PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19014879-8 2009 Finally, IFNalpha induced the binding of PEA3 to JAK1, as well as PEA3 tyrosine and serine phosphorylation. Serine 84-90 interferon alpha 1 Homo sapiens 9-17 18722370-3 2008 Cigarette smoking condensate (but not pure nicotine) stimulated specific serine phosphorylation-dependent ubiquitination and degradation of the IFNAR1 subunit of the Type I IFN receptor leading to attenuation of IFN signaling and decreased resistance to viral infection. Serine 73-79 interferon alpha 1 Homo sapiens 144-147 18722370-3 2008 Cigarette smoking condensate (but not pure nicotine) stimulated specific serine phosphorylation-dependent ubiquitination and degradation of the IFNAR1 subunit of the Type I IFN receptor leading to attenuation of IFN signaling and decreased resistance to viral infection. Serine 73-79 interferon alpha 1 Homo sapiens 173-176 18417573-4 2008 Results indicate that PLK1 is engaged by Nipah virus V protein amino acids 100 to 160, previously identified as being the STAT1 binding domain responsible for host interferon (IFN) signaling evasion, via a Thr-Ser-Ser-Pro motif surrounding residue 130. Serine 210-213 interferon alpha 1 Homo sapiens 164-174 18417573-4 2008 Results indicate that PLK1 is engaged by Nipah virus V protein amino acids 100 to 160, previously identified as being the STAT1 binding domain responsible for host interferon (IFN) signaling evasion, via a Thr-Ser-Ser-Pro motif surrounding residue 130. Serine 210-213 interferon alpha 1 Homo sapiens 176-179 18417573-4 2008 Results indicate that PLK1 is engaged by Nipah virus V protein amino acids 100 to 160, previously identified as being the STAT1 binding domain responsible for host interferon (IFN) signaling evasion, via a Thr-Ser-Ser-Pro motif surrounding residue 130. Serine 214-217 interferon alpha 1 Homo sapiens 164-174 18417573-4 2008 Results indicate that PLK1 is engaged by Nipah virus V protein amino acids 100 to 160, previously identified as being the STAT1 binding domain responsible for host interferon (IFN) signaling evasion, via a Thr-Ser-Ser-Pro motif surrounding residue 130. Serine 214-217 interferon alpha 1 Homo sapiens 176-179 17554018-3 2007 STAT1 is serine-phosphorylated downstream of PI3K and MEK in LCLs and this modification restricts IFN-stimulated STAT1-DNA binding. Serine 9-15 interferon alpha 1 Homo sapiens 98-101 17332776-4 2007 Moreover, IFNalpha induced the phosphorylation of both serine and threonine in eEF-1A. Serine 55-61 interferon alpha 1 Homo sapiens 10-18 16751416-3 2006 Overexpression of IFN-lambda induced cell surface MHC class I expression and Fas/CD95 Ag, induced significant caspase-3/7 activity, and increased p21(Waf1/Cip1) and dephosphorylated Rb (Ser(780)) in B16 cells in vitro. Serine 186-189 interferon alpha 1 Homo sapiens 18-21 16260419-4 2005 The influence of PKCdelta on IFN-mediated induction of PLSCR1 was dependent upon the phosphorylation of STAT1 at Ser-727. Serine 113-116 interferon alpha 1 Homo sapiens 29-32 15850832-6 2005 Such phosphorylation/activation of PKC-delta was required for phosphorylation of Stat1 on serine 727, as inhibition of PKC-delta activity blocked the IFN-alpha-dependent serine phosphorylation of Stat1 and IFN-alpha-inducible gene transcription. Serine 90-96 interferon alpha 1 Homo sapiens 150-159 15850832-6 2005 Such phosphorylation/activation of PKC-delta was required for phosphorylation of Stat1 on serine 727, as inhibition of PKC-delta activity blocked the IFN-alpha-dependent serine phosphorylation of Stat1 and IFN-alpha-inducible gene transcription. Serine 90-96 interferon alpha 1 Homo sapiens 206-215 15850832-6 2005 Such phosphorylation/activation of PKC-delta was required for phosphorylation of Stat1 on serine 727, as inhibition of PKC-delta activity blocked the IFN-alpha-dependent serine phosphorylation of Stat1 and IFN-alpha-inducible gene transcription. Serine 170-176 interferon alpha 1 Homo sapiens 150-159 15850832-6 2005 Such phosphorylation/activation of PKC-delta was required for phosphorylation of Stat1 on serine 727, as inhibition of PKC-delta activity blocked the IFN-alpha-dependent serine phosphorylation of Stat1 and IFN-alpha-inducible gene transcription. Serine 170-176 interferon alpha 1 Homo sapiens 206-215 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. Serine 91-97 interferon alpha 1 Homo sapiens 146-155 12759354-4 2003 Our data demonstrate that p70 S6K is rapidly phosphorylated on threonine 421 and serine 424 and is activated during treatment of cells with IFNalpha or IFNbeta. Serine 81-87 interferon alpha 1 Homo sapiens 140-148 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. Serine 138-144 interferon alpha 1 Homo sapiens 15-24 12161037-7 2002 In untreated patients with active MS, serine phosphorylation of the STAT1 transcription factor was markedly reduced, suggesting a mechanism for the low levels of IFN-induced genes. Serine 38-44 interferon alpha 1 Homo sapiens 162-165 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. Serine 72-78 interferon alpha 1 Homo sapiens 15-24 11846979-3 2002 IFN regulatory factor (IRF) proteins are key to this regulation, and their conversion from latent to active involves virus-induced serine phosphorylation. Serine 131-137 interferon alpha 1 Homo sapiens 0-3 11277596-3 2001 After the 36th Phe residue, which was located closely to the 122nd Tyr residue in the tertiary structure, was mutated to Ser using site-directed mutagenesis, the analgesic activity of this mutant lost completely, but the antiviral activity of IFNalpha still maintained 40.5% of wild type IFNalpha. Serine 121-124 interferon alpha 1 Homo sapiens 243-251 11277596-3 2001 After the 36th Phe residue, which was located closely to the 122nd Tyr residue in the tertiary structure, was mutated to Ser using site-directed mutagenesis, the analgesic activity of this mutant lost completely, but the antiviral activity of IFNalpha still maintained 40.5% of wild type IFNalpha. Serine 121-124 interferon alpha 1 Homo sapiens 288-296 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). Serine 149-155 interferon alpha 1 Homo sapiens 48-57 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). Serine 211-217 interferon alpha 1 Homo sapiens 48-57 11162588-2 2001 Here we report that FKBP12-rapamycin-associated protein (FRAP) is a physiologic IRS-1 kinase that blocks IFN alpha signaling by serine phosphorylating IRS-1. Serine 128-134 interferon alpha 1 Homo sapiens 105-114 11095741-5 2000 IFN promotes inhibitor of kappa B alpha (IkappaBalpha) serine phosphorylation and degradation, and stimulates NF-kappaB DNA-binding and transcriptional activity. Serine 55-61 interferon alpha 1 Homo sapiens 0-3 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. Serine 61-64 interferon alpha 1 Homo sapiens 37-45 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. Serine 137-140 interferon alpha 1 Homo sapiens 44-52 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. Serine 60-63 interferon alpha 1 Homo sapiens 36-44 10777558-6 2000 Last, the IFNalpha-induced serine phosphorylation of STAT1 and STAT3 is not inhibited by piceatannol but is sensitive to the Src kinase-specific inhibitor PP2. Serine 27-33 interferon alpha 1 Homo sapiens 10-18 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. Serine 228-234 interferon alpha 1 Homo sapiens 48-56 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. Serine 21-27 interferon alpha 1 Homo sapiens 147-156 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. Serine 21-27 interferon alpha 1 Homo sapiens 203-212 9822609-6 1998 Induction of IRF7 protein in response to IFN and its subsequent activation by phosphorylation in response to virus-specific signals, involving two C-terminal serine residues, are required for induction of the delayed IFNalpha gene set. Serine 158-164 interferon alpha 1 Homo sapiens 41-44 9822609-6 1998 Induction of IRF7 protein in response to IFN and its subsequent activation by phosphorylation in response to virus-specific signals, involving two C-terminal serine residues, are required for induction of the delayed IFNalpha gene set. Serine 158-164 interferon alpha 1 Homo sapiens 217-225 9707562-5 1998 IRF-3-mediated activation of IFN genes depends in part on carboxyl-terminal phosphorylation of a cluster of Ser/Thr residues, because a mutant with Ser/Thr to Ala substitutions activates the IFN promoter less efficiently. Serine 108-111 interferon alpha 1 Homo sapiens 29-32 9707562-5 1998 IRF-3-mediated activation of IFN genes depends in part on carboxyl-terminal phosphorylation of a cluster of Ser/Thr residues, because a mutant with Ser/Thr to Ala substitutions activates the IFN promoter less efficiently. Serine 148-151 interferon alpha 1 Homo sapiens 29-32 9707562-5 1998 IRF-3-mediated activation of IFN genes depends in part on carboxyl-terminal phosphorylation of a cluster of Ser/Thr residues, because a mutant with Ser/Thr to Ala substitutions activates the IFN promoter less efficiently. Serine 148-151 interferon alpha 1 Homo sapiens 191-194 9036989-3 1997 32P-labeling experiments and phosphoaminoacid analysis of immunoprecipitated IRS-1 protein demonstrated that, in addition to tyrosine phosphorylation, IFN-alpha induces its phosphorylation on serine residues. Serine 192-198 interferon alpha 1 Homo sapiens 151-160 9036989-4 1997 In vitro kinase assays on alphaIRS-1 immunoprecipitates also demonstrated IFN-alpha-dependent serine phosphorylation of IRS-1, suggesting that the protein associates with an IFN-alpha-regulated serine kinase. Serine 94-100 interferon alpha 1 Homo sapiens 74-83 9036989-4 1997 In vitro kinase assays on alphaIRS-1 immunoprecipitates also demonstrated IFN-alpha-dependent serine phosphorylation of IRS-1, suggesting that the protein associates with an IFN-alpha-regulated serine kinase. Serine 94-100 interferon alpha 1 Homo sapiens 174-183 8943379-0 1996 Activation of STAT4 by IL-12 and IFN-alpha: evidence for the involvement of ligand-induced tyrosine and serine phosphorylation. Serine 104-110 interferon alpha 1 Homo sapiens 33-42 8943379-7 1996 Since tyrosine and serine phosphorylation of STAT1 have previously been shown to be important in IFN-alpha-mediated signaling, we also investigated IL-12- and IFN-alpha-induced serine phosphorylation of STAT4. Serine 177-183 interferon alpha 1 Homo sapiens 159-168 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. Serine 113-119 interferon alpha 1 Homo sapiens 61-70 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. Serine 178-184 interferon alpha 1 Homo sapiens 15-24 7508909-5 1994 Immunoprecipitation experiments performed with 32P-labeled U-266 cells and phosphoaminoacid analysis of the bands corresponding to p95vav showed that p95vav is phosphorylated on serine residues prior to IFN alpha stimulation of the cells. Serine 178-184 interferon alpha 1 Homo sapiens 203-212 8279808-5 1993 IFN-alpha J/C(Fnu4HI), [Ser-116]IFN-alpha J1, and IFN-alpha C were the most active of the interferons, and were all more active than IFN-alpha A, against RV 39, RV 1A, and VSV. Serine 24-27 interferon alpha 1 Homo sapiens 32-41 8279808-5 1993 IFN-alpha J/C(Fnu4HI), [Ser-116]IFN-alpha J1, and IFN-alpha C were the most active of the interferons, and were all more active than IFN-alpha A, against RV 39, RV 1A, and VSV. Serine 24-27 interferon alpha 1 Homo sapiens 32-41 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. Serine 152-158 interferon alpha 1 Homo sapiens 199-208 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-22 interferon alpha 1 Homo sapiens 24-27 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-22 interferon alpha 1 Homo sapiens 64-67 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-22 interferon alpha 1 Homo sapiens 64-67 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-22 interferon alpha 1 Homo sapiens 64-67 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-19 interferon alpha 1 Homo sapiens 24-27 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-19 interferon alpha 1 Homo sapiens 64-67 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-19 interferon alpha 1 Homo sapiens 64-67 2332772-1 1990 Interferon-beta-serine (IFN-beta-ser) is a muteine, recombinant IFN that is tolerated at a dose fivefold to 10-fold higher than IFN-alfa and interacts with the same cell membrane receptor as IFN-alfa. Serine 16-19 interferon alpha 1 Homo sapiens 64-67 26359551-9 2015 Mutant analysis showed that IFN promoter activity was mostly mediated by the phosphorylation sites at serine residue S379 and S387. Serine 102-108 interferon alpha 1 Homo sapiens 28-31 34131022-0 2021 The transmembrane serine protease hepsin suppresses type I interferon induction by cleaving STING. Serine 18-24 interferon alpha 1 Homo sapiens 59-69 3045221-1 1988 Interferon-beta serine (IFN-beta ser) was administered intravenously (i.v.) Serine 16-22 interferon alpha 1 Homo sapiens 24-27 3045221-1 1988 Interferon-beta serine (IFN-beta ser) was administered intravenously (i.v.) Serine 16-19 interferon alpha 1 Homo sapiens 24-27 2826671-17 1988 A serine at position 110 and a valine at 85 were unique to MuIFN-alpha 10 as compared to all known MuIFN-alpha and human IFN-alpha subspecies. Serine 2-8 interferon alpha 1 Homo sapiens 61-70 3572088-1 1986 Site-specific in vitro mutagenesis was used to direct serine for cysteine substitutions within the sequence of human interferon-alpha 1 (IFN-alpha 1). Serine 54-60 interferon alpha 1 Homo sapiens 117-135 3572088-1 1986 Site-specific in vitro mutagenesis was used to direct serine for cysteine substitutions within the sequence of human interferon-alpha 1 (IFN-alpha 1). Serine 54-60 interferon alpha 1 Homo sapiens 137-148 3756886-1 1986 Beta-interferon serine (IFN-beta ser) is a genetically altered recombinant IFN with a specific activity of 2 X 10(8) IU/mg protein. Serine 16-22 interferon alpha 1 Homo sapiens 24-27 3756886-1 1986 Beta-interferon serine (IFN-beta ser) is a genetically altered recombinant IFN with a specific activity of 2 X 10(8) IU/mg protein. Serine 16-19 interferon alpha 1 Homo sapiens 24-27 3756886-14 1986 We conclude that IFN-beta ser is a well tolerated IFN with minimal renal, hepatic, and bone marrow toxicity. Serine 26-29 interferon alpha 1 Homo sapiens 17-20 3014018-2 1986 IFN-beta ser was cleared from the nose like IFN-alpha. Serine 9-12 interferon alpha 1 Homo sapiens 44-53 2416427-8 1986 The addition of IFN-alpha 54 to IFN-beta ser in the SKCO 1 cell line resulted in an antagonistic interaction. Serine 41-44 interferon alpha 1 Homo sapiens 16-25 3160832-2 1985 We herein demonstrate that three of these IFN preparations (IFN-alpha 76, -alpha 54, -beta ser), as well as naturally produced IFN-beta, can each affect MLC in opposing ways. Serine 91-94 interferon alpha 1 Homo sapiens 42-45 30439382-3 2019 The aim of this study was to generate a novel long-acting IFNalpha with the help of PASylation technology that adds a polypeptide comprising Proline, Alanine and Serine (PAS) to increase plasma half-life. Serine 162-168 interferon alpha 1 Homo sapiens 58-66 27802159-0 2016 Phosphorylation of STAT2 on serine-734 negatively regulates the IFN-alpha-induced antiviral response. Serine 28-34 interferon alpha 1 Homo sapiens 64-73 24449862-0 2014 Novel antiviral host factor, TNK1, regulates IFN signaling through serine phosphorylation of STAT1. Serine 67-73 interferon alpha 1 Homo sapiens 45-48 22996189-5 2013 Ectopic expression of Pol suppressed IFN-alpha-induced STAT1 serine 727 phosphorylation and STAT1/2 nuclear accumulation, whereas STAT1 tyrosine 701 phosphorylation, and STAT1-STAT2 heterodimer formation were not affected. Serine 61-67 interferon alpha 1 Homo sapiens 37-46 22550181-3 2012 We provide evidence that mTORC2 complexes control IFN-induced phosphorylation of AKT on serine 473 and their function is ultimately required for IFN-dependent gene transcription via interferon-stimulated response elements. Serine 88-94 interferon alpha 1 Homo sapiens 50-53 22550181-3 2012 We provide evidence that mTORC2 complexes control IFN-induced phosphorylation of AKT on serine 473 and their function is ultimately required for IFN-dependent gene transcription via interferon-stimulated response elements. Serine 88-94 interferon alpha 1 Homo sapiens 145-148 22065572-3 2011 Here we show that inhibitor of kappaB kinase epsilon (IKKepsilon) phosphorylation of STAT1 at serine 708 (Ser-708) drives IFIT2 expression to mediate anti-WNV effector function of IFN. Serine 94-100 interferon alpha 1 Homo sapiens 180-183 22065572-3 2011 Here we show that inhibitor of kappaB kinase epsilon (IKKepsilon) phosphorylation of STAT1 at serine 708 (Ser-708) drives IFIT2 expression to mediate anti-WNV effector function of IFN. Serine 106-109 interferon alpha 1 Homo sapiens 180-183 22065572-6 2011 STAT1 Ser-708 phosphorylation occurs independently of IRF-3 but requires signaling through the IFN-alpha/beta receptor as a late event in the IFN-induced innate immune response that coincides with IKKepsilon-responsive ISGs expression. Serine 6-9 interferon alpha 1 Homo sapiens 95-104 21865166-2 2011 The extent of cellular responses to IFNalpha is limited by several important mechanisms including the ligand-stimulated and specific serine phosphorylation-dependent degradation of the IFNAR1 chain of Type 1 IFN receptor. Serine 133-139 interferon alpha 1 Homo sapiens 36-44 21478011-10 2011 The sensitising enhancement ratio (SER) for IFNalpha 3000 IU/ml was 2.15 in MiaPaca-2 and 1.90 in Panc-1. Serine 35-38 interferon alpha 1 Homo sapiens 44-52 20406818-8 2010 Collectively, these data suggest that the phosphorylation of RIG-I serine 8 operates as a negative switch of RIG-I activation by suppressing TRIM25 interaction, further underscoring the importance of RIG-I and TRIM25 connection in type I IFN signal transduction. Serine 67-73 interferon alpha 1 Homo sapiens 238-241 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. Serine 208-214 interferon alpha 1 Homo sapiens 86-95