Original Literature | Model OverView |
---|---|
Publication
Title
TLR signaling.
Affiliation
Exploratory Research for Advanced Technology, Japan Science and TechnologyAgency, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan.
Abstract
The Toll-like receptor (TLR) family plays an instructive role in innate immuneresponses against microbial pathogens, as well as the subsequent induction ofadaptive immune responses. TLRs recognize specific molecular patterns found in abroad range of microbial pathogens such as bacteria and viruses, triggeringinflammatory and antiviral responses and dendritic cell maturation, which resultin the eradication of invading pathogens. Individual TLRs interact withdifferent combinations of adapter proteins and activate various transcriptionfactors such as nuclear factor (NF)-kappaB, activating protein-1 and interferonregulatory factors, driving a specific immune response. This review outlines therecent advances in our understanding of TLR-signaling pathways and their rolesin immune responses. Further, we also discuss a new concept of TLR-independentmechanisms for recognition of microbial pathogens.
PMID
16410796
|
Entity
RIP1
--
MO000000065
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m71
10
infinite
0
InterPro | IPR000198 |
TRANSPATH | MO000000065 |
--
MEK1{active}
--
MO000000078
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m70
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000078 |
--
IKK{active}
--
MO000000248
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m207
10
infinite
0
TRANSPATH | MO000000248 |
--
AP-1
--
MO000000276
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m219
10
infinite
0
TRANSPATH | MO000000276 |
--
IRF-5
--
MO000007700
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m979
10
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0
InterPro | IPR008984 |
TRANSPATH | MO000007700 |
--
MEK2{active}
--
MO000009393
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m1135
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000009393 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
MKK6{p}
--
MO000038355
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m16567
10
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0
TRANSPATH | MO000038355 |
--
IRAK-4
--
MO000039077
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m17258
10
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0
TRANSPATH | MO000039077 |
--
TRIF
--
MO000041125
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m18998
10
infinite
0
TRANSPATH | MO000041125 |
--
dsRNA:TLR3:TRIF
--
MO000041437
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19305
10
infinite
0
TRANSPATH | MO000041437 |
--
dsRNA:TLR3
--
MO000041446
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19314
10
infinite
0
TRANSPATH | MO000041446 |
--
TLR8(h)
--
MO000042006
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m155646
10
infinite
0
Affymetrix | 220832_at |
Ensembl | ENSG00000101916 |
HGNC | TLR8 |
OMIM | 300366 |
Proteome | HumanPSD/TLR8 |
RefSeq | NM_016610 |
TRANSPATH | MO000042006 |
Unigene | Hs.272410 |
UniProt | Q9NR97 |
--
--
e1
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane
--
--
--
csml-variable:Double
m1
0
infinite
0
--
--
e10
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytosol
--
--
--
csml-variable:Double
m10
0
infinite
0
--
TLR1:TLR2:triacyl lipopeptide
--
e11
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m11
0
infinite
0
--
TLR2:TLR6
--
e12
cso30:c:Complex
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--
csml-variable:Double
m12
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0
--
diacyl lipopeptide
--
e13
cso30:c:Protein
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--
--
csml-variable:Double
m13
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0
--
diacyl lipopeptide:TLR2:TLR6
--
e14
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m14
0
infinite
0
--
flagellin
--
e15
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m15
0
infinite
0
--
flagellin:TLR5
--
e16
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m16
0
infinite
0
--
csml-variable:Double
m17
0
infinite
0
--
loxoribine:TLR7
--
e18
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m18
0
infinite
0
--
ssRNA
--
e19
cso30:c:Rna
cso30:i:CC_Extracellular
--
csml-variable:Double
m19
0
infinite
0
--
--
e2
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m2
0
infinite
0
--
ssRNA:TLR7
--
e20
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m20
0
infinite
0
--
imidazoquinolines
--
e21
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m21
0
infinite
0
--
imidazoquinolines:TLR8(h)
--
e22
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m22
0
infinite
0
--
ssRNA:TLR8(h)
--
e23
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m23
0
infinite
0
--
csml-variable:Double
m24
0
infinite
0
--
CpG DNA:TLR9
--
e25
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m25
0
infinite
0
--
hemozoin
--
e26
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m26
0
infinite
0
--
hemozoin:TLR9
--
e27
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m27
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infinite
0
--
LPS:TLR4
--
e28
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m28
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infinite
0
--
IkappaB{p}:NF-kappaB
--
e29
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m29
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
IkappaB:NF-kappaB
--
e30
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m30
0
infinite
0
--
NF-kappaB
--
e31
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m31
0
infinite
0
--
protein remnants
--
e32
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m32
0
infinite
0
--
IkappaB{p}{ub}:NF-kappaB
--
e33
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m33
0
infinite
0
--
NF-kappaB
--
e34
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m34
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0
--
LPS:TLR4:TIRAP
--
e35
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m35
0
infinite
0
--
LPS:TLR4:TIRAP:MYD88
--
e36
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m36
0
infinite
0
--
LPS:TLR4:TIRAP:MYD88:IRAK-4
--
e37
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m37
0
infinite
0
--
IRAK1
--
e38
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m38
0
infinite
0
--
LPS:TLR4:TIRAP:MYD88:IRAK4:IRAK1
--
e39
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m39
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
LPS:TLR4:MYD88:IRAK4{p}:IRAK1{p}
--
e40
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m40
0
infinite
0
--
TRAF6{active}
--
e41
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m41
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000000212 |
--
Uev1A
--
e42
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m42
0
infinite
0
--
TRAF6:Ubc13:Uev1A
--
e43
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m43
0
infinite
0
--
TAB1:TAB2:TAB3:TAK1
--
e44
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m44
0
infinite
0
--
TAB1:TAB2:TAB3:TAK1
--
e45
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m45
0
infinite
0
--
TLR1:TLR2
--
e5
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m5
0
infinite
0
--
--
e50
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelopeLumen
--
--
--
csml-variable:Double
m50
0
infinite
0
--
--
e51
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearPore
--
--
--
csml-variable:Double
m51
0
infinite
0
--
--
e52
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearInnerMembrane
--
--
--
csml-variable:Double
m52
0
infinite
0
--
--
e53
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearLumen
--
--
--
csml-variable:Double
m53
0
infinite
0
--
--
e54
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearOuterMembrane
--
--
--
csml-variable:Double
m54
0
infinite
0
--
--
e55
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleus
--
--
--
csml-variable:Double
m55
0
infinite
0
--
--
e56
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleoplasm
--
--
--
csml-variable:Double
m56
0
infinite
0
--
--
e57
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearBody
--
--
--
csml-variable:Double
m57
0
infinite
0
--
--
e58
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleolus
--
--
--
csml-variable:Double
m58
0
infinite
0
--
--
e59
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelope
--
--
--
csml-variable:Double
m59
0
infinite
0
--
triacyl lipopeptide
--
e6
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m6
0
infinite
0
--
--
e60
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Chromatin
--
--
--
csml-variable:Double
m60
0
infinite
0
--
--
e61
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearChromosome
--
--
--
csml-variable:Double
m61
0
infinite
0
--
--
e62
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearCentromere
--
--
--
csml-variable:Double
m62
0
infinite
0
--
LPS:TLR4:TRAM
--
e65
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m68
0
infinite
0
--
LPS:TLR4:TRAM:TRIF
--
e66
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m69
0
infinite
0
--
dsRNA:TLR3:TRIF:RIP1
--
e67
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m72
0
infinite
0
--
NF-kappaB{active}
--
e68
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m73
0
infinite
0
--
dsRNA:TLR4:TRIF:TRAF6
--
e69
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m74
0
infinite
0
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
LPS:TLR4:TRAM:TRIF:TBK1
--
e70
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m75
0
infinite
0
--
LPS:TLR4:TRAM:TRIF:TBK1:IKK-i
--
e71
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m76
0
infinite
0
--
(IRF-3)2
--
e72
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m77
0
infinite
0
--
(IRF-3)2
--
e73
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m78
0
infinite
0
--
--
e74
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m79
0
infinite
0
--
--
e75
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
csml-variable:Double
m80
0
infinite
0
--
--
e76
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
csml-variable:Double
m81
0
infinite
0
--
CpG:TLR9:MYD88
--
e77
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m82
0
infinite
0
--
CpG:TLR9:MYD88:IRAK1:IRAK4:IRF7
--
e78
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m83
0
infinite
0
--
dsRNA:RIG-I:IPS1:FADD:RIP1
--
e79
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m84
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
CpG:TLR9:IRAK1:IRAK4:IRF7[p}
--
e80
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m85
0
infinite
0
--
CpG:TLR9:IRAK1:IRAK4:IRF7[p}{ub}
--
e81
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m86
0
infinite
0
--
(IRF7)2
--
e82
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m87
0
infinite
0
--
(IRF7)2
--
e83
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m88
0
infinite
0
--
IRF-5:MYD88
--
e84
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m89
0
infinite
0
--
RIG-I
--
e88
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m93
0
infinite
0
--
dsRNA:RIG-I
--
e89
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m94
0
infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0
infinite
0
--
LGP2
--
e90
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m95
0
infinite
0
--
dsRNA:LGP2
--
e91
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m96
0
infinite
0
--
Mda5
--
e92
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m97
0
infinite
0
--
dsRNA:Mda5
--
e93
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m98
0
infinite
0
--
csml-variable:Double
m99
0
infinite
0
--
dsRNA:RIG-I:IPS1
--
e95
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m100
0
infinite
0
--
dsRNA:Mda5:IPS1
--
e96
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m101
0
infinite
0
--
IPS1:TRAF6
--
e97
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m102
0
infinite
0
--
TRIF:IPS1
--
e98
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m103
0
infinite
0
--
e99
--
e99
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m104
0
infinite
0
--
p1
p1
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m3963*m3964*0.1
nodelay
--
0
PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.
p10
p10
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c28 : 1
stoichiometry:c29 : 1
stoichiometry:c30 : 1
m155646*m19*0.1
nodelay
--
0
PMID: 16410796, 14976262, 14579267, 12032557 human TLR8 mediates the recognition of imidazoquinolines and ssRNA.
p11
p11
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c31 : 1
stoichiometry:c32 : 1
stoichiometry:c33 : 1
m19828*m24*0.1
nodelay
--
0
PMID: 16410796, 11130078, 15345224, 12900525, 15630134 TLR9 recognizes bacterial and viral CpG DNA motifs and malaria pigment hemozoin.
p12
p12
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c34 : 1
stoichiometry:c35 : 1
stoichiometry:c36 : 1
m19828*m26*0.1
nodelay
--
0
PMID: 16410796, 11130078, 15345224, 12900525, 15630134 TLR9 recognizes bacterial and viral CpG DNA motifs and malaria pigment hemozoin.
p13
p13
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c37 : 1
stoichiometry:c38 : 1
stoichiometry:c39 : 1
m155666*m3961*0.1
nodelay
--
0
PMID: 16410796, 9851930, 10201887 LPS of Gram-negative bacteria is recognized by TLR4 (hToll)
p14
p14
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c40 : 1
stoichiometry:c42 : 1
stoichiometry:c41 : 1
m30*m207*0.1
nodelay
--
0
PMID: 16410796 Upon stimulation with various TLR ligands, IkappaBs are phosphorylated at serine residues by an IKK complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c43 : 1
stoichiometry:c44 : 1
m29*0.1
nodelay
--
0
PMID: 16410796 The phosphorylation targets IkappaBs for ubiquitination and degradation by the 26S proteasome, allowing NF-kappaB to be released into the nucleus and to bind to the kappaB site.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c45 : 1
stoichiometry:c46 : 1
stoichiometry:c47 : 1
m33*0.1
nodelay
--
0
PMID: 16410796 The phosphorylation targets IkappaBs for ubiquitination and degradation by the 26S proteasome, allowing NF-kappaB to be released into the nucleus and to bind to the kappaB site.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c49 : 1
m73*0.1
nodelay
--
0
PMID: 16410796 The phosphorylation targets IkappaBs for ubiquitination and degradation by the 26S proteasome, allowing NF-kappaB to be released into the nucleus and to bind to the kappaB site.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c50 : 1
stoichiometry:c51 : 1
stoichiometry:c52 : 1
m6810*m28*0.1
nodelay
--
0
PMID: 16410796 TIRAP/Mal and TRAM are required for the activation of MyD88- and Trif-dependent pathways, respectively.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c53 : 1
stoichiometry:c54 : 1
stoichiometry:c55 : 1
m35*m1572*0.1
nodelay
--
0
PMID: 16410796 MyD88 is a central adapter shared by almost all TLRs. The association of TLRs and MyD88 recruits members of the interleukin-1 receptor-associated kinase (IRAK) family.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m5*m6*0.1
nodelay
--
0
PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c57 : 1
stoichiometry:c58 : 1
m36*m17258*0.1
nodelay
--
0
PMID: 16410796 The association of TLRs and MyD88 recruits members of the interleukin-1 receptor-associated kinase (IRAK) family.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c59 : 1
stoichiometry:c60 : 1
stoichiometry:c61 : 1
m38*m37*0.1
nodelay
--
0
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c62 : 1
stoichiometry:c63 : 1
m39*0.1
nodelay
--
0
PMID: 16410796 In response to stimuli, IRAK4 and IRAK1 are sequentially phosphorylated and dissociated from MyD88.
p23
p23
cso30:i:ME_Dissociation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c64 : 1
stoichiometry:c65 : 1
stoichiometry:c66 : 1
stoichiometry:c67 : 1
m40*0.1
nodelay
--
0
PMID: 16410796 In response to stimuli, IRAK4 and IRAK1 are sequentially phosphorylated and dissociated from MyD88.
p24
p24
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c70 : 1
stoichiometry:c69 : 1
m183*m40*0.1
nodelay
--
0
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c120 : 1
stoichiometry:c121 : 1
stoichiometry:c119 : 1
m28*m19005*0.1
nodelay
--
0
PMID: 16410796, 14556004 TRAM is required for the activation of the Trif-dependent pathway, indicating that TRAM is an adapter linking TLR4 to Trif.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c71 : 1
stoichiometry:c72 : 1
stoichiometry:c73 : 1
stoichiometry:c74 : 1
m41*m6443*m42*0.1
nodelay
--
0
PMID: 16410796, 16056267 TRAF6 which contains an N-terminal RING domain that is found in a number of E3 ubiquitin ligases, and forms a complex with Ubc13 and Uev1A, serving as the ubiquitin E3 ligase to promote synthesis of lysine 63-linked polyubiquitin chains.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c75 : 1
stoichiometry:c77 : 1
stoichiometry:c76 : 1
m44*m43*0.1
nodelay
--
0
PMID: 16410796, 16056267 TRAF6 in turn activates transforming growth factor-beta-activated protein kinase 1 (TAK1), a member of the MAP kinase kinase kinase (MAP3K) family, in a ubiquitin-dependent manner.
p28
p28
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c78 : 1
stoichiometry:c80 : 1
stoichiometry:c79 : 1
m46*m45*0.1
nodelay
--
0
PMID: 16410796 TAK1 activates the IKK complex that leads to NF-kappaB activation.
p29
p29
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c81 : 1
stoichiometry:c82 : 1
stoichiometry:c83 : 1
stoichiometry:c84 : 1
stoichiometry:c85 : 1
m1573*m1583*m6433*m19389*0.1
nodelay
--
0
PMID: 16410796 TAK1 forms a complex with TAB1, TAB2 and TAB3.
p3
p3
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
stoichiometry:c9 : 1
m3987*m3964*0.1
nodelay
--
0
PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.
p30
p30
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c86 : 1
stoichiometry:c221 : 1
stoichiometry:c87 : 1
m1875*m45*0.1
nodelay
--
0
PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.
p31
p31
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c89 : 1
stoichiometry:c220 : 1
stoichiometry:c90 : 1
m3613*m45*0.1
nodelay
--
0
PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.
p32
p32
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c92 : 1
stoichiometry:c94 : 1
stoichiometry:c93 : 1
m48*m16567*0.1
nodelay
--
0
PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.
p33
p33
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c95 : 1
stoichiometry:c97 : 1
stoichiometry:c96 : 1
m48*m47*0.1
nodelay
--
0
PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.
p34
p34
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c98 : 1
stoichiometry:c103 : 1
stoichiometry:c99 : 1
m63*m16567*0.1
nodelay
--
0
PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.
p35
p35
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c100 : 1
stoichiometry:c102 : 1
stoichiometry:c101 : 1
m63*m47*0.1
nodelay
--
0
PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.
p36
p36
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c104 : 1
stoichiometry:c109 : 1
stoichiometry:c105 : 1
m65*m1135*0.1
nodelay
--
0
PMID: 16410796 ERK is also activated in response to TLR ligands through the activation of MEK1 and MEK2, although an upstream kinase activating MEK1 and MEK2 in TLR signaling remains unknown.
p37
p37
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c106 : 1
stoichiometry:c108 : 1
stoichiometry:c107 : 1
m65*m70*0.1
nodelay
--
0
PMID: 16410796 ERK is also activated in response to TLR ligands through the activation of MEK1 and MEK2, although an upstream kinase activating MEK1 and MEK2 in TLR signaling remains unknown.
p38
p38
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c110 : 1
stoichiometry:c112 : 1
stoichiometry:c111 : 1
m219*m64*0.1
nodelay
--
0
PMID: 16410796 AP-1 activation in TLR signaling is mostly mediated by MAP kinases such as c-Jun N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK). PMID: 16410796 TAK1 simultaneously activates the MAP kinase pathway, which results in phosphorylation (P) and activation of AP-1.
p39
p39
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c113 : 1
stoichiometry:c115 : 1
stoichiometry:c114 : 1
m219*m49*0.1
nodelay
--
0
PMID: 16410796 AP-1 activation in TLR signaling is mostly mediated by MAP kinases such as c-Jun N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK). PMID: 16410796 TAK1 simultaneously activates the MAP kinase pathway, which results in phosphorylation (P) and activation of AP-1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c10 : 1
stoichiometry:c11 : 1
stoichiometry:c12 : 1
m12*m13*0.1
nodelay
--
0
PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.
p40
p40
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c116 : 1
stoichiometry:c118 : 1
stoichiometry:c117 : 1
m219*m66*0.1
nodelay
--
0
PMID: 16410796 AP-1 activation in TLR signaling is mostly mediated by MAP kinases such as c-Jun N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK). PMID: 16410796 TAK1 simultaneously activates the MAP kinase pathway, which results in phosphorylation (P) and activation of AP-1.
p41
p41
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c122 : 1
stoichiometry:c123 : 1
stoichiometry:c124 : 1
m18998*m19314*0.1
nodelay
--
0
PMID: 16410796 Trif is the sole adapter utilized by TLR3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c125 : 1
stoichiometry:c126 : 1
stoichiometry:c127 : 1
m18998*m68*0.1
nodelay
--
0
PMID: 16410796, 14556004 TRAM is required for the activation of the Trif-dependent pathway, indicating that TRAM is an adapter linking TLR4 to Trif.
p43
p43
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c128 : 1
stoichiometry:c129 : 1
stoichiometry:c130 : 1
m19305*m71*0.1
nodelay
--
0
PMID: 16410796, 15064760 Trif?RIP1 interactions are responsible for NF-kappaB activation in TLR3 signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c48 : 1
stoichiometry:c133 : 1
stoichiometry:c131 : 1
m31*m72*0.1
nodelay
--
0
PMID: 16410796, 15064760 Trif?RIP1 interactions are responsible for NF-kappaB activation in TLR3 signaling.
p45
p45
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c134 : 1
stoichiometry:c135 : 1
stoichiometry:c136 : 1
m19305*m183*0.1
nodelay
--
0
PMID: 16410796 Trif possesses three typical TRAF6-binding domains in the N-terminal region, which mediate interaction with TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c139 : 1
stoichiometry:c138 : 1
m31*m74*0.1
nodelay
--
0
PMID: 16410796 Trif activates NF-kappaB by recruiting TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c140 : 1
stoichiometry:c141 : 1
stoichiometry:c142 : 1
m69*m3902*0.1
nodelay
--
0
PMID: 16410796 TLR4 also recruits TRAM and Trif, which interacts with TBK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c143 : 1
stoichiometry:c144 : 1
stoichiometry:c145 : 1
m75*m1599*0.1
nodelay
--
0
PMID: 16410796 TBK1 together with IKKi mediates phosphorylation of IRF3.
p49
p49
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c146 : 1
stoichiometry:c148 : 1
stoichiometry:c147 : 1
m977*m104*0.1
nodelay
--
0
PMID: 16410796 TBK1 together with IKKi mediates phosphorylation of IRF3.
p5
p5
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c14 : 1
stoichiometry:c15 : 1
m3965*m119368*0.1
nodelay
--
0
PMID: 16410796, 11607032 TLR3 recognizes double-stranded RNA (dsRNA) that is produced from many viruses during replication.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c149 : 1
stoichiometry:c150 : 1
m19324*0.1
nodelay
--
0
PMID: 16410796 Phosphorylated IRF3 is dimerized and translocated into nucleus to bind DNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c151 : 1
stoichiometry:c152 : 1
m77*0.1
nodelay
--
0
PMID: 16410796 Phosphorylated IRF3 is dimerized and translocated into nucleus to bind DNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c154 : 1
stoichiometry:c153 : 1
m78*0.1
nodelay
--
0
PMID: 16410796 Initial induction of IFNbeta is largely dependent on IRF3 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c155 : 1
stoichiometry:c156 : 1
stoichiometry:c157 : 1
m25*m1572*0.1
nodelay
--
0
PMID: 16410796 After ligand ligation, these TLRs elicit the MyD88-dependent pathway to regulate inflammatory responses by activating NF-kappaB and AP-1.
p54
p54
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c158 : 1
stoichiometry:c159 : 1
stoichiometry:c160 : 1
stoichiometry:c161 : 1
stoichiometry:c162 : 1
m980*m82*m17258*m38*0.1
nodelay
--
0
PMID: 16410796 In pDCs, IRF7 is constitutively expressed and forms a signaling complex with MyD88, IRAK1 and IRAK4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c163 : 1
stoichiometry:c164 : 1
m83*0.1
nodelay
--
0
PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c165 : 1
stoichiometry:c183 : 1
stoichiometry:c166 : 1
m85*m41*0.1
nodelay
--
0
PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei. Additionally, TRAF6-dependent ubiquitination is also required for IRF7 activation.
p57
p57
cso30:i:ME_Dimerization
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c168 : 1
stoichiometry:c169 : 1
stoichiometry:c170 : 1
stoichiometry:c171 : 1
stoichiometry:c172 : 1
m86*0.1
nodelay
--
0
PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c173 : 1
stoichiometry:c174 : 1
m87*0.1
nodelay
--
0
PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei.
p59
p59
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c175 : 1
stoichiometry:c176 : 1
stoichiometry:c177 : 1
m979*m1572*0.1
nodelay
--
0
PMID: 16410796, 15665823 It is also reported that IRF5 interacts with MyD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c17 : 1
stoichiometry:c18 : 1
m3966*m15*0.1
nodelay
--
0
PMID: 16410796, 11323673 TLR5 recognizes bacterial flagellin.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c180 : 1
stoichiometry:c178 : 1
stoichiometry:c179 : 1
m25*m91*0.1
nodelay
--
0
PMID: 16410796 IRF5 translocates into the nucleus in response to ligand stimulation.
p61
p61
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c181 : 1
stoichiometry:c91 : 1
stoichiometry:c182 : 1
m979*m75*0.1
nodelay
--
0
PMID: 16410796, 15210742, 15556946 Although it is reported that IRF5 is phosphorylated by TBK1 and IKKi in vitro, cells deficient in TBK1 and IKKi show normal inflammatory responses in response to various TLR ligands.
p62
p62
cso30:i:ME_Phosphorylation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c184 : 1
stoichiometry:c207 : 1
stoichiometry:c185 : 1
m979*m76*0.1
nodelay
--
0
PMID: 16410796, 15210742, 15556946 Although it is reported that IRF5 is phosphorylated by TBK1 and IKKi in vitro, cells deficient in TBK1 and IKKi show normal inflammatory responses in response to various TLR ligands.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c187 : 1
stoichiometry:c188 : 1
stoichiometry:c189 : 1
m93*m92*0.1
nodelay
--
0
PMID: 16410796 The helicase domain of RIG-I interacts with dsRNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c190 : 1
stoichiometry:c191 : 1
stoichiometry:c192 : 1
m92*m95*0.1
nodelay
--
0
PMID: 16410796, 16116171 LGP2 is also related to RIG-I and Mda5, but lacks the CARD-like domains, and is therefore suggested to function as a negative regulator for RIG-I and Mda5.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c193 : 1
stoichiometry:c194 : 1
stoichiometry:c195 : 1
m97*m92*0.1
nodelay
--
0
PMID: 16410796, 11805321, 12015121, 15563593 Melanoma differentiation-associated gene 5 (Mda5) (also known as Helicard) is structurally similar to RIG-I, which also contains two CARD-like and a single helicase domain, and is suggested to mediate antiviral responses.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c196 : 1
stoichiometry:c197 : 1
stoichiometry:c198 : 1
m94*m99*0.1
nodelay
--
0
PMID: 16410796 IPS-1 interacts with RIG-I and Mda5 via the CARD domain.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c199 : 1
stoichiometry:c200 : 1
stoichiometry:c201 : 1
m98*m99*0.1
nodelay
--
0
PMID: 16410796 IPS-1 interacts with RIG-I and Mda5 via the CARD domain.
p68
p68
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c202 : 1
stoichiometry:c203 : 1
stoichiometry:c204 : 1
stoichiometry:c205 : 1
m71*m1814*m100*0.1
nodelay
--
0
PMID: 16410796, 16127453 IPS-1 interacts with FADD and RIP-1 via non-CARD region to facilitate NF-kappaB, rather than IRF3 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c206 : 1
stoichiometry:c88 : 1
stoichiometry:c208 : 1
m99*m41*0.1
nodelay
--
0
PMID: 16410796, 16153868 VISA contains two TRAF6-binding domains, and interacts with TRAF6 through these domains.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c20 : 1
stoichiometry:c21 : 1
m19940*m17*0.1
nodelay
--
0
PMID: 16410796, 11812998, 14976261, 14976262, 14579267, 12032557, 15034168, 15723075 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single-stranded RNA (ssRNA) derived from human immunodeficiency virus type I (HIV-1), vesicular stomatitis virus (VSV) and influenza virus, and certain siRNAs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c209 : 1
stoichiometry:c211 : 1
stoichiometry:c210 : 1
m31*m102*0.1
nodelay
--
0
PMID: 16410796, 16153868 VISA?TRAF6 interaction is required for NF-kappaB but not IRF3 activation.
p71
p71
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c212 : 1
stoichiometry:c213 : 1
stoichiometry:c214 : 1
m99*m18998*0.1
nodelay
--
0
PMID: 16410796, 16153868 VISA interacts with Trif.
p72
p72
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c215 : 1
stoichiometry:c217 : 1
stoichiometry:c216 : 1
m46*m100*0.1
nodelay
--
0
PMID: 16410796 IPS-1 initiates intracellular signaling pathways leading to IRF3, NF-kappaB and AP-1 via TBK1/IKKi, IKKalpha/IKKbeta and MAP kinases, respectively.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c218 : 1
stoichiometry:c219 : 1
m76*0.1
nodelay
--
0
PMID: 16410796 IPS-1 initiates intracellular signaling pathways leading to IRF3, NF-kappaB and AP-1 via TBK1/IKKi, IKKalpha/IKKbeta and MAP kinases, respectively.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c22 : 1
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m19940*m19*0.1
nodelay
--
0
PMID: 16410796, 11812998, 14976261, 14976262, 14579267, 12032557, 15034168, 15723075 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single-stranded RNA (ssRNA) derived from human immunodeficiency virus type I (HIV-1), vesicular stomatitis virus (VSV) and influenza virus, and certain siRNAs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
stoichiometry:c27 : 1
m155646*m21*0.1
nodelay
--
0
PMID: 16410796, 14976262, 14579267, 12032557 human TLR8 mediates the recognition of imidazoquinolines and ssRNA.
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--