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indirect

PMID: 17502339 TLR signaling results in the downstream activation of three major families of proteins important in activating inflammatory gene expression: NF-{kappa}B/Rel proteins; IRFs; and MAPKs—the ERKs and the stress kinases JNK and p38.

indirect

PMID: 17502339 TLR signaling results in the downstream activation of three major families of proteins important in activating inflammatory gene expression: NF-{kappa}B/Rel proteins; IRFs; and MAPKs—the ERKs and the stress kinases JNK and p38.

indirect

PMID: 17502339 TLR signaling results in the downstream activation of three major families of proteins important in activating inflammatory gene expression: NF-{kappa}B/Rel proteins; IRFs; and MAPKs—the ERKs and the stress kinases JNK and p38.

indirect

PMID: 17502339 TLR signaling results in the downstream activation of three major families of proteins important in activating inflammatory gene expression: NF-{kappa}B/Rel proteins; IRFs; and MAPKs—the ERKs and the stress kinases JNK and p38.

indirect

PMID: 17502339 TLR signaling results in the downstream activation of three major families of proteins important in activating inflammatory gene expression: NF-{kappa}B/Rel proteins; IRFs; and MAPKs—the ERKs and the stress kinases JNK and p38.

indirect

PMID: 17502339 NF-{kappa}B proteins are transcription factors whose nuclear translocation is triggered by TLR ligands, and NF-{kappa}B plays a key role in the transcriptional activation of multiple inflammatory genes.

PMID: 17502339 NF-{kappa}B proteins are transcription factors whose nuclear translocation is triggered by TLR ligands, and NF-{kappa}B plays a key role in the transcriptional activation of multiple inflammatory genes.

PMID: 17502339 IRFs are induced or activated by TLR ligation and are particularly important in driving Type I IFN production and downstream activation of IFN-inducible genes.

PMID: 17502339 IRFs are induced or activated by TLR ligation and are particularly important in driving Type I IFN production and downstream activation of IFN-inducible genes.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 MAPKs induce the expression of AP-1 family transcription factors such as Fos and Jun and activate the transcriptional activity of AP-1 proteins by phosphorylation of their transcription activation domains.

PMID: 17502339 AP-1 proteins have been implicated in invasive cell growth and matrix metalloprotease (MMP) production and in cell line models, have been suggested to mediate induction of inflammatory genes such as TNF-{alpha}.

PMID: 17502339 AP-1 proteins have been implicated in invasive cell growth and matrix metalloprotease (MMP) production and in cell line models, have been suggested to mediate induction of inflammatory genes such as TNF-{alpha}.

indirect

PMID: 17502339 AP-1 proteins have been implicated in invasive cell growth and matrix metalloprotease (MMP) production and in cell line models, have been suggested to mediate induction of inflammatory genes such as TNF-{alpha}.

PMID: 17502339, 15067049, 15123779 Fos actually suppresses the expression of IL-12.

indirect

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

indirect

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

indirect

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

indirect

indirect

indirect

indirect

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

indirect

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

indirect

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

PMID: 17502339, 11743587 MAPKs can activate Ets and CREB/activating transcription factor, stabilize mRNAs, which encode inflammatory cytokines, induce efficient translation of TNF-{alpha} mRNA, and lead to phosphorylation of histones at inflammatory gene loci

PMID: 17502339 Binding of IFN-{gamma} to its cell surface receptor leads to the activation of receptor-associated Jak protein tyrosine kinases, followed by tyrosine phosphorylation and activation of latent cytoplasmic proteins—STATs—which in turn, dimerize and translocate to the nucleus, where they bind to promoter sequences and activate transcription.

PMID: 17502339 Binding of IFN- to its cell surface receptor leads to the activation of receptor-associated Jak protein tyrosine kinases, followed by tyrosine phosphorylation and activation of latent cytoplasmic proteins—STATs—which in turn, dimerize and translocate to the nucleus, where they bind to promoter sequences and activate transcription.

PMID: 17502339 Binding of IFN-gamma to its cell surface receptor leads to the activation of receptor-associated Jak protein tyrosine kinases, followed by tyrosine phosphorylation and activation of latent cytoplasmic proteins—STATs—which in turn, dimerize and translocate to the nucleus, where they bind to promoter sequences and activate transcription. PMID: 17502339 IFN-{gamma} activates Stat1 predominantly, which mediates the activating functions of IFN-{gamma}, including enhanced microbial killing, increased antigen presentation, and enhanced inflammatory cytokine production.

PMID: 17502339 Binding of IFN-gamma to its cell surface receptor leads to the activation of receptor-associated Jak protein tyrosine kinases, followed by tyrosine phosphorylation and activation of latent cytoplasmic proteins—STATs—which in turn, dimerize and translocate to the nucleus, where they bind to promoter sequences and activate transcription.

PMID: 17502339 Binding of IFN- to its cell surface receptor leads to the activation of receptor-associated Jak protein tyrosine kinases, followed by tyrosine phosphorylation and activation of latent cytoplasmic proteins—STATs—which in turn, dimerize and translocate to the nucleus, where they bind to promoter sequences and activate transcription.

PMID: 17502339 Binding of IFN- to its cell surface receptor leads to the activation of receptor-associated Jak protein tyrosine kinases, followed by tyrosine phosphorylation and activation of latent cytoplasmic proteins—STATs—which in turn, dimerize and translocate to the nucleus, where they bind to promoter sequences and activate transcription.

PMID: 17502339 STAT transcriptional activity is potentiated by serine phosphorylation of transcription activation domains, which can be mediated by multiple kinases, including MAPKs, PKC, and calmodulin-dependent protein kinase II. PMID: 17502339 IFN-{gamma} activates Stat1 predominantly, which mediates the activating functions of IFN-{gamma}, including enhanced microbial killing, increased antigen presentation, and enhanced inflammatory cytokine production.

PMID: 17502339 STAT transcriptional activity is potentiated by serine phosphorylation of transcription activation domains, which can be mediated by multiple kinases, including MAPKs, PKC, and calmodulin-dependent protein kinase II. PMID: 17502339 IFN-{gamma} activates Stat1 predominantly, which mediates the activating functions of IFN-{gamma}, including enhanced microbial killing, increased antigen presentation, and enhanced inflammatory cytokine production.

PMID: 17502339 STAT transcriptional activity is potentiated by serine phosphorylation of transcription activation domains, which can be mediated by multiple kinases, including MAPKs, PKC, and calmodulin-dependent protein kinase II. PMID: 17502339 IFN-{gamma} activates Stat1 predominantly, which mediates the activating functions of IFN-{gamma}, including enhanced microbial killing, increased antigen presentation, and enhanced inflammatory cytokine production.

indirect

PMID: 17502339 IFN-{gamma}-induced increases in TLR and Fc{gamma}RI expression

indirect

PMID: 17502339 IFN-{gamma}-induced increases in TLR and Fc{gamma}RI expression

indirect

PMID: 17502339 IFN-gamma enhanced activation of NF-{kappa}B

indirect

PMID: 17502339 Stat1, which is activated by IFN-{gamma}, and Stat3, activated by IL-10, oppose each other’s activity in the regulation of inflammation PMID: 17502339, 16713974 We reported recently that IFN-{gamma} suppresses TLR-mediated induction of IL-10 expression and downstream Stat3 activation, thereby interrupting a TLR2-induced feedback inhibition loop

indirect

PMID: 17502339, 16571725 Pleiotropic cytokines such as Type I IFNs and IL-6 activate Stat1 and Stat3, and the balance between Stat1 and Stat3 activation by these cytokines can determine the balance of their pro- and anti-inflammatory functions.

indirect

indirect

PMID: 17502339, 16571725 Pleiotropic cytokines such as Type I IFNs and IL-6 activate Stat1 and Stat3, and the balance between Stat1 and Stat3 activation by these cytokines can determine the balance of their pro- and anti-inflammatory functions.

indirect

PMID: 17502339, 16571725 Pleiotropic cytokines such as Type I IFNs and IL-6 activate Stat1 and Stat3, and the balance between Stat1 and Stat3 activation by these cytokines can determine the balance of their pro- and anti-inflammatory functions.

indirect

indirect

indirect

PMID: 17502339 IFN-{alpha}-induced activation of Stat1 is amplified by the ITAM-containing adapters FcR{gamma} and DAP12 and the downstream kinase Syk, which can phosphorylate Stat1 directly or could phosphorylate IFNAR Stat1-docking sites.

PMID: 17502339 IFN-{alpha}-induced activation of Stat1 is amplified by the ITAM-containing adapters FcR{gamma} and DAP12 and the downstream kinase Syk, which can phosphorylate Stat1 directly or could phosphorylate IFNAR Stat1-docking sites.

PMID: 17502339 The shift in IFN-{alpha}-induced STAT activation toward increased Stat1 activation relative to Stat2 and Stat3 activation results in enhanced expression of Stat1-dependent inflammatory genes such as the chemokines CXCL9 and CXCL10 and a shift to a more inflammatory phenotype.

PMID: 17502339 The shift in IFN-{alpha}-induced STAT activation toward increased Stat1 activation relative to Stat2 and Stat3 activation results in enhanced expression of Stat1-dependent inflammatory genes such as the chemokines CXCL9 and CXCL10 and a shift to a more inflammatory phenotype.

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

indirect

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

indirect

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

indirect

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

indirect

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

indirect

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

indirect

PMID: 17502339 Ligation of the DAP12-associated, ITAM-coupled receptors TREM2 and SIRPβ1 by endogenous ligands, expressed on myeloid lineage osteoclast precursors, "costimulates" RANK signaling by regulating calcium oscillations, leading to expression and activation of NFATc1 and osteoclastogenesis

PMID: 17502339, 16715077 A recent, exciting discovery identified Semaphorin 6D as an endogenous ligand for a receptor complex containing plexin A1-TREM2-DAP12

PMID: 17502339 Consistent with intact MAPK activation, LPS-induced Fos and Jun mRNA expression was not inhibited in IFN-{gamma}-preactivated macrophages.

indirect

PMID: 17502339 Consistent with intact MAPK activation, LPS-induced Fos and Jun mRNA expression was not inhibited in IFN-{gamma}-preactivated macrophages.

indirect

PMID: 17502339 Consistent with intact MAPK activation, LPS-induced Fos and Jun mRNA expression was not inhibited in IFN-{gamma}-preactivated macrophages.

indirect

PMID: 17502339 Consistent with intact MAPK activation, LPS-induced Fos and Jun mRNA expression was not inhibited in IFN-{gamma}-preactivated macrophages.

indirect

PMID: 17502339, 16713974 We reported recently that IFN-{gamma} suppresses TLR-mediated induction of IL-10 expression and downstream Stat3 activation, thereby interrupting a TLR2-induced feedback inhibition loop

indirect

PMID: 17502339 The mechanism of inhibition of TLR2-induced IL-10 production involves attenuation of TLR2-induced MAPK activation, which results in diminished AP-1 (Fos and Jun) expression and diminished CREB phosphorylation on the transcription-activating site serine 13

PMID: 17502339 The mechanism of inhibition of TLR2-induced IL-10 production involves attenuation of TLR2-induced MAPK activation, which results in diminished AP-1 (Fos and Jun) expression and diminished CREB phosphorylation on the transcription-activating site serine 13

indirect

PMID: 17502339 In addition, IFN-{gamma} suppresses TLR2-induced Akt activity, which is linked with decreased phosphorylation and increased activity of GSK3β, which in turn, contributes to inhibition of AP-1 DNA binding, likely by phosphorylation of the Jun DNA-binding domain

PMID: 17502339 In addition, IFN-{gamma} suppresses TLR2-induced Akt activity, which is linked with decreased phosphorylation and increased activity of GSK3β, which in turn, contributes to inhibition of AP-1 DNA binding, likely by phosphorylation of the Jun DNA-binding domain

PMID: 17502339 IFN-{gamma} suppresses TLR2-induced Akt activity, linked with decreased phosphorylation and increased activity of GSK3β, which in turn, contributes to inhibition of AP-1 DNA binding.

indirect

PMID: 17502339, 16713974 Diminished AP-1 and CREB activity in IFN-{gamma}-primed, TLR2-activated cells leads to decreased expression of AP-1 and CREB target genes, including MMP-1 (collagenase), plasminogen activator inhibitor-2 (PAI-2), and IL-10

PMID: 17502339, 16713974 Diminished AP-1 and CREB activity in IFN-{gamma}-primed, TLR2-activated cells leads to decreased expression of AP-1 and CREB target genes, including MMP-1 (collagenase), plasminogen activator inhibitor-2 (PAI-2), and IL-10

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

indirect

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

indirect

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

indirect

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

indirect

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

indirect

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).

PMID: 17502339 ITAM-mediated signaling is initiated by Src family kinase phosphorylation of the two ITAM motif tyrosines, leading to the recruitment and activation of the PTK Syk and downstream signaling pathways, which include activation of PTKs, NF-{kappa}B, MAPKs, and protein kinase C (PKC) and calcium-mediated signaling pathways (via activation of phospholipase C{gamma}).