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0.568 18.3036 0.568 12 z"/> <path style="fill:url(#color3_0_7J]v]j1TnAamZwDU);stroke:none;" d="M 8.6611 19.6732 c 0 0.5832 -0.4166 0.8748 -0.9789 0.8748 c -0.5832 0 -0.9789 -0.2916 -0.9789 -0.8956 V 6.4471 c 0 -1.6038 0.6456 -2.2495 2.1244 -2.2495 h 4.624 c 3.291 0 5.1446 1.6871 5.1446 4.6447 c 0 3.1243 -1.9161 4.9363 -5.228 4.9363 h -4.7072 V 19.6732 z M 13.3267 12.0292 c 2.1037 0 3.2284 -1.1247 3.2284 -3.1452 c 0 -1.8746 -1.1456 -2.916 -3.2284 -2.916 h -3.9991 c -0.4582 0 -0.6665 0.2708 -0.6665 0.729 v 5.3322 H 13.3267 z"/> </svg> PMID: 18049472 It was also shown that microbial nucleic acids, lipids, polysaccharides or proteins trigger induction of IFNs through activation of TLRs. PMID: 18049472 It was also shown that microbial nucleic acids, lipids, polysaccharides or proteins trigger induction of IFNs through activation of TLRs. PMID: 18049472 It was also shown that microbial nucleic acids, lipids, polysaccharides or proteins trigger induction of IFNs through activation of TLRs. PMID: 18049472 It was also shown that microbial nucleic acids, lipids, polysaccharides or proteins trigger induction of IFNs through activation of TLRs. PMID: 18049472, 15208624 dsRNA is recognized by TLR3, which is present mostly in endosomal membranes4, and also by two cytoplasmic RNA helicases, retinoic acid-inducible gene I (RIG-I) and melanoma differentiation associated protein 5 (MDA5). PMID: 18049472, 15208624 dsRNA is recognized by TLR3, which is present mostly in endosomal membranes4, and also by two cytoplasmic RNA helicases, retinoic acid-inducible gene I (RIG-I) and melanoma differentiation associated protein 5 (MDA5). PMID: 18049472, 15208624 dsRNA is recognized by TLR3, which is present mostly in endosomal membranes4, and also by two cytoplasmic RNA helicases, retinoic acid-inducible gene I (RIG-I) and melanoma differentiation associated protein 5 (MDA5). PMID: 18049472 It was also shown that microbial nucleic acids, lipids, polysaccharides or proteins trigger induction of IFNs through activation of TLRs. Indirect PMID: 18049472 It was also shown that microbial nucleic acids, lipids, polysaccharides or proteins trigger induction of IFNs through activation of TLRs. PMID: 18049472 TLR3 dimerizes, binds to CD14 and activates the signalling complex assembled by TLR adaptor molecule 1 (TRIF). PMID: 18049472 The cytoplasmic RNA helicases RIG-I and MDA5 recognize dsRNA or 5' triphosphorylated single-stranded (ss) RNA and use the mitochondrial membrane-bound protein IFN-beta-promoter stimulator 1 (IPS1; also known as VISA) as the specific adaptor. PMID: 18049472, 15710892 For example, a hepatitis C virus (HCV)-encoded protease can cleave IPS1 off the mitochondrial membrane and block RIG-I/MDA5-mediated signalling. PMID: 18049472 The cytoplasmic RNA helicases RIG-I and MDA5 recognize dsRNA or 5' triphosphorylated single-stranded (ss) RNA and use the mitochondrial membrane-bound protein IFN-beta-promoter stimulator 1 (IPS1; also known as VISA) as the specific adaptor. PMID: 18049472, 15710892 For example, a hepatitis C virus (HCV)-encoded protease can cleave IPS1 off the mitochondrial membrane and block RIG-I/MDA5-mediated signalling. PMID: 18049472, 17038589 NS1 protein of influenza viruses prevents establishment of an antiviral state through the interaction with RIG-I. PMID; 18049472, 17190786 Other nucleic acids such as ssRNA, acting through TLR7 and TLR8, and bacterial oligodeoxyribonucleotides, acting through TLR9, are also potent inducers. PMID: 18049472 They also function as dimers and recognize double-stranded (ds) RNA, single-stranded (ss) RNA or dsDNA containing CpG sequences. GPI, glycosylphosphatidylinisotol; LPS, lipopolysaccharide. PMID; 18049472, 17190786 Other nucleic acids such as ssRNA, acting through TLR7 and TLR8, and bacterial oligodeoxyribonucleotides, acting through TLR9, are also potent inducers. PMID: 18049472 They also function as dimers and recognize double-stranded (ds) RNA, single-stranded (ss) RNA or dsDNA containing CpG sequences. GPI, glycosylphosphatidylinisotol; LPS, lipopolysaccharide. PMID; 18049472, 17190786 Other nucleic acids such as ssRNA, acting through TLR7 and TLR8, and bacterial oligodeoxyribonucleotides, acting through TLR9, are also potent inducers. PMID: 18049472 They also function as dimers and recognize double-stranded (ds) RNA, single-stranded (ss) RNA or dsDNA containing CpG sequences. GPI, glycosylphosphatidylinisotol; LPS, lipopolysaccharide. PMID: 18049472 TLR3 recognizes dsRNA in the lumen of the endosome, which causes phosphorylation of specific tyrosine residues in TLR3 by an unidentified protein tyrosine kinase (PTK). PMID: 18049472 TLR3 dimerizes, binds to CD14 and activates the signalling complex assembled by TLR adaptor molecule 1 (TRIF). PMID: 18049472 TLR3 dimerizes, binds to CD14 and activates the signalling complex assembled by TLR adaptor molecule 1 (TRIF). PMID: 18049472 Two major pathways bifurcate from TRIF. One, composed of tumour necrosis factor (TNF) receptor-associated factor 3 (TRAF3) and TANK-binding kinase (TBK1/IKKE), leads to phosphorylation of the transcription factor IFN regulatory factor 3 (IRF3). PMID: 18049472 Two major pathways bifurcate from TRIF. One, composed of tumour necrosis factor (TNF) receptor-associated factor 3 (TRAF3) and TANK-binding kinase (TBK1/IKKE), leads to phosphorylation of the transcription factor IFN regulatory factor 3 (IRF3). PMID: 18049472, 16979567 IRFs are activated by the kinases TBK1 or IKK-epsilon activated IRFs then dimerize and translocate to the nucleus. PMID: 18049472 Two major pathways bifurcate from TRIF. One, composed of tumour necrosis factor (TNF) receptor-associated factor 3 (TRAF3) and TANK-binding kinase (TBK1/IKKE), leads to phosphorylation of the transcription factor IFN regulatory factor 3 (IRF3). PMID: 18049472 IRF3 requires further phosphorylation by the phosphatidylinositol 3-kinase (P13K)/AKT pathway for its full activation, which is initiated by binding PI3K to phosphorylated TLR3. PMID: 18049472 IRF3 requires further phosphorylation by the phosphatidylinositol 3-kinase (P13K)/AKT pathway for its full activation, which is initiated by binding PI3K to phosphorylated TLR3. PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. Indirect PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. Indirect PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The IKK protein kinase complex phosphorylates IkappaB and releases it from NFkappaB. PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The IKK protein kinase complex phosphorylates IkappaB and releases it from NFkappaB. Indirect PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. Indirect PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. Indirect PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect PMID: 18049472 The other branch acts through TRAF6 and transforming growth factor-beta-activated kinase 1 (TAK1; also known as MAP3K7) leading to the activation of nuclear factor-kappaB (NFkappaB), JUN and activating transcription factor 2 (ATF2) transcription factors. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 The activated transcription factors translocate from the cytoplasm to the nucleus, bind to the cognate sites in the promoters of the target genes and singly or in combinations induce their transcription. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472, 16762830 Both TRIF and IPS1 recruit inhibitor of nuclear factor-kappaB (NFkappaB) kinase (IKK) and TANK-binding kinase (TBK1), the common activator kinases. PMID: 18049472, 16979567 IRFs are activated by the kinases TBK1 or IKK-epsilon activated IRFs then dimerize and translocate to the nucleus. PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472, 16979567 IRFs are activated by the kinases TBK1 or IKK-epsilon activated IRFs then dimerize and translocate to the nucleus. Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. Indirect PMID: 18049472 IPS1 functions like TRIF and activates the same transcription factors leading to the induction of similar genes. PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. Indirect PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. Indirect PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. Indirect PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. Indirect PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. Indirect PMID: 18049472, 16762830 Both TRIF and IPS1 recruit inhibitor of nuclear factor-kappaB (NFkappaB) kinase (IKK) and TANK-binding kinase (TBK1), the common activator kinases. Indirect PMID: 18049472, 16762830 Both TRIF and IPS1 recruit inhibitor of nuclear factor-kappaB (NFkappaB) kinase (IKK) and TANK-binding kinase (TBK1), the common activator kinases. PMID: 18049472 Bacterial lipopolysaccharides induce IFNs through TLR4 and also recruit TRIF. Indirect PMID: 18049472 Bacterial lipopolysaccharides induce IFNs through TLR4 and also recruit TRIF. Indirect PMID: 18049472, 15710892 For example, a hepatitis C virus (HCV)-encoded protease can cleave IPS1 off the mitochondrial membrane and block RIG-I/MDA5-mediated signalling. PMID: 18049472, 17038589 NS1 protein of influenza viruses prevents establishment of an antiviral state through the interaction with RIG-I. PMID: 18049472, 11812998 the quinolinamine imiquimod and its analogues activate TLR7. Indirect PMID: 18049472, 17562815 DMXAA induces IFN synthesis through a TLR-independent pathway. Indirect PMID: 18049472, 14991609 stimulation of TLR3 or TLR4 induces mostly IFN-beta and IFN-alpha1, which emphasizes the differences in the promoter sequences for the IFN-alphas, IFN-omega, and IFN-beta genes that govern the response to different inducers. Indirect PMID: 18049472, 14991609 stimulation of TLR3 or TLR4 induces mostly IFN-beta and IFN-alpha1, which emphasizes the differences in the promoter sequences for the IFN-alphas, IFN-omega, and IFN-beta genes that govern the response to different inducers. Indirect PMID: 18049472, 14991609 stimulation of TLR3 or TLR4 induces mostly IFN-beta and IFN-alpha1, which emphasizes the differences in the promoter sequences for the IFN-alphas, IFN-omega, and IFN-beta genes that govern the response to different inducers. Indirect PMID: 18049472, 14991609 stimulation of TLR3 or TLR4 induces mostly IFN-beta and IFN-alpha1, which emphasizes the differences in the promoter sequences for the IFN-alphas, IFN-omega, and IFN-beta genes that govern the response to different inducers. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2. PMID: 18049472, 17969444 They act through a cell-surface receptor composed of two ubiquitously expressed transmembrane proteins, IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2 (the genes for which are clustered on chromosome 21), and are associated with two cytoplasmic tyrosine kinases, TYK2 and JAK1. PMID: 18049472, 17969444 Formation of the IFN–receptor complex involves one side of the IFN protein interacting with IFNAR2 in a region forming the hinge between the two fibronectin type III (FnIII) domains (Fig. 3); binding affinity is in the nanomolar range39. IFNAR1 binds IFNs with an affinity 1,000-fold weaker than that of IFNAR2, with a binding site located opposite to the IFNAR2 binding site. Binding studies are consistent with the ternary complex between IFNAR1, IFN and IFNAR2 having a 1:1:1 stoichiometry, and a similar if not identical architecture for all type I IFNs. Ternary complex assembly is a two-step process; the ligand binds first to one IFNAR and then recruits the second with no identified interaction between the two IFNARs. PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2; type II IFN-gamma with IFN-gamma receptor 1 (IFNGR1) and IFNGR2; and type III IFN-lambdas with IFN-lambda receptor 1 (IFNLR1; also known as IL28RA) and interleukin 10 receptor 2 (IL10R2; also known as IL10RB). PMID; 18049472 Type II IFN-gamma is an antiparallel homodimer exhibiting a two-fold axis of symmetry. It binds two IFNGR1 receptor chains, assembling a complex that is stabilized by two IFNGR2 chains. PMID: 18049472 Type II IFN-gamma is an antiparallel homodimer exhibiting a two-fold axis of symmetry. It binds two IFNGR1 receptor chains, assembling a complex that is stabilized by two IFNGR2 chains. These receptors are associated with two kinases from the JAK family: JAK1 and TYK2 for type I and III IFNs; JAK1 and JAK2 for type II IFN. PMID: 18049472 IFN-gamma receptor 1 (IFNGR1) maps to chromosome 6 and has a JAK1 binding domain and a STAT1 docking site. IFNGR2 contains a JAK2 binding domain and maps to chromosome 21q22.1 in a cluster that also contains IFNAR1, IFNAR2 and interleukin 10 receptor 2 (IL10R2; also known as IL10RB). PMID: 18049472 Type I interferons (IFNs) (alpha, beta omega, kappa, epsilon, delta (pigs), tau (ruminants)) interact with IFN (alpha, beta and omega) receptor 1 (IFNAR1) and IFNAR2; type II IFN-gamma with IFN-gamma receptor 1 (IFNGR1) and IFNGR2; and type III IFN-lambdas with IFN-lambda receptor 1 (IFNLR1; also known as IL28RA) and interleukin 10 receptor 2 (IL10R2; also known as IL10RB). PMID: 18049472 These receptors are associated with two kinases from the JAK family: JAK1 and TYK2 for type I and III IFNs. Indirect PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. Indirect PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. Indirect PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472 Minimum requirements for a response to type I IFNs are the heterodimeric IFN receptor; the tyrosine kinases TYK2 and JAK1, which reciprocally transphosphorylate the receptor chains when activated. PMID: 18049472, 15284232 STAT1 and STAT3 bind competitively to the same phosphotyrosine residue of IFNGR1, with the binding of STAT1 greatly favoured. PMID: 18049472 Upon activation of receptors, the JAKs undergo autophosphorylation and transphosphorylation to increase their activity, and then phosphorylate the IFN receptors and finally STATs. PMID: 18049472, 12169689 In at least some cell types, the p85 subunit of phosphatidylinositol 3-kinase (PI3K) is associated with IFNAR1. The activation of p85 by IFN leads to AKT phosphorylation and expression of the chemokine (C-X-C motif) ligand 11 (CXCL11) gene, encoding an important chemokine. Indirect PMID: 18049472, 12169689 In at least some cell types, the p85 subunit of phosphatidylinositol 3-kinase (PI3K) is associated with IFNAR1. The activation of p85 by IFN leads to AKT phosphorylation and expression of the chemokine (C-X-C motif) ligand 11 (CXCL11) gene, encoding an important chemokine. Indirect PMID: 18049472, 12169689 In at least some cell types, the p85 subunit of phosphatidylinositol 3-kinase (PI3K) is associated with IFNAR1. The activation of p85 by IFN leads to AKT phosphorylation and expression of the chemokine (C-X-C motif) ligand 11 (CXCL11) gene, encoding an important chemokine. PMID: 18049472, 9625760, 2115167, 8798467 As examples, three closely related chemokines involved in accumulation of activated T cells and macrophages are the ISGs CXCL9 (also known as MIG, monokine induced by IFN-gamma); CXCL10 (also known as IP-10, IFN-gamma 10 kD inducible protein); and CXCL11 (also known as I-TAC, interferon-inducible T-cell alpha-chemoattractant)136, 137, 138, 139. True to their names, these chemokines are not expressed in the absence of IFN signalling. PMID: 18049472, 12169689 In at least some cell types, the p85 subunit of phosphatidylinositol 3-kinase (PI3K) is associated with IFNAR1. The activation of p85 by IFN leads to AKT phosphorylation and expression of the chemokine (C-X-C motif) ligand 11 (CXCL11) gene, encoding an important chemokine. PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. Indirect PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. PMID: 18049472, 9625760, 2115167, 8798467 As examples, three closely related chemokines involved in accumulation of activated T cells and macrophages are the ISGs CXCL9 (also known as MIG, monokine induced by IFN-gamma); CXCL10 (also known as IP-10, IFN-gamma 10 kD inducible protein); and CXCL11 (also known as I-TAC, interferon-inducible T-cell alpha-chemoattractant)136, 137, 138, 139. True to their names, these chemokines are not expressed in the absence of IFN signalling. Indirect PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. Indirect PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. PMID: 18049472, 17969446 Serine 727 of STAT1 is phosphorylated in response to IFN-gamma by the kinase cascade PI3K—AKT—PKC—MKK4—p38 (MKK4, mitogen-activated protein kinase kinase 4; also known as MAP2K4), with some variation in the activation of different PKC or MKK proteins in different cells. Indirect PMID: 18049472, 17969446 Serine 727 of STAT1 is phosphorylated in response to IFN-gamma by the kinase cascade PI3K—AKT—PKC—MKK4—p38 (MKK4, mitogen-activated protein kinase kinase 4; also known as MAP2K4), with some variation in the activation of different PKC or MKK proteins in different cells. PMID: 18049472, 17969446 Serine 727 of STAT1 is phosphorylated in response to IFN-gamma by the kinase cascade PI3K—AKT—PKC—MKK4—p38 (MKK4, mitogen-activated protein kinase kinase 4; also known as MAP2K4), with some variation in the activation of different PKC or MKK proteins in different cells. Indirect PMID: 18049472, 17969446 Serine 727 of STAT1 is phosphorylated in response to IFN-gamma by the kinase cascade PI3K—AKT—PKC—MKK4—p38 (MKK4, mitogen-activated protein kinase kinase 4; also known as MAP2K4), with some variation in the activation of different PKC or MKK proteins in different cells. PMID: 18049472 IFN-dependent activation of PI3K, extracellular response kinases (ERKs) and p38 stimulates the phosphorylation of NFkappaB (but not IkappaB), AP-1 and possibly PU.1, respectively. PMID: 18049472 IFN-dependent activation of PI3K, extracellular response kinases (ERKs) and p38 stimulates the phosphorylation of NFkappaB (but not IkappaB), AP-1 and possibly PU.1, respectively. Indirect PMID: 18049472 IFN-dependent activation of PI3K, extracellular response kinases (ERKs) and p38 stimulates the phosphorylation of NFkappaB (but not IkappaB), AP-1 and possibly PU.1, respectively. PMID: 18049472 IFN-dependent activation of PI3K, extracellular response kinases (ERKs) and p38 stimulates the phosphorylation of NFkappaB (but not IkappaB), AP-1 and possibly PU.1, respectively. Indirect PMID: 18049472 IFN-dependent activation of PI3K, extracellular response kinases (ERKs) and p38 stimulates the phosphorylation of NFkappaB (but not IkappaB), AP-1 and possibly PU.1, respectively. PMID: 18049472 IFN-dependent activation of PI3K, extracellular response kinases (ERKs) and p38 stimulates the phosphorylation of NFkappaB (but not IkappaB), AP-1 and possibly PU.1, respectively. Indirect PMID: 18049472, 15032587 SOCS inhibit receptor signalling both by directly inhibiting JAKs and by targeting the receptor complex for proteasomal degradation. Indirect PMID: 18049472, 15032587 SOCS inhibit receptor signalling both by directly inhibiting JAKs and by targeting the receptor complex for proteasomal degradation. Indirect PMID: 18049472, 15032587 SOCS inhibit receptor signalling both by directly inhibiting JAKs and by targeting the receptor complex for proteasomal degradation. Indirect PMID: 18049472 STAT1 is activated in response to both type I and type II IFNs and STAT3 is activated in response to gp130 cytokines such as IL6. PMID: 18049472, 17510282 For example, unphosphorylated STAT3 activates a subset of kappaB-dependent genes by forming a complex with NFkappaB. Indirect PMID: 18049472, 272640 Viral dsRNA can directly activate one of several human OAS proteins to produce a unique 2'-to-5' linked oligoadenylate of 3–6 bases (2–5A) from ATP. Indirect PMID: 18049472, 272640 Viral dsRNA can directly activate one of several human OAS proteins to produce a unique 2'-to-5' linked oligoadenylate of 3–6 bases (2–5A) from ATP. PMID: 18049472, 7876164, 6162102, 6165080 2–5A binding to RNASEL induces monomeric, inactive RNASEL to dimerize into a potent endoribonuclease that cleaves single-stranded regions of RNA on the 3' side of UpUp and UpAp dinucleotides. PMID: 18049472, 7876164, 6162102, 6165080 2–5A binding to RNASEL induces monomeric, inactive RNASEL to dimerize into a potent endoribonuclease that cleaves single-stranded regions of RNA on the 3' side of UpUp and UpAp dinucleotides. PMID: 18049472, 7680958 The only well-established function of 2–5A is activation of the ubiquitous, latent enzyme, RNASEL. Indirect PMID: 18049472, 7876164, 6162102, 6165080 2–5A binding to RNASEL induces monomeric, inactive RNASEL to dimerize into a potent endoribonuclease that cleaves single-stranded regions of RNA on the 3' side of UpUp and UpAp dinucleotides. PMID: 18049472, 17804500 The OAS–RNASEL pathway can inhibit the replication of encephalomyocarditis virus, Coxsackie virus B4, West Nile virus, some retroviruses and HCV. Indirect PMID: 18049472, 9351818, 10200477, 9294150 Furthermore, degradation of cellular mRNA and rRNA by RNASEL damages the host cell machinery that is required for viral replication and can result in apoptosis, contributing to both antiviral and antitumour actions. Indirect PMID: 18049472, 17653195 RNASEL also cleaves self-RNA into small degradation products that activate the recognition receptors, RIG-I and MDA5, to induce IFN-beta, similar to that of non-self viral RNA90, thus perpetuating and amplifying the production of IFN-beta. Indirect Indirect PMID: 18049472, 17653195 RNASEL also cleaves self-RNA into small degradation products that activate the recognition receptors, RIG-I and MDA5, to induce IFN-beta, similar to that of non-self viral RNA90, thus perpetuating and amplifying the production of IFN-beta. Indirect PMID: 18049472, 17653195 RNASEL also cleaves self-RNA into small degradation products that activate the recognition receptors, RIG-I and MDA5, to induce IFN-beta, similar to that of non-self viral RNA90, thus perpetuating and amplifying the production of IFN-beta. Indirect Indirect PMID: 18049472, 17653195 RNASEL also cleaves self-RNA into small degradation products that activate the recognition receptors, RIG-I and MDA5, to induce IFN-beta, similar to that of non-self viral RNA90, thus perpetuating and amplifying the production of IFN-beta. Indirect Indirect PMID: 18049472, 17653195 RNASEL also cleaves self-RNA into small degradation products that activate the recognition receptors, RIG-I and MDA5, to induce IFN-beta, similar to that of non-self viral RNA90, thus perpetuating and amplifying the production of IFN-beta. Indirect PMID: 18049472, 1004583, 283387 The dsRNA-activated protein kinase (PKR) and OAS were the first enzymes identified that uniquely respond to IFNs. Indirect PMID: 18049472, 9687506 In addition, the cellular protein PACT (also known as PRKRA) activates PKR in the absence of dsRNA. PMID: 18049472 PKR mediates translational control by phosphorylating the protein synthesis initiation factor EIF2alpha, resulting in an inactive complex between EIF2–GDP and the recycling factor, EIF2B. PMID: 18049472 PKR mediates translational control by phosphorylating the protein synthesis initiation factor EIF2alpha, resulting in an inactive complex between EIF2–GDP and the recycling factor, EIF2B. PMID: 18049472 p56 and p54 bind to different subunits of EIF3 and block some of its diverse functions. PMID: 18049472 p56 and p54 bind to different subunits of EIF3 and block some of its diverse functions. Indirect Indirect PMID: 18048472, 10224285, 11410525, 11568006 TRAIL/APO2L is an ISG that contributes to apoptosis and therefore probably to both the antiviral and antitumour effects of IFNs. Indirect PMID: 18049472, 15685448 Although many ISGs promote apoptosis, some promote cell survival. For example, the ISG G1P3 (or 6–16)116, 117 localizes to mitochondria and has anti-apoptotic actions, including inhibition of caspase-3. Indirect PMID: 18049472, 17579067 MHC class II proteins are selectively upregulated by IFN-gamma, whereas type I IFNs fail to do so owing to the STAT2-dependent induction of SOCS1. Indirect PMID: 18049472, 17579067 MHC class II proteins are selectively upregulated by IFN-gamma, whereas type I IFNs fail to do so owing to the STAT2-dependent induction of SOCS1. Indirect PMID: 18049472 IFNs also promote accumulation of leukocytes at sites of pathogen invasion; specifically, IFNs (along with cytokines such as TNFalpha and IL1beta), strongly promote the expression of vascular adhesion molecules including intracellular adhesion molecule 1 (ICAM1). Indirect PMID: 18049472 IFNs also promote accumulation of leukocytes at sites of pathogen invasion; specifically, IFNs (along with cytokines such as TNFalpha and IL1beta), strongly promote the expression of vascular adhesion molecules including intracellular adhesion molecule 1 (ICAM1). Indirect PMID: 18049472 IFNs also promote accumulation of leukocytes at sites of pathogen invasion; specifically, IFNs (along with cytokines such as TNFalpha and IL1beta), strongly promote the expression of vascular adhesion molecules including intracellular adhesion molecule 1 (ICAM1). PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. Indirect PMID: 18049472, 9625760, 2115167, 8798467 As examples, three closely related chemokines involved in accumulation of activated T cells and macrophages are the ISGs CXCL9 (also known as MIG, monokine induced by IFN-gamma); CXCL10 (also known as IP-10, IFN-gamma 10 kD inducible protein); and CXCL11 (also known as I-TAC, interferon-inducible T-cell alpha-chemoattractant)136, 137, 138, 139. True to their names, these chemokines are not expressed in the absence of IFN signalling. Indirect PMID: 18049472 As one example, an IFN-beta ISG product, CD69, forms an inhibitory association with a sphingosine 1-phosphate receptor (S1PR). PMID: 18049472, 9153530, 9007090, 9007089 Reduction in expression of matrix metalloproteinase 9 (MMP9) in activated lymphocytes and increased soluble vascular cell adhesion molecule (sVCAM) levels in plasma have also been identified and assigned putative roles in the beneficial effects of IFN-beta for patients with MS. Indirect PMID: 18049472, 9153530, 9007090, 9007089 Reduction in expression of matrix metalloproteinase 9 (MMP9) in activated lymphocytes and increased soluble vascular cell adhesion molecule (sVCAM) levels in plasma have also been identified and assigned putative roles in the beneficial effects of IFN-beta for patients with MS. Indirect PMID: 18049472, 12766484, 14977850 Induction of apoptosis by the ISG products APO2L/TRAIL and Fas has been identified in many malignant cell types, as has induction of APO2L/TRAIL on immune effector cell surfaces, thus sensitizing tumour cells to T-cell, NK cell and macrophage-mediated cytotoxicity. Indirect PMID: 18049472, 10417772, 12171874 Intralesional administration of IFN-alpha into basal cell carcinomas increased Fas expression and correlated with regression244. IFN-gamma has increased susceptibility to apoptosis by Fas activators and cytotoxic chemotherapies in many cell types including melanoma and colorectal carcinoma. PMID: 18049472, 12029096, 16909101 Through interactions with p53 and the inhibitor of apoptosis, XIAP, the ISG product XAF1 may allow APO2L/TRAIL to fully activate downstream caspases. Indirect PMID: 18049472, 12029096, 16909101 Through interactions with p53 and the inhibitor of apoptosis, XIAP, the ISG product XAF1 may allow APO2L/TRAIL to fully activate downstream caspases. Indirect Indirect PMID: 18049472, 12029096, 16909101 Through interactions with p53 and the inhibitor of apoptosis, XIAP, the ISG product XAF1 may allow APO2L/TRAIL to fully activate downstream caspases. Indirect PMID: 18049472, 1569446 In addition, IFN-gamma can upregulate the tumour-associated antigens, carcinoembryonic antigen and TAG72, both in vitro and in vivo. Indirect PMID: 18049472, 1569446 In addition, IFN-gamma can upregulate the tumour-associated antigens, carcinoembryonic antigen and TAG72, both in vitro and in vivo. Indirect PMID: 18049472, 1569446 In addition, IFN-gamma can upregulate the tumour-associated antigens, carcinoembryonic antigen and TAG72, both in vitro and in vivo. PMID: 18049472, 12644537 IFNs also inhibit vascular endothelial growth factor (VEGF) mRNA and protein expression by regulating its promoter. PMID: 18049472, 12644537 IFNs also inhibit vascular endothelial growth factor (VEGF) mRNA and protein expression by regulating its promoter. PMID: 18049472, 12881412 In endothelial cells, the ISG product guanylate binding protein 1, interferon-inducible, 67 kDa (GBP1), functioned as an inflammatory response factor inhibiting endothelial cell proliferation and angiogenesis in part through MMPs. PMID: 18049472, 14607926 Type I IFNs also activate p38, and inactivation of p38 blocks induction by IFN-beta of CXCL11 and TNFSF10 (encoding tumour necrosis factor-related apoptosis-inducing ligand, APO2L/TRAIL)68 and of CXCL10 (encoding the chemokine IP-10; also known as IFN-gamma-induced peptide, 10 kDa) in primary leukocytes. PMID: 18049472 In addition, they cause apoptosis by activating caspases 8 and 10 through the interaction of FADD with IPS1. PMID: 18049472, 17969446 Serine 727 of STAT1 is phosphorylated in response to IFN-gamma by the kinase cascade PI3K—AKT—PKC—MKK4—p38 (MKK4, mitogen-activated protein kinase kinase 4; also known as MAP2K4), with some variation in the activation of different PKC or MKK proteins in different cells. PMID: 18049472, 17969446 Serine 727 of STAT1 is phosphorylated in response to IFN-gamma by the kinase cascade PI3K—AKT—PKC—MKK4—p38 (MKK4, mitogen-activated protein kinase kinase 4; also known as MAP2K4), with some variation in the activation of different PKC or MKK proteins in different cells. PMID: 18049472 IRF3 requires further phosphorylation by the phosphatidylinositol 3-kinase (P13K)/AKT pathway for its full activation, which is initiated by binding PI3K to phosphorylated TLR3.