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PMID: 15950447 TLR4 recognizes bacterial LPS.

PMID: 15950447 TLR3 recognizes viral dsRNA.

PMID: 15950447 Structures and ligands for Toll-like receptors. TLR2, in collaboration with TLR1 or TLR6, discriminates between the molecular structures of triacyl and diacyl lipopeptides, respectively.

PMID: 15950447 Structures and ligands for Toll-like receptors. TLR2, in collaboration with TLR1 or TLR6, discriminates between the molecular structures of triacyl and diacyl lipopeptides, respectively.

PMID: 15950447, 12524386 All TLRs possess amino-terminal leucine-rich repeats, which are responsible for the recognition of PAMPs, and also possess a carboxy-terminal Toll–interleukin-1 (IL-1) receptor (TIR) domain, which is required for initiating intracellular signaling.

PMID: 15950447 TLR5 recognizes bacterial flagellin.

PMID: 15950447 TLR11 recognizes uropathigenic bacteria products.

PMID: 15950447 TLR9 recognizes bacterial and viral CpG DNA motifs.

PMID: 15950447 TLR9 also recognizes non-nucleic acids, such as hemozoin.

PMID: 15950447 TLR3, TLR7, TLR8 and TLR9 reside in endosomal compartments and recognize nucleic acids; TLR3 recognizes viral dsRNA, whereas TLR7 and TLR8 recognize viral ssRNA.

PMID: 15950447 TLR3, TLR7, TLR8 and TLR9 reside in endosomal compartments and recognize nucleic acids; TLR3 recognizes viral dsRNA, whereas TLR7 and TLR8 recognize viral ssRNA.

PMID: 15950447, 12524386, 10549626 TLR2 recognizes peptidoglycan, in addition to the lipoproteins and lipopeptides of Gram-positive bacteria and mycoplasma lipopeptide.

PMID: 15950447, 12524386, 10549626 TLR2 recognizes peptidoglycan, in addition to the lipoproteins and lipopeptides of Gram-positive bacteria and mycoplasma lipopeptide.

PMID: 15950447, 12524386, 10549626 TLR2 recognizes peptidoglycan, in addition to the lipoproteins and lipopeptides of Gram-positive bacteria and mycoplasma lipopeptide.

PMID: 15950447, 12719479 Innate immune responses against zymosan, a cell-wall preparation of yeast, are mediated by the collaborative recognition of TLR2 and dectin-1, a lectin family of receptors for beta-glucans.

PMIID: 15950447, 15690042 CD36, a class II scavenger receptor expressed on the surface of innate immune cells, is involved in sensing some, but not all, TLR2 ligands.

Indirect

PMID: 15950447 Signaling through dectin-1 enhanced the TLR2-mediated transcription of target genes.

PMID: 15950447, 12032557 TLR8 is a close relative of TLR7, and a transfection study has demonstrated that human, but not mouse, TLR8 confers responsiveness to resiquimod.

PMID: 15950447 Synthetic imidazoquinoline-like molecules imiquimod (R-837) and resiquimod (R-848), and guanosine analogs such as loxoribine, have potent antiviral activities and are currently used for treating viral infections. PMID: 15950447 Taken together, these findings indicate that mouse TLR7, human TLR7 and human TLR8 mediate the recognition of these molecules.

PMID: 15950447 Synthetic imidazoquinoline-like molecules imiquimod (R-837) and resiquimod (R-848), and guanosine analogs such as loxoribine, have potent antiviral activities and are currently used for treating viral infections. PMID: 15950447 Taken together, these findings indicate that mouse TLR7, human TLR7 and human TLR8 mediate the recognition of these molecules.

PMID: 15950447 Synthetic imidazoquinoline-like molecules imiquimod (R-837) and resiquimod (R-848), and guanosine analogs such as loxoribine, have potent antiviral activities and are currently used for treating viral infections. PMID: 15950447 Taken together, these findings indicate that mouse TLR7, human TLR7 and human TLR8 mediate the recognition of these molecules.

PMID: 15950447 Synthetic imidazoquinoline-like molecules imiquimod (R-837) and resiquimod (R-848), and guanosine analogs such as loxoribine, have potent antiviral activities and are currently used for treating viral infections. PMID: 15950447 Taken together, these findings indicate that mouse TLR7, human TLR7 and human TLR8 mediate the recognition of these molecules.

PMID: 15950447 Synthetic imidazoquinoline-like molecules imiquimod (R-837) and resiquimod (R-848), and guanosine analogs such as loxoribine, have potent antiviral activities and are currently used for treating viral infections. PMID: 15950447 Taken together, these findings indicate that mouse TLR7, human TLR7 and human TLR8 mediate the recognition of these molecules.

PMID: 15950447, 15558055 TLR3 also mediates the recognition of West Nile virus (WNV).

PMID: 15950447 MyD88 is utilized by all TLRs, with the exception of TLR3.

PMID: 15950447 The association of TLRs and MyD88 recruits members of the IL-1 receptor-associated kinase (IRAK) family; two members, IRAK4 and IRAK1, are sequentially phosphorylated, causing them to dissociate from the receptor complex, and then associate with TRAF6.

PMID: 15950447 The association of TLRs and MyD88 recruits members of the IL-1 receptor-associated kinase (IRAK) family; two members, IRAK4 and IRAK1, are sequentially phosphorylated, causing them to dissociate from the receptor complex, and then associate with TRAF6.

PMID: 15950447 The association of TLRs and MyD88 recruits members of the IL-1 receptor-associated kinase (IRAK) family; two members, IRAK4 and IRAK1, are sequentially phosphorylated, causing them to dissociate from the receptor complex, and then associate with TRAF6.

PMID: 15950447 The association of TLRs and MyD88 recruits members of the IL-1 receptor-associated kinase (IRAK) family; two members, IRAK4 and IRAK1, are sequentially phosphorylated, causing them to dissociate from the receptor complex, and then associate with TRAF6.

PMID: 15950447 The association of TLRs and MyD88 recruits members of the IL-1 receptor-associated kinase (IRAK) family; two members, IRAK4 and IRAK1, are sequentially phosphorylated, causing them to dissociate from the receptor complex, and then associate with TRAF6.

PMID: 15950447 TRAF6 forms a complex with ubiquitin-conjugating enzymes to activate the kinase TAK1, which in turn activates transcription factors nuclear factor (NF)-kappaB and activator protein-1 through the canonical IkappaB kinase (IKK) complex and the mitogen-activated protein kinase pathway, respectively.

Indirect

PMID: 15950447 TRAF6 forms a complex with ubiquitin-conjugating enzymes to activate the kinase TAK1, which in turn activates transcription factors nuclear factor (NF)-kappaB and activator protein-1 through the canonical IkappaB kinase (IKK) complex and the mitogen-activated protein kinase pathway, respectively.

Indirect

PMID: 15950447 TRAF6 forms a complex with ubiquitin-conjugating enzymes to activate the kinase TAK1, which in turn activates transcription factors nuclear factor (NF)-kappaB and activator protein-1 through the canonical IkappaB kinase (IKK) complex and the mitogen-activated protein kinase pathway, respectively.

Indirect

PMID: 15950447 TRAF6 forms a complex with ubiquitin-conjugating enzymes to activate the kinase TAK1, which in turn activates transcription factors nuclear factor (NF)-kappaB and activator protein-1 through the canonical IkappaB kinase (IKK) complex and the mitogen-activated protein kinase pathway, respectively.

Indirect

PMID: 15950447 TRAF6 forms a complex with ubiquitin-conjugating enzymes to activate the kinase TAK1, which in turn activates transcription factors nuclear factor (NF)-kappaB and activator protein-1 through the canonical IkappaB kinase (IKK) complex and the mitogen-activated protein kinase pathway, respectively.

PMID: 15950447, 15229469, 10435584 NF-kappaB activation by this ‘MyD88-dependent pathway’ results in the expression of inflammatory cytokine genes, including tumor necrosis factor-alpha, IL-6 and IL-1beta.

Indirect

PMID: 15950447, 15229469, 10435584 NF-kappaB activation by this ‘MyD88-dependent pathway’ results in the expression of inflammatory cytokine genes, including tumor necrosis factor-alpha, IL-6 and IL-1beta.

Indirect

PMID: 15950447, 15229469, 10435584 NF-kappaB activation by this ‘MyD88-dependent pathway’ results in the expression of inflammatory cytokine genes, including tumor necrosis factor-alpha, IL-6 and IL-1beta.

Indirect

PMID: 15950447, 15229469, 10435584 NF-kappaB activation by this ‘MyD88-dependent pathway’ results in the expression of inflammatory cytokine genes, including tumor necrosis factor-alpha, IL-6 and IL-1beta.

PMID: 15950447, 12447441, 12447442 Among these adapters, TIRAP–MAL is required for the activation of the MyD88-dependent pathway downstream of TLR2 and TLR4.

PMID: 15950447, 12447441, 12447442 Among these adapters, TIRAP–MAL is required for the activation of the MyD88-dependent pathway downstream of TLR2 and TLR4.

PMID: 15950447, 12447441, 12447442 Among these adapters, TIRAP–MAL is required for the activation of the MyD88-dependent pathway downstream of TLR2 and TLR4.

PMID: 15950447, 12447441, 12447442 Among these adapters, TIRAP–MAL is required for the activation of the MyD88-dependent pathway downstream of TLR2 and TLR4.

PMID: 15950447, 14556004 Additionally, TLR4 also requires another adaptor, TRAM, for IRF3 activation.

PMID: 15950447, 12855817, 12872135 It has been demonstrated that TRIF is responsible for TLR3- and TLR4-mediated IRF3 activation.

PMID: 15950447, 12855817, 12872135 It has been demonstrated that TRIF is responsible for TLR3- and TLR4-mediated IRF3 activation.

Indirect

PMID: 15950447, 12692549, 12702806 IRF3 activation occurs through the actions of the IKK-related kinases TRAF-family-member-associated NF-κB activator (TANK)-binding kinase 1 (TBK1) and IKKi (also called IKKvar epsilon), which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.

Indirect

PMID: 15950447, 12692549, 12702806 IRF3 activation occurs through the actions of the IKK-related kinases TRAF-family-member-associated NF-κB activator (TANK)-binding kinase 1 (TBK1) and IKKi (also called IKKvar epsilon), which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.

Indirect

PMID: 15950447, 12692549, 12702806 IRF3 activation occurs through the actions of the IKK-related kinases TRAF-family-member-associated NF-κB activator (TANK)-binding kinase 1 (TBK1) and IKKi (also called IKKvar epsilon), which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.

Indirect

PMID: 15950447, 12692549, 12702806 IRF3 activation occurs through the actions of the IKK-related kinases TRAF-family-member-associated NF-κB activator (TANK)-binding kinase 1 (TBK1) and IKKi (also called IKKvar epsilon), which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.

PMID: 15950447, 12692549, 12702806 IRF3 activation occurs through the actions of the IKK-related kinases TRAF-family-member-associated NF-κB activator (TANK)-binding kinase 1 (TBK1) and IKKi (also called IKKvar epsilon), which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.

Indirect

Indirect

PMID: 15950447, 12692549, 12702806 IRF3 activation occurs through the actions of the IKK-related kinases TRAF-family-member-associated NF-κB activator (TANK)-binding kinase 1 (TBK1) and IKKi (also called IKKvar epsilon), which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.

Indirect

PMID: 15950447, 11698465, 12855817 Stimulation of macrophages and DCs with LPS and dsRNA results in the activation of the transcription factor IFN regulatory factor 3 (IRF3) and subsequent induction of IFN-beta and IFN-inducible genes.

Indirect

PMID: 15950447, 11698465, 12855817 Stimulation of macrophages and DCs with LPS and dsRNA results in the activation of the transcription factor IFN regulatory factor 3 (IRF3) and subsequent induction of IFN-beta and IFN-inducible genes.

PMID: 15950447, 14530355 TRAF6 is also reported to bind TRIF and cooperatively activate NF-kappaB.

PMID: 15950447, 14530355, 15064760 Furthermore, TRIF interacts with two different protein kinases, TBK1 and receptor-interacting protein-1 (RIP1).

PMID: 15950447, 14530355 TRAF6 is also reported to bind TRIF and cooperatively activate NF-kappaB.

Indirect

PMID: 15950447, 11698465 However, cells doubly deficient in TRAF6 and MyD88 still partially activated NF-kappaB in response to LPS, suggesting that TRIF activates NF-kappaB through both TRAF6-dependent and -independent pathways in TLR4 signaling.

Indirect

PMID: 15950447 Thus, TRIF is likely to use TBK1 and RIP1 for IRF3- and NF-kappaB activation, respectively, in TLR3 signaling. PMID: 15950447 In cells lacking RIP1, TLR3-mediated NF-kappaB activation and the subsequent induction of Icam-1 was severely impaired, whereas IFNbeta induction was intact.

Indirect

PMID: 15950447, 11698465 However, cells doubly deficient in TRAF6 and MyD88 still partially activated NF-kappaB in response to LPS, suggesting that TRIF activates NF-kappaB through both TRAF6-dependent and -independent pathways in TLR4 signaling.

Indirect

PMID: 15950447 In cells lacking RIP1, TLR3-mediated NF-kappaB activation and the subsequent induction of Icam-1 was severely impaired, whereas IFNbeta induction was intact.

PMID: 15950447, 12626561 It appears that IFN-alpha induction by TLR7 and TLR9 depends entirely on MyD88.

PMID: 15950447, 12626561 It appears that IFN-alpha induction by TLR7 and TLR9 depends entirely on MyD88.

PMID: 15950447, 15361868, 15492225 IRF7 forms a signaling complex with MyD88 and TRAF6 in the cytoplasm.

PMID: 15950447, 15361868, 15492225 IRF7 forms a signaling complex with MyD88 and TRAF6 in the cytoplasm.

PMID: 15950447, 15361868, 15492225 IRF7 forms a signaling complex with MyD88 and TRAF6 in the cytoplasm.

PMID: 15950447, 15361868, 15492225 IRF7 forms a signaling complex with MyD88 and TRAF6 in the cytoplasm.

PMID: 15950447 Similar to IRF3, phosphorylation is required for the activation of IRF7. PMID: 15950447, 15767370 In this regard, IRAK1 has been demonstrated to serve as an IRF7 kinase, and in IRAK1-deficient mice, TLR7- and TLR9-induced IFN-alpha production was completely abolished, although inflammatory cytokines were produced.

PMID: 15950447 Similar to IRF3, phosphorylation is required for the activation of IRF7. PMID: 15950447, 15767370 In this regard, IRAK1 has been demonstrated to serve as an IRF7 kinase, and in IRAK1-deficient mice, TLR7- and TLR9-induced IFN-alpha production was completely abolished, although inflammatory cytokines were produced.

PMID: 15950447, 15361868, 15492225 After stimulation, IRF7 translocates into the nucleus to induce IFN-alpha.

Indirect

PMID: 15950447, 15361868, 15492225 After stimulation, IRF7 translocates into the nucleus to induce IFN-alpha.

Indirect

PMID: 15950447 Accordingly, pDCs respond to CpG DNA, by rapidly secreting large amounts of IFN-alpha. Synthesized ssRNA can also induce IFN-alpha via TLR7.

PMID: 15950447, 15665823, 15695821 More recently, IRF5 has been shown to be involved in a MyD88–TRAF6 complex.

PMID: 15950447, 15665823 Upon TLR ligand stimulation, IRF5 was shown to translocate to the nucleus from the cytoplasm and bind the potential IFN-stimulated response element (ISRE) motifs present in the promoter region of proinflammatory cytokine genes.

PMID: 15950447, 15665823 Upon TLR ligand stimulation, IRF5 was shown to translocate to the nucleus from the cytoplasm and bind the potential IFN-stimulated response element (ISRE) motifs present in the promoter region of proinflammatory cytokine genes.

PMID: 15950447 These observations indicate that IRF5 is a general signal transducer that mediates MyD88-dependent gene induction of proinflammatory cytokines, in contrast to IRF7, which requires MyD88-dependent IFN-alpha induction.

Indirect

PMID: 15950447, 15153500 In these cells, TLR9-stimulated NF-kappaB activation was unexpectedly impaired, suggesting that IRF8 mediates NF-kappaB activation in TLR9 signaling.

Indirect

PMID: 15950447, 15153500 In these cells, TLR9-stimulated NF-kappaB activation was unexpectedly impaired, suggesting that IRF8 mediates NF-kappaB activation in TLR9 signaling.

Indirect

PMID: 15950447, 14978071, 15067049 For example, various TLR2 ligands induce abundant IL-10 and favor Th2-biased immune responses both in human and mice, whereas ligands for TLR4, TLR5 and TLR9 induce Th1-associated cytokines, such as IL-12p70. PMID: 15950447 It was demonstrated that TLR2 ligands induce a higher phosphorylation of ERK and stabilization of the transcription factor c-Fos in DCs, which results in induction of IL-10 and suppression of IL-12p70.

Indirect

PMID: 15950447, 14978071, 15067049 For example, various TLR2 ligands induce abundant IL-10 and favor Th2-biased immune responses both in human and mice, whereas ligands for TLR4, TLR5 and TLR9 induce Th1-associated cytokines, such as IL-12p70. PMID: 15950447 It was demonstrated that TLR2 ligands induce a higher phosphorylation of ERK and stabilization of the transcription factor c-Fos in DCs, which results in induction of IL-10 and suppression of IL-12p70.

Indirect

PMID: 15950447, 14978071, 15067049 For example, various TLR2 ligands induce abundant IL-10 and favor Th2-biased immune responses both in human and mice, whereas ligands for TLR4, TLR5 and TLR9 induce Th1-associated cytokines, such as IL-12p70. PMID: 15950447 It was demonstrated that TLR2 ligands induce a higher phosphorylation of ERK and stabilization of the transcription factor c-Fos in DCs, which results in induction of IL-10 and suppression of IL-12p70.

Indirect

PMID: 15950447, 14978071, 15067049 For example, various TLR2 ligands induce abundant IL-10 and favor Th2-biased immune responses both in human and mice, whereas ligands for TLR4, TLR5 and TLR9 induce Th1-associated cytokines, such as IL-12p70. PMID: 15950447 It was demonstrated that TLR2 ligands induce a higher phosphorylation of ERK and stabilization of the transcription factor c-Fos in DCs, which results in induction of IL-10 and suppression of IL-12p70.

Indirect

PMID: 15950447 It was demonstrated that TLR2 ligands induce a higher phosphorylation of ERK and stabilization of the transcription factor c-Fos in DCs, which results in induction of IL-10 and suppression of IL-12p70.

Indirect

Indirect

PMID: 15950447 For example, intracellular introduction of dsRNA stimulates DCs lacking TLR3 to secrete type I IFN.

Indirect

PMID: 15950447, 12855817, 15210742 TRIF but does require TBK1 and IRF3.

PMID: 15950447, 15208624 Retinoic acid-inducible gene I has recently been identified as an intracellular sensor for dsRNA, and is composed of the RNA helicase domain, which binds dsRNA, and the caspase recruitment domain (CARD), which culminates in IRF3 activation.

Indirect

Indirect

PMID: 15950447, 15208624 Retinoic acid-inducible gene I has recently been identified as an intracellular sensor for dsRNA, and is composed of the RNA helicase domain, which binds dsRNA, and the caspase recruitment domain (CARD), which culminates in IRF3 activation. PMID: 15950447, 15549108 Fas-associated death domain (FADD) and RIP1 have been demonstrated to be involved in this pathway.

PMID: 15950447, 15476921 NOD1 and NOD2 recognize naturally occurring degradation products and minimal motifs of bacterial peptidoglycan.

PMID: 15950447, 15476921 NOD1 and NOD2 recognize naturally occurring degradation products and minimal motifs of bacterial peptidoglycan.

PMID: 15950447, 15476921 NOD1 and NOD2 recognize naturally occurring degradation products and minimal motifs of bacterial peptidoglycan.

PMID: 15950447, 15476921 NOD1 and NOD2 recognize naturally occurring degradation products and minimal motifs of bacterial peptidoglycan.