Ras-independent signal transducer and activator of transcription, Stat1 alpha) protein is promptly induced and translocate from the cytoplasm to the nucleus to transduce the signal. Tyrosine 100-108 interferon alpha 1 Homo sapiens 28-31 7729946-7 1995 EGF-induced tyrosine (tyr) phosphorylation both of total cellular protein extracts and of the immunoprecipitated EGF-R is increased in IFN alpha-treated cells. Tyrosine 12-20 interferon alpha 1 Homo sapiens 135-144 7629131-2 1995 We report that Tyk-2 forms stable complexes with the SH2-containing hematopoietic cell phosphatase (HCP) in several hematopoietic cell lines in vivo, and that the IFN alpha-induced tyrosine-phosphorylated form of Tyk-2 is a substrate for the phosphatase activity of HCP in in vitro assays. Tyrosine 181-189 interferon alpha 1 Homo sapiens 163-172 7608146-1 1995 Interferon-alpha (IFN alpha) induces rapid tyrosine phosphorylation of the insulin receptor substrate-1 (IRS-1), a docking protein with multiple tyrosine phosphorylation sites that bind to the Src homology 2 (SH2) domains of various signaling proteins. Tyrosine 43-51 interferon alpha 1 Homo sapiens 18-27 7608146-1 1995 Interferon-alpha (IFN alpha) induces rapid tyrosine phosphorylation of the insulin receptor substrate-1 (IRS-1), a docking protein with multiple tyrosine phosphorylation sites that bind to the Src homology 2 (SH2) domains of various signaling proteins. Tyrosine 145-153 interferon alpha 1 Homo sapiens 18-27 7608146-2 1995 During IFN alpha stimulation, the p85 regulatory subunit of the phosphatidylinositol 3"-kinase binds via its SH2 domains to tyrosine-phosphorylated IRS-1, and phosphatidylinositol 3"-kinase activity is detected in association with IRS-1. Tyrosine 124-132 interferon alpha 1 Homo sapiens 7-16 7729946-7 1995 EGF-induced tyrosine (tyr) phosphorylation both of total cellular protein extracts and of the immunoprecipitated EGF-R is increased in IFN alpha-treated cells. Tyrosine 12-15 interferon alpha 1 Homo sapiens 135-144 7884896-7 1995 In this study, we have investigated whether alpha/beta IFN produced by NS20Y/MS cells activates cellular protein tyrosine kinases which will induce tyrosine phosphorylating activity specific to virus-infected cells. Tyrosine 113-121 interferon alpha 1 Homo sapiens 55-58 7759950-4 1995 In addition to ligand binding, IFN-alpha/beta R is directly involved in signaling, because it becomes phosphorylated at Tyr residues on ligand binding and it is physically associated with the cytoplasmic tyrosine kinase JAK1. Tyrosine 120-123 interferon alpha 1 Homo sapiens 31-40 7535819-3 1995 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. Tyrosine 54-62 interferon alpha 1 Homo sapiens 0-3 7535054-4 1995 Treatment with IFN-alpha had a dual effect on relative phosphoamino acids content of P60: inhibited the phosphorylation on threonine residue, and enhanced the phosphorylation on serine and tyrosine residues. Tyrosine 189-197 interferon alpha 1 Homo sapiens 15-24 8027027-3 1994 Both IFN-alpha and IFN-beta induced tyrosine phosphorylation of the beta subunit of the receptor. Tyrosine 36-44 interferon alpha 1 Homo sapiens 5-14 7988557-4 1994 IFN alpha induced the tyrosine phosphorylation of JAK1 and Tyk2, but not JAK2 or JAK3. Tyrosine 22-30 interferon alpha 1 Homo sapiens 0-9 7929242-4 1994 In addition, cells from the G1/S phase exhibited increased tyrosine phosphorylation of JAK-1 and Tyk-2 kinases and p91 by IFN-alpha as compared with asynchronized cells. Tyrosine 59-67 interferon alpha 1 Homo sapiens 122-131 7532663-0 1995 Resistance of melanoma cell lines to interferons correlates with reduction of IFN-induced tyrosine phosphorylation. Tyrosine 90-98 interferon alpha 1 Homo sapiens 78-81 7532663-7 1995 Furthermore, the IFN responsiveness of three melanoma cell lines could be correlated with the ability to detect by immunoblotting of SDS-PAGE displays of cell lysates, IFN-induced tyrosine phosphorylated cellular proteins in the range m.w. Tyrosine 180-188 interferon alpha 1 Homo sapiens 17-20 7532663-7 1995 Furthermore, the IFN responsiveness of three melanoma cell lines could be correlated with the ability to detect by immunoblotting of SDS-PAGE displays of cell lysates, IFN-induced tyrosine phosphorylated cellular proteins in the range m.w. Tyrosine 180-188 interferon alpha 1 Homo sapiens 168-171 7532663-10 1995 Based on these results, we propose that the IFN-resistant melanoma cell lines examined contain a deficiency early in the IFN signal transduction pathway resulting in a reduced potential for IFN-induced tyrosine phosphorylation and a lack of responsiveness to IFN. Tyrosine 202-210 interferon alpha 1 Homo sapiens 44-47 7532663-10 1995 Based on these results, we propose that the IFN-resistant melanoma cell lines examined contain a deficiency early in the IFN signal transduction pathway resulting in a reduced potential for IFN-induced tyrosine phosphorylation and a lack of responsiveness to IFN. Tyrosine 202-210 interferon alpha 1 Homo sapiens 121-124 7532663-10 1995 Based on these results, we propose that the IFN-resistant melanoma cell lines examined contain a deficiency early in the IFN signal transduction pathway resulting in a reduced potential for IFN-induced tyrosine phosphorylation and a lack of responsiveness to IFN. Tyrosine 202-210 interferon alpha 1 Homo sapiens 121-124 7532663-10 1995 Based on these results, we propose that the IFN-resistant melanoma cell lines examined contain a deficiency early in the IFN signal transduction pathway resulting in a reduced potential for IFN-induced tyrosine phosphorylation and a lack of responsiveness to IFN. Tyrosine 202-210 interferon alpha 1 Homo sapiens 121-124 8055912-4 1994 Using these, we have identified tyk2 as a 134-kDa protein which is rapidly and transiently phosphorylated on tyrosine in response to IFN-alpha/beta and possesses an inducible kinase activity when tested in vitro. Tyrosine 109-117 interferon alpha 1 Homo sapiens 133-142 8027027-4 1994 The Type I IFN-induced tyrosine phosphorylation of the beta subunit was rapid and transient, being detectable within 1 min of Type I IFN treatment and gradually diminishing to almost base-line levels by 60 min. Tyrosine 23-31 interferon alpha 1 Homo sapiens 11-14 8027027-4 1994 The Type I IFN-induced tyrosine phosphorylation of the beta subunit was rapid and transient, being detectable within 1 min of Type I IFN treatment and gradually diminishing to almost base-line levels by 60 min. Tyrosine 23-31 interferon alpha 1 Homo sapiens 133-136 8027027-5 1994 All Type I IFNs studied were found to induce tyrosine phosphorylation of the alpha subunit of the Type I IFN receptor, the p135tyk2 and JAK-1 tyrosine kinases, and the ISGF3 alpha components. Tyrosine 45-53 interferon alpha 1 Homo sapiens 11-14 8027027-6 1994 Interestingly, IFN-beta, but not IFN-alpha or IFN-omega, induced tyrosine phosphorylation of an alpha subunit-associated protein with an apparent molecular mass of approximately 100 kDa (p100). Tyrosine 65-73 interferon alpha 1 Homo sapiens 15-18 8114747-1 1994 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. Tyrosine 85-93 interferon alpha 1 Homo sapiens 126-135 7510216-1 1994 Stat91 (a 91 kd protein that acts as a signal transducer and activator of transcription) is inactive in the cytoplasm of untreated cells but is activated by phosphorylation on tyrosine in response to a number of polypeptide ligands, including interferon alpha (IFN-alpha) and IFN-gamma. Tyrosine 176-184 interferon alpha 1 Homo sapiens 243-270 8114747-9 1994 The inability of class B mutants to phosphorylate the 84-, 91-, or 113-kDa protein on tyrosine residues correlated with the loss of biological response to IFN-alpha and -gamma. Tyrosine 86-94 interferon alpha 1 Homo sapiens 155-164 8378773-1 1993 Interferon-alpha (IFN-alpha) and IFN-gamma regulate gene expression by tyrosine phosphorylation of several transcription factors that have the 91-kilodalton (p91) protein of interferon-stimulated gene factor-3 (ISGF-3) as a common component. Tyrosine 71-79 interferon alpha 1 Homo sapiens 18-27 8306959-0 1994 Tyrosine phosphorylated p91 binds to a single element in the ISGF2/IRF-1 promoter to mediate induction by IFN alpha and IFN gamma, and is likely to autoregulate the p91 gene. Tyrosine 0-8 interferon alpha 1 Homo sapiens 106-115 8306959-5 1994 Tyrosine phosphorylation and DNA binding activity of p91 parallel transcription of ISGF2 in response to IFN alpha and/or IFN gamma, consistent with induction mediated by only a GAS. Tyrosine 0-8 interferon alpha 1 Homo sapiens 104-113 7504784-1 1993 Binding of interferons IFN-alpha and IFN-gamma to their cell surface receptors promptly induces tyrosine phosphorylation of latent cytoplasmic transcriptional activators (or Stat proteins, for signal transducers and activators of transcription). Tyrosine 96-104 interferon alpha 1 Homo sapiens 23-32 7504785-1 1993 Interferons IFN-alpha/beta and IFN-gamma act through independent cell-surface receptors, inducing gene expression through tyrosine phosphorylation of cytoplasmic transcription factors . Tyrosine 122-130 interferon alpha 1 Homo sapiens 12-21 7508909-2 1994 Immunoblotting experiments using an anti-phosphotyrosine monoclonal antibody showed that interferon alpha (IFN alpha) induces rapid tyrosine phosphorylation of p95vav after binding to its cell surface receptor in the U-266 human myeloma cell line. Tyrosine 48-56 interferon alpha 1 Homo sapiens 107-116 7508909-3 1994 The IFN alpha-induced tyrosine phosphorylation of p95vav was time- and dose-dependent, confirming the specificity of the process. Tyrosine 22-30 interferon alpha 1 Homo sapiens 4-13 7508909-4 1994 IFN alpha-dependent tyrosine phosphorylation of p95vav was also observed in other hematopoietic cell lines of B-cell origin (Daudi), T-cell origin (MOLT-4), and promyelocytic origin (HL-60). Tyrosine 20-28 interferon alpha 1 Homo sapiens 0-9 7508909-6 1994 After IFN alpha stimulation significant amounts of phosphorylation of p95vav on tyrosine residues were detectable. Tyrosine 80-88 interferon alpha 1 Homo sapiens 6-15 8321205-6 1993 Therefore, specificity for IFN-induced transcriptional activation of early response genes requires at least two events: (i) ligand-induced activation of membrane-associated protein by tyrosine phosphorylation and (ii) formation of a complex composed of an activated membrane protein(s) and a sequence-specific DNA-binding component. Tyrosine 184-192 interferon alpha 1 Homo sapiens 27-30 1385434-5 1992 Phosphoamino acid analysis confirmed the IFN alpha-induced tyrosine phosphorylation and demonstrated that the base-line phosphorylation corresponded to serine phosphorylation that increased 50% upon IFN alpha treatment. Tyrosine 59-67 interferon alpha 1 Homo sapiens 41-50 1385434-7 1992 Phosphorylation of the alpha subunit of the receptor occurred rapidly after IFN alpha binding, both at 37 and 4 degrees C. Exposure of the cells to the tyrosine kinase inhibitor genistein blocked the IFN alpha-induced tyrosine phosphorylation of this subunit of the IFN alpha receptor. Tyrosine 152-160 interferon alpha 1 Homo sapiens 200-209 1385434-3 1992 Immunoblotting experiments showed that IFN alpha induced rapid tyrosine phosphorylation of the alpha subunit in the IFN alpha-sensitive H-929, U-266, and Daudi cell lines. Tyrosine 63-71 interferon alpha 1 Homo sapiens 39-48 1385434-3 1992 Immunoblotting experiments showed that IFN alpha induced rapid tyrosine phosphorylation of the alpha subunit in the IFN alpha-sensitive H-929, U-266, and Daudi cell lines. Tyrosine 63-71 interferon alpha 1 Homo sapiens 116-125 1385434-7 1992 Phosphorylation of the alpha subunit of the receptor occurred rapidly after IFN alpha binding, both at 37 and 4 degrees C. Exposure of the cells to the tyrosine kinase inhibitor genistein blocked the IFN alpha-induced tyrosine phosphorylation of this subunit of the IFN alpha receptor. Tyrosine 152-160 interferon alpha 1 Homo sapiens 200-209 1385434-10 1992 Altogether these data suggest that tyrosine phosphorylation of the alpha subunit may play a role in the signal transduction pathway of IFN alpha. Tyrosine 35-43 interferon alpha 1 Homo sapiens 135-144 1995306-7 1991 These results demonstrate that IFN-alpha synergises hemin-mediated erythroid differentiation as it reduces the in vivo tyrosine phosphorylation of P210bcr/abl in K-562 cells. Tyrosine 119-127 interferon alpha 1 Homo sapiens 31-40 1496401-2 1992 Treatment of cells with IFN-alpha caused these three proteins to be phosphorylated on tyrosine and to translocate to the cell nucleus where they stimulate transcription through binding to IFN-alpha-stimulated response elements in DNA. Tyrosine 86-94 interferon alpha 1 Homo sapiens 24-33 1496401-2 1992 Treatment of cells with IFN-alpha caused these three proteins to be phosphorylated on tyrosine and to translocate to the cell nucleus where they stimulate transcription through binding to IFN-alpha-stimulated response elements in DNA. Tyrosine 86-94 interferon alpha 1 Homo sapiens 188-197 2526185-0 1989 Structure-function studies of interferons-alpha: amino acid substitutions at the conserved residue tyrosine 123 in human interferon-alpha 1. Tyrosine 99-107 interferon alpha 1 Homo sapiens 121-139 2526185-2 1989 The tyrosine residue 123, which is conserved in all known mammalian IFNs-alpha and -beta, was replaced by each of 6 amino acids or was deleted from the protein. Tyrosine 4-12 interferon alpha 1 Homo sapiens 68-88 32420725-3 2020 Our data indicated that IL-1beta alone does not inhibit HCV replication, yet when in combination with IFN-alpha, it can boost anti-HCV activity of IFN-alpha, which is mediated by augmented STAT1 tyrosine 701 phosphorylation. Tyrosine 195-203 interferon alpha 1 Homo sapiens 102-111 32420725-3 2020 Our data indicated that IL-1beta alone does not inhibit HCV replication, yet when in combination with IFN-alpha, it can boost anti-HCV activity of IFN-alpha, which is mediated by augmented STAT1 tyrosine 701 phosphorylation. Tyrosine 195-203 interferon alpha 1 Homo sapiens 147-156 31633442-6 2020 Furthermore, ISG expression in VLV-infected cells was dependent on IFN receptor signaling through the Janus kinase (JAK) tyrosine kinases and phosphorylation of the STAT1 protein, and JAK inhibition restored VLV replication in otherwise uninfectable cell lines. Tyrosine 121-129 interferon alpha 1 Homo sapiens 67-70