Original Literature | Model OverView |
---|---|
Publication
Title
The role of viral nucleic acid recognition in dendritic cells for innate andadaptive antiviral immunity.
Affiliation
Department of Medicine II, Technical University, Ismaninger Str 22, D-81675,Munich, Germany.
Abstract
Dendritic cells which are located at the interface of innate and adaptiveimmunity are targets for infection by many different DNA and RNA viruses.Dendritic cell subpopulations express specific nucleic acid recognitionreceptors belonging to the Toll-like receptor family (TLR3, 7, 8, 9) and thecytosolic RNA helicase family (RIG-I, MDA5, LGP2). Activation of dendritic cellsby viral DNA and RNA via these receptors is essential for triggering the innateantiviral immune response and shaping the ensuing adaptive antiviral immunity.This review will summarize our current knowledge of viral nucleic acidrecognition and signaling by Toll-like receptors and RNA helicases focusing onrecent evidence for their specific functions in antiviral defense in vivo.
PMID
18086372
|
Entity
Process
NF-kappaB
--
MO000000058
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m17
10
infinite
0
TRANSPATH | MO000000058 |
--
TRAF6
--
MO000000212
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m183
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000000212 |
--
IRAK
--
MO000000213
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m184
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000213 |
--
chemokines
--
MO000000265
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m211
10
infinite
0
TRANSPATH | MO000000265 |
--
IRF-3
--
MO000007694
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m977
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007694 |
--
IRF-7
--
MO000007702
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m980
10
infinite
0
TRANSPATH | MO000007702 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
IFN Type I
--
MO000016658
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1634
10
infinite
0
TRANSPATH | MO000016658 |
--
IFNalpha1
--
MO000016659
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m1635
10
infinite
0
InterPro | IPR000471 |
TRANSPATH | MO000016659 |
--
IKK-alpha:IKK-beta:IKK-gamma
--
MO000016661
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1637
10
infinite
0
TRANSPATH | MO000016661 |
--
IFNgamma
--
MO000016665
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1639
10
infinite
0
InterPro | IPR002069 |
TRANSPATH | MO000016665 |
--
Caspases
--
MO000016907
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1822
10
infinite
0
TRANSPATH | MO000016907 |
--
cytokines
--
MO000019387
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3957
10
infinite
0
TRANSPATH | MO000019387 |
--
protein remnants
--
MO000019479
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m360980
10
infinite
0
TRANSPATH | MO000019479 |
--
dsRNA
--
MO000022224
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m119368
10
infinite
0
TRANSPATH | MO000022224 |
--
IRAK-4
--
MO000039077
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m17258
10
infinite
0
TRANSPATH | MO000039077 |
--
dsRNA:TLR3:TRIF
--
MO000041437
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19305
10
infinite
0
TRANSPATH | MO000041437 |
--
dsRNA:TLR3:TRIF:TBK1:IKK-i
--
MO000041441
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19309
10
infinite
0
TRANSPATH | MO000041441 |
--
IRF-3{p}
--
MO000041456
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19324
10
infinite
0
TRANSPATH | MO000041456 |
--
IRF-7{p}
--
MO000041457
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19325
10
infinite
0
TRANSPATH | MO000041457 |
--
TLR8
--
MO000042007
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19823
10
infinite
0
TRANSPATH | MO000042007 |
--
TLR7
--
MO000042126
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19940
10
infinite
0
TRANSPATH | MO000042126 |
--
IPS-1
--
MO000094908
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m68199
10
infinite
0
TRANSPATH | MO000094908 |
--
MDA-5
--
MO000103999
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m76904
10
infinite
0
TRANSPATH | MO000103999 |
--
--
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
--
dsRNA: MDA-5
--
e100
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m103
0
infinite
0
--
LGP2
--
e101
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m104
0
infinite
0
--
dsRNA: LGP2
--
e102
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m105
0
infinite
0
--
dsRNA: RIG-1: IPS-1
--
e103
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m106
0
infinite
0
--
TBK1: IKK-i
--
e104
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m107
0
infinite
0
--
LGP2: RIG-1
--
e105
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m108
0
infinite
0
--
dsRNA: RIG-1: IPS-1: TRAF3
--
e106
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m109
0
infinite
0
--
dsRNA: RIG-1: IPS-1: TBK1: IKK-i
--
e107
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m110
0
infinite
0
--
dsRNA: RIG-1: IPS-1: TBK1: IKK-i: IRF-3
--
e108
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m111
0
infinite
0
--
dsRNA: RIG-1: IPS-1: RIP1: FADD
--
e109
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m112
0
infinite
0
--
--
e11
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m11
0
infinite
0
--
TBK1: IKK-i{activated}
--
e110
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m113
0
infinite
0
--
dsRNA: RIG-1: IPS-1: TRAF6
--
e111
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m114
0
infinite
0
--
5'-triphosphate ssRNA
--
e112
cso30:c:Rna
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m115
0
infinite
0
--
5'-triphosphate ssRNA: RIG-1
--
e113
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m116
0
infinite
0
--
card domain
--
e114
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m117
0
infinite
0
--
C-terminal helicase domain
--
e115
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
csml-variable:Double
m118
0
infinite
0
--
C-terminal helicase domain
--
e116
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
csml-variable:Double
m119
0
infinite
0
--
MDA-5
--
e117
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m120
0
infinite
0
--
RIG-1
--
e118
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m121
0
infinite
0
--
LGP2
--
e119
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m122
0
infinite
0
--
ssRNA
--
e12
cso30:c:Rna
cso30:i:CC_Extracellular
--
csml-variable:Double
m12
0
infinite
0
--
dsRNA: MDA-5: IPS-1
--
e120
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m123
0
infinite
0
--
dsRNA: MDA-5: IPS-1: TBK1: IKK-i
--
e121
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m124
0
infinite
0
--
NS1
--
e122
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m69
0
infinite
0
--
dsRNA: NS1
--
e123
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m125
0
infinite
0
--
dsRNA: NS1: RIG-1: IPS-1
--
e124
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m126
0
infinite
0
--
RSV NS1
--
e125
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m127
0
infinite
0
--
RSV NS2
--
e126
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m128
0
infinite
0
--
phosphoprotein P
--
e127
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m129
0
infinite
0
--
V protein
--
e128
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
csml-variable:Double
m130
0
infinite
0
--
V rpotein: MDA-5
--
e129
cso30:c:Complex
cso30:i:CC_Cell_WithoutCellWall_
--
csml-variable:Double
m131
0
infinite
0
--
csml-variable:Double
m13
0
infinite
0
--
poliovirus protin
--
e130
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m132
0
infinite
0
--
--
e131
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialCentromere
--
--
--
csml-variable:Double
m133
0
infinite
0
--
--
e132
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialChromosome
--
--
--
csml-variable:Double
m134
0
infinite
0
--
--
e133
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialInnerMembrane
--
--
--
csml-variable:Double
m135
0
infinite
0
--
--
e134
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialOuterMembrane
--
--
--
csml-variable:Double
m136
0
infinite
0
--
--
e135
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialIntermembraneSpace
--
--
--
csml-variable:Double
m137
0
infinite
0
--
--
e136
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialEnvelope
--
--
--
csml-variable:Double
m138
0
infinite
0
--
--
e137
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialMatrix
--
--
--
csml-variable:Double
m139
0
infinite
0
--
--
e138
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Mitochondria
--
--
--
csml-variable:Double
m140
0
infinite
0
--
--
e139
cso30:c:EntityBiologicalCompartment
cso30:i:CC_MitochondrialLumen
--
--
--
csml-variable:Double
m141
0
infinite
0
--
ssRNA: TLR7
--
e14
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m14
0
infinite
0
--
NS3/4A
--
e140
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
csml-variable:Double
m142
0
infinite
0
--
csml-variable:Double
m143
0
infinite
0
--
ligand: TLR
--
e142
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m144
0
infinite
0
--
MAPKs{activated}
--
e143
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m146
10
infinite
0
TRANSPATH | MO000000077 |
--
chemokine
--
e144
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m147
0
infinite
0
--
ssRNA: TLR8
--
e15
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m15
0
infinite
0
--
CpG DNA: TLR9
--
e16
cso30:c:Complex
cso30:i:CC_EndosomeMembrane
--
csml-variable:Double
m16
0
infinite
0
--
poly U RNA
--
e17
cso30:c:RnaOther
cso30:i:CC_Extracellular
--
csml-variable:Double
m18
0
infinite
0
--
Poly U RNA: TLR7
--
e18
cso30:c:Complex
cso30:i:CC_EndosomeMembrane
--
--
csml-variable:Double
m19
0
infinite
0
--
Poly U RNA: TLR8
--
e19
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m20
0
infinite
0
--
--
e2
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m2
0
infinite
0
--
siRNA
--
e20
cso30:c:RnaOther
cso30:i:CC_Extracellular
--
csml-variable:Double
m21
0
infinite
0
--
siRNA: TLR8
--
e21
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m22
0
infinite
0
--
siRNA: TLR7
--
e22
cso30:c:Complex
cso30:i:CC_EndosomeMembrane
--
--
csml-variable:Double
m23
0
infinite
0
--
imidazoquinoline
--
e23
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
csml-variable:Double
m24
0
infinite
0
--
imidazoquinoline: TLR7
--
e24
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m25
0
infinite
0
--
imidazoquinoline: TLR8
--
e25
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m26
0
infinite
0
--
poly I: C
--
e26
cso30:c:RnaOther
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m27
0
infinite
0
--
poly I: C: TLR3
--
e27
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m28
0
infinite
0
--
dsRNA:TLR3:TRIF: TRAF3
--
e28
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m29
0
infinite
0
--
IRF-7: IRF-7{p}
--
e29
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m30
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
IRF-3: IRF-3{p}
--
e30
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m31
0
infinite
0
--
csml-variable:Double
m32
0
infinite
0
--
IRF-7: IRF-7{p}
--
e32
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m33
0
infinite
0
--
IRF-3{p}: IRF-7{p}
--
e33
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m34
0
infinite
0
--
IRF-3: IRF-3{p}
--
e34
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m35
0
infinite
0
--
dsRNA:TLR3:TRIF: RIP1
--
e35
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m37
0
infinite
0
--
dsRNA:TLR3:TRIF: TRAF6
--
e36
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m38
0
infinite
0
--
IKK-alpha:IKK-beta:IKK-gamma{activated}
--
e38
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m40
10
infinite
0
TRANSPATH | MO000016661 |
--
IkappaB: NF-kappaB
--
e39
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m41
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
NF-kappaB{nuclear}
--
e40
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m42
10
infinite
0
TRANSPATH | MO000000058 |
--
IFN Type I
--
e41
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m43
0
infinite
0
--
IFN inducible genes
--
e42
cso30:c:mRNA
cso30:i:CC_Nucleolus
--
csml-variable:Double
m44
0
infinite
0
--
IL-8
--
e43
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m45
0
infinite
0
--
ODN
--
e44
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m46
0
infinite
0
--
ODN: TLR9
--
e45
cso30:c:Complex
cso30:i:CC_EndosomeMembrane
--
csml-variable:Double
m47
0
infinite
0
--
CpG DNA: TLR9: MyD88
--
e46
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m48
0
infinite
0
--
CpG DNA: TLR9: MyD88: IRAk-1: IRAK-4: TRAF6: IRF-7
--
e47
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m49
0
infinite
0
--
CpG DNA: TLR9: MyD88: IRAk-1: IRAK-4: TRAF6
--
e48
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m63
0
infinite
0
--
cytokine
--
e49
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m64
0
infinite
0
--
--
e5
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
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
--
--
e6
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
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
--
costimulatory molecule genes
--
e63
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m65
0
infinite
0
--
IFN Type I: IFNRs
--
e64
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m66
0
infinite
0
--
IRF-1{activated}
--
e65
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m67
10
infinite
0
InterPro | IPR001346 |
TRANSPATH | MO000007685 |
--
IL-12p35
--
e66
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m68
0
infinite
0
--
CpG-B ODN
--
e67
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m70
0
infinite
0
--
--
e68
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m71
0
infinite
0
--
--
e69
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m72
0
infinite
0
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
--
e70
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane
--
--
--
csml-variable:Double
m73
0
infinite
0
--
--
e71
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m74
0
infinite
0
--
--
e72
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearCentromere
--
--
--
csml-variable:Double
m75
0
infinite
0
--
--
e73
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearChromosome
--
--
--
csml-variable:Double
m76
0
infinite
0
--
--
e74
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Chromatin
--
--
--
csml-variable:Double
m77
0
infinite
0
--
--
e75
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearBody
--
--
--
csml-variable:Double
m78
0
infinite
0
--
--
e76
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleoplasm
--
--
--
csml-variable:Double
m79
0
infinite
0
--
--
e77
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearPore
--
--
--
csml-variable:Double
m80
0
infinite
0
--
--
e78
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearInnerMembrane
--
--
--
csml-variable:Double
m81
0
infinite
0
--
--
e79
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleus
--
--
--
csml-variable:Double
m82
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
--
e80
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearOuterMembrane
--
--
--
csml-variable:Double
m83
0
infinite
0
--
--
e81
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearLumen
--
--
--
csml-variable:Double
m84
0
infinite
0
--
--
e82
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelopeLumen
--
--
--
csml-variable:Double
m85
0
infinite
0
--
--
e83
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelope
--
--
--
csml-variable:Double
m86
0
infinite
0
--
--
e84
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleolus
--
--
--
csml-variable:Double
m87
0
infinite
0
--
--
e85
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m88
0
infinite
0
--
--
e86
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m89
0
infinite
0
--
--
e87
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytosol
--
--
--
csml-variable:Double
m90
0
infinite
0
--
--
e88
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m91
0
infinite
0
--
IL-12: IL-12R
--
e89
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m92
0
infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0
infinite
0
--
IL-8 receptor
--
e90
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m93
0
infinite
0
--
IL-8: IL-8 receptor
--
e91
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m94
0
infinite
0
--
ssRNA: TLR7: MyD88
--
e92
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m95
0
infinite
0
--
ssRNA: TLR7: MyD88: IRAK-1: IRAk-4: TRAF6: IRF-7
--
e93
cso30:c:Complex
cso30:i:CC_EndosomeMembrane
--
csml-variable:Double
m96
0
infinite
0
--
ssRNA: TLR7: MyD88: IRAK-1: IRAk-4: TRAF6
--
e94
cso30:c:Complex
cso30:i:CC_EndosomeMembrane
--
--
csml-variable:Double
m97
0
infinite
0
--
ssRNA: TLR8: MyD88
--
e95
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m98
0
infinite
0
--
ssRNA: TLR8: MyD88: IRAK-1: IRAk-4: TRAF6: IRF-7
--
e96
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m99
0
infinite
0
--
ssRNA: TLR8: MyD88: IRAK-1: IRAk-4: TRAF6
--
e97
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m100
0
infinite
0
--
RIG-1
--
e98
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m101
0
infinite
0
--
dsRNA: RIG-1
--
e99
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m102
0
infinite
0
--
p1
p1
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m12*m19940*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
p10
p10
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c28 : 1
stoichiometry:c30 : 1
stoichiometry:c32 : 1
m24*m19940*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
p100
p100
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cell_WithoutCellWall_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c294 : 1
stoichiometry:c295 : 1
stoichiometry:c296 : 1
stoichiometry:c297 : 1
m132*m1822*m76904*0.1
nodelay
--
0
PMID: 18086372 Degradation of MDA5 in poliovirus-infected cells occurs in a proteasome- and caspase-dependent manner and correlates with the induction of apoptosis in poliovirus-infected cells.
p101
p101
cso30:i:ME_ProteinCleavage
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c298 : 1
stoichiometry:c299 : 1
stoichiometry:c300 : 1
m68199*m142*0.1
nodelay
--
0
PMID: 18086372, 16301520, 16177806 Hepatitis C virus (HCV) encodes the protease NS3/4A which targets IPS-1 by cleaving it at position Cys-508, thereby dislocating it from the mitochondrial membrane and thus abrogating further downstream signaling to type I IFN and NFkappaB-dependent target gene expression.
p102
p102
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c303 : 1
stoichiometry:c305 : 1
stoichiometry:c304 : 1
m1637*m144*0.1
nodelay
--
0
PMID: 18086372 Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.
p103
p103
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell_WithoutCellWall_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c306 : 1
stoichiometry:c307 : 1
stoichiometry:c308 : 1
m144*m145*0.1
nodelay
--
0
PMID: 18086372 Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.
p104
p104
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c310 : 1
stoichiometry:c311 : 1
stoichiometry:c309 : 1
m147*m144*0.1
nodelay
--
0
PMID: 18086372 Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.
p105
p105
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c312 : 1
stoichiometry:c313 : 1
stoichiometry:c314 : 1
m64*m144*0.1
nodelay
--
0
PMID: 18086372 Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c29 : 1
stoichiometry:c31 : 1
stoichiometry:c33 : 1
m24*m19823*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
p12
p12
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c35 : 1
stoichiometry:c34 : 1
stoichiometry:c36 : 1
m3965*m27*0.1
nodelay
--
0
PMID: 18086372, 11607032 Another ligand for TLR3 is poly(I:C) which is a synthetic dsRNA mimicking viral infection.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c37 : 1
stoichiometry:c38 : 1
m66*0.1
nodelay
--
0
PMID: 18086372 Up-regulation of TLR3 expression by type I IFN amplifies the response to TLR3 ligands.
p14
p14
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c39 : 1
stoichiometry:c40 : 1
stoichiometry:c41 : 1
m1872*m19305*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
p15
p15
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c42 : 1
stoichiometry:c43 : 1
stoichiometry:c45 : 1
stoichiometry:c44 : 1
m3902*m1599*m29*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
p16
p16
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c46 : 1
stoichiometry:c50 : 1
stoichiometry:c47 : 1
m980*m19309*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
p17
p17
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c48 : 1
stoichiometry:c51 : 1
stoichiometry:c282 : 1
stoichiometry:c285 : 1
stoichiometry:c49 : 1
m977*m19309*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression. PMID: 18086372, 12885884 Two viral proteins of RSV, NS1 and NS2, are involved in blocking the pathway leading to IRF3 phosphorylation, although the activation of NFkappaB and AP-1 is unaffected.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c52 : 1
stoichiometry:c53 : 1
m19325*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c54 : 1
stoichiometry:c55 : 1
m19324*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
p2
p2
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
stoichiometry:c9 : 1
m13*m19828*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
p20
p20
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c57 : 1
stoichiometry:c58 : 1
m19325*m19324*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression. PMID: 18086372, 16127453 This receptor?adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes.
p21
p21
cso30:i:ME_Translocation
cso30:i:CC_NuclearEnvelopeLumen
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c59 : 1
stoichiometry:c60 : 1
m30*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c61 : 1
stoichiometry:c62 : 1
m32*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression. PMID: 18086372, 16127453 This receptor?adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c63 : 1
stoichiometry:c64 : 1
m31*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
p24
p24
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c65 : 1
stoichiometry:c66 : 1
stoichiometry:c67 : 1
m19305*m36*0.1
nodelay
--
0
PMID: 18086372 NFkappaB activation by TLR3 ligands is mediated in two ways ? via association of TRIF with RIP1 or via interaction of TRIF with TRAF6, which in turn activates TAK1.
p25
p25
cso30:i:ME_Binding
cso30:i:CC_EndosomeLumen
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c69 : 1
stoichiometry:c70 : 1
m19305*m183*0.1
nodelay
--
0
PMID: 18086372 NFkappaB activation by TLR3 ligands is mediated in two ways ? via association of TRIF with RIP1 or via interaction of TRIF with TRAF6, which in turn activates TAK1.
p26
p26
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c71 : 1
stoichiometry:c72 : 1
stoichiometry:c73 : 1
m38*m1573*0.1
nodelay
--
0
PMID: 18086372 NFkappaB activation by TLR3 ligands is mediated in two ways ? via association of TRIF with RIP1 or via interaction of TRIF with TRAF6, which in turn activates TAK1.
p27
p27
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c74 : 1
stoichiometry:c76 : 1
stoichiometry:c77 : 1
m37*m1637*0.1
nodelay
--
0
PMID: 18086372, 15064760, 14530355 Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus.
p28
p28
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c75 : 1
stoichiometry:c78 : 1
stoichiometry:c79 : 1
m39*m1637*0.1
nodelay
--
0
PMID: 18086372, 15064760, 14530355 Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus.
p29
p29
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c80 : 1
stoichiometry:c83 : 1
stoichiometry:c81 : 1
stoichiometry:c82 : 1
m40*m41*0.1
nodelay
--
0
PMID: 18086372, 15064760, 14530355 Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus. PMID: 18086372 Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta. PMID: 18086372 Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
p3
p3
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m12*m19823*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
p30
p30
cso30:i:ME_Translocation
cso30:i:CC_NuclearOuterMembrane
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c84 : 1
stoichiometry:c85 : 1
m17*0.1
nodelay
--
0
PMID: 18086372, 15064760, 14530355 Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus. PMID: 18086372 Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c86 : 1
stoichiometry:c89 : 1
m33*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c87 : 1
stoichiometry:c90 : 1
m34*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression. PMID: 18086372, 16127453 This receptor?adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c88 : 1
stoichiometry:c91 : 1
m35*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c92 : 1
stoichiometry:c95 : 1
m33*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c93 : 1
stoichiometry:c96 : 1
m34*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c94 : 1
stoichiometry:c97 : 1
m35*0.1
nodelay
--
0
PMID: 18086372, 12692549, 12702806, 12855817 Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c98 : 1
stoichiometry:c100 : 1
m42*0.1
nodelay
--
0
PMID: 18086372, 17339430 Interestingly, human lung epithelial cells express proinflammatory cytokines including IL-6 and IL-8 upon infection with influenza A virus in a TLR3-dependent manner , suggesting that TLR3-mediated inflammatory responses may also contribute to influenza virus-induced lung pathology in humans.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c99 : 1
stoichiometry:c101 : 1
m42*0.1
nodelay
--
0
PMID: 18086372, 17339430 Interestingly, human lung epithelial cells express proinflammatory cytokines including IL-6 and IL-8 upon infection with influenza A virus in a TLR3-dependent manner , suggesting that TLR3-mediated inflammatory responses may also contribute to influenza virus-induced lung pathology in humans.
p39
p39
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c102 : 1
stoichiometry:c103 : 1
stoichiometry:c104 : 1
m19828*m46*0.1
nodelay
--
0
PMID: 18086372 TLR9 has been described to recognize bacterial DNA or synthetic oligodesoxyribonucleotides (ODN) containing specific unmethylated CpG sequence motifs. These can also be found in the genome of DNA viruses.
p4
p4
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c10 : 1
stoichiometry:c11 : 1
stoichiometry:c281 : 1
stoichiometry:c12 : 1
m119368*m3965*0.1
nodelay
--
0
PMID: 18086372, 15558055, 16424225 TLR3 binds double-stranded (ds) RNA which is found in dsRNA viruses, such as reovirus, or is generated during replication of single-stranded (ss) RNA viruses such as West Nile virus or respiratory syncytial virus or as a by-product of symmetrical transcription of viral DNA, for example from herpes viruses. PMID: 18086372, 15298172, 10933707 By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c105 : 1
stoichiometry:c106 : 1
stoichiometry:c107 : 1
m1572*m16*0.1
nodelay
--
0
PMID: 18086372, 15492225, 15361868 Upon ligand binding the TIR domain of TLR9 recruits MyD88 which forms a supramolecular complex with TRAF6, IRAK1, IRAK4 and IRF7.
p41
p41
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c108 : 1
stoichiometry:c109 : 1
stoichiometry:c110 : 1
stoichiometry:c111 : 1
stoichiometry:c112 : 1
stoichiometry:c113 : 1
m183*m48*m184*m17258*m980*0.1
nodelay
--
0
PMID: 18086372, 15492225, 15361868 Upon ligand binding the TIR domain of TLR9 recruits MyD88 which forms a supramolecular complex with TRAF6, IRAK1, IRAK4 and IRF7.
p42
p42
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c114 : 1
stoichiometry:c116 : 1
stoichiometry:c115 : 1
m49*0.1
nodelay
--
0
PMID: 18086372, 15492225, 15361868 Upon ligand binding the TIR domain of TLR9 recruits MyD88 which forms a supramolecular complex with TRAF6, IRAK1, IRAK4 and IRF7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c118 : 1
stoichiometry:c117 : 1
m47*0.1
nodelay
--
0
PMID: 18086372 CpG ODN class A, B and C have been designed to trigger primarily type I IFN response (A) or costimulatory molecule expression and inflammatory cytokine production (B) or both (C) in pDCs. PMID: 18086372, 16864658 Induction of type I IFNs by TLR9 ligands in pDCs depends on retention of the ligand?receptor complex within early endosomes at a pH value between 6.2 and 5.5.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c121 : 1
stoichiometry:c119 : 1
m47*0.1
nodelay
--
0
PMID: 18086372 CpG ODN class A, B and C have been designed to trigger primarily type I IFN response (A) or costimulatory molecule expression and inflammatory cytokine production (B) or both (C) in pDCs. PMID: 18086372, 16864658 Delivery of TLR9 ligands to late endosome with lower pH values (<4.5) impairs the induction of type I IFNs and promotes inflammatory cytokine and costimulatory molecule expression in pDCs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c122 : 1
stoichiometry:c120 : 1
m47*0.1
nodelay
--
0
PMID: 18086372 CpG ODN class A, B and C have been designed to trigger primarily type I IFN response (A) or costimulatory molecule expression and inflammatory cytokine production (B) or both (C) in pDCs. PMID: 18086372, 16864658 Delivery of TLR9 ligands to late endosome with lower pH values (<4.5) impairs the induction of type I IFNs and promotes inflammatory cytokine and costimulatory molecule expression in pDCs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c124 : 1
stoichiometry:c123 : 1
m43*0.1
nodelay
--
0
PMID: 18086372 During the second phase secreted type I IFNs signal via type I IFN receptor in an autocrine and paracrine manner.
p47
p47
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c125 : 1
stoichiometry:c126 : 1
stoichiometry:c127 : 1
m1634*m1771*0.1
nodelay
--
0
PMID: 18086372 During the second phase secreted type I IFNs signal via type I IFN receptor in an autocrine and paracrine manner.
p48
p48
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c128 : 1
stoichiometry:c129 : 1
stoichiometry:c130 : 1
m93631*m66*0.1
nodelay
--
0
PMID: 18086372 Downstream signaling of the type I IFN receptor induces a strong up-regulation of IRF7 production leading to full expression of type I IFN genes (positive feedback loop).
p49
p49
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c131 : 1
stoichiometry:c133 : 1
m970*m70*0.1
nodelay
--
0
PMID: 18086372, 17018642, 17273999 In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1¡Ý/¡Ý mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
p5
p5
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c15 : 1
stoichiometry:c14 : 1
m19314*m18998*0.1
nodelay
--
0
PMID: 18086372 TRIF is recruited to the cytoplasmatic TIR domain of TLR3 and interacts with a set of different signaling molecules and kinases which in turn initiate activation of NFkappaB or IRF3 and IRF7 leading to type I interferon induction.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c134 : 1
m67*0.1
nodelay
--
0
PMID: 18086372, 17018642, 17273999 In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1¡Ý/¡Ý mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c138 : 1
stoichiometry:c135 : 1
m67*0.1
nodelay
--
0
PMID: 18086372, 17018642, 17273999 In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1¡Ý/¡Ý mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c139 : 1
stoichiometry:c136 : 1
m67*0.1
nodelay
--
0
PMID: 18086372, 17018642, 17273999 In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1¡Ý/¡Ý mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
p53
p53
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c141 : 1
stoichiometry:c142 : 1
stoichiometry:c140 : 1
m93589*m16*0.1
nodelay
--
0
PMID: 18086372 In the very early phase of systemic MCMV infection pDCs and conventional DCs release the first wave of type I interferons and inflammatory cytokines including IL-12.
p54
p54
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c143 : 1
stoichiometry:c144 : 1
stoichiometry:c145 : 1
m2121*m12340*0.1
nodelay
--
0
PMID: 18086372, 8557990 Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c150 : 1
stoichiometry:c146 : 1
m45*0.1
nodelay
--
0
PMID: 18086372, 8557990 Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
p56
p56
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c151 : 1
stoichiometry:c154 : 1
stoichiometry:c155 : 1
m94*m93423*0.1
nodelay
--
0
PMID: 18086372, 8557990 Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
p57
p57
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c147 : 1
stoichiometry:c148 : 1
stoichiometry:c149 : 1
m2120*m93*0.1
nodelay
--
0
PMID: 18086372, 8557990 Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
p58
p58
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c152 : 1
stoichiometry:c153 : 1
stoichiometry:c156 : 1
m92*m93423*0.1
nodelay
--
0
PMID: 18086372, 8557990 Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
PMID: 18086372, 8557990 Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
p6
p6
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c17 : 1
stoichiometry:c18 : 1
m18*m19940*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c158 : 1
stoichiometry:c159 : 1
stoichiometry:c160 : 1
m14*m1572*0.1
nodelay
--
0
PMID: 18086372 The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
p61
p61
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c161 : 1
stoichiometry:c162 : 1
stoichiometry:c163 : 1
stoichiometry:c164 : 1
stoichiometry:c165 : 1
m184*m17258*m183*m980*0.1
nodelay
--
0
PMID: 18086372 The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
p62
p62
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c166 : 1
stoichiometry:c167 : 1
stoichiometry:c168 : 1
m96*0.1
nodelay
--
0
PMID: 18086372 The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c169 : 1
stoichiometry:c170 : 1
stoichiometry:c171 : 1
m15*m1572*0.1
nodelay
--
0
PMID: 18086372 The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
p64
p64
cso30:i:ME_Binding
cso30:i:CC_EndosomeLumen
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c172 : 1
stoichiometry:c173 : 1
stoichiometry:c174 : 1
stoichiometry:c175 : 1
stoichiometry:c176 : 1
stoichiometry:c177 : 1
m98*m184*m17258*m183*m980*0.1
nodelay
--
0
PMID: 18086372 The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
p65
p65
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c178 : 1
stoichiometry:c179 : 1
stoichiometry:c180 : 1
m99*0.1
nodelay
--
0
PMID: 18086372 The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
p66
p66
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c181 : 1
stoichiometry:c183 : 1
stoichiometry:c202 : 1
stoichiometry:c278 : 1
stoichiometry:c185 : 1
m119368*m101*0.1
nodelay
--
0
PMID: 18086372 In addition to the TLRs, a new family of viral pattern recognition receptors consisting of RNA helicases retinoic acid inducible gene I (RIG-I), melanoma differentiation antigen 5 (MDA5) and laboratory of genetics and physiology 2 (LGP2) ? was discovered and characterized in the last 3 years. PMID: 18086372, 17190814 Saito et al. also identified an analogous RD within the C terminus of LGP2 suggesting that LGP2 might inhibit RIG-I through their RD interactions. PMID: 18086372, 15298172, 10933707 By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
p67
p67
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c182 : 1
stoichiometry:c184 : 1
stoichiometry:c279 : 1
stoichiometry:c293 : 1
stoichiometry:c186 : 1
m119368*m76904*0.1
nodelay
--
0
PMID: 18086372 In addition to the TLRs, a new family of viral pattern recognition receptors consisting of RNA helicases retinoic acid inducible gene I (RIG-I), melanoma differentiation antigen 5 (MDA5) and laboratory of genetics and physiology 2 (LGP2) ? was discovered and characterized in the last 3 years. PMID: 18086372, 15298172, 10933707 By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3. PMID: 18086372, 15563593, 17049367 The V proteins of this diverse group of viruses bind MDA5 via their highly conserved cysteine-rich C-terminal domain.This suggests that paramyxoviruses use this interaction to reduce the amount of IFN released by infected cells.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c187 : 1
stoichiometry:c188 : 1
stoichiometry:c280 : 1
stoichiometry:c189 : 1
m119368*m104*0.1
nodelay
--
0
PMID: 18086372 In addition to the TLRs, a new family of viral pattern recognition receptors consisting of RNA helicases retinoic acid inducible gene I (RIG-I), melanoma differentiation antigen 5 (MDA5) and laboratory of genetics and physiology 2 (LGP2) ? was discovered and characterized in the last 3 years. PMID: 18086372, 16116171 LGP2 is a close relative of RIG-I, which lacks the CARDs, but is capable of binding dsRNA. PMID: 18086372, 15298172, 10933707 By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c197 : 1
stoichiometry:c196 : 1
stoichiometry:c301 : 1
stoichiometry:c198 : 1
m68199*m102*0.1
nodelay
--
0
PMID: 18086372 The binding of dsRNA to the helicase domain of RIG-I likely induces a conformational change that exposes the N-terminal CARD domains to recruit its signaling adaptor IPS-1. PMID: 18086372, 16301520, 16177806 Hepatitis C virus (HCV) encodes the protease NS3/4A which targets IPS-1 by cleaving it at position Cys-508, thereby dislocating it from the mitochondrial membrane and thus abrogating further downstream signaling to type I IFN and NFkappaB-dependent target gene expression.
p7
p7
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c20 : 1
stoichiometry:c21 : 1
m18*m19823*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c190 : 1
stoichiometry:c192 : 1
stoichiometry:c191 : 1
m43*m105*0.1
nodelay
--
0
PMID: 18086372 These molecules, which are localized in the cytosol, bind specific RNA molecules derived from the genome of different RNA viruses and, with the exception of LGP2 which does not signal itself, trigger a signaling cascade leading to the production of type I IFNs and of proinflammatory cytokines in response to viral infection.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c193 : 1
stoichiometry:c195 : 1
stoichiometry:c194 : 1
m64*m105*0.1
nodelay
--
0
PMID: 18086372 These molecules, which are localized in the cytosol, bind specific RNA molecules derived from the genome of different RNA viruses and, with the exception of LGP2 which does not signal itself, trigger a signaling cascade leading to the production of type I IFNs and of proinflammatory cytokines in response to viral infection.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c199 : 1
stoichiometry:c200 : 1
stoichiometry:c201 : 1
m101*m104*0.1
nodelay
--
0
PMID: 18086372, 17190814 Saito et al. also identified an analogous RD within the C terminus of LGP2 suggesting that LGP2 might inhibit RIG-I through their RD interactions.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c203 : 1
stoichiometry:c204 : 1
stoichiometry:c205 : 1
m110*m977*0.1
nodelay
--
0
PMID: 18086372, 16153868 Coimmunoprecipitation experiments suggest that IPS-1 interacts with TBK1 and recruits endogenous IRF3 in a virus-inducible manner.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c206 : 1
stoichiometry:c207 : 1
stoichiometry:c208 : 1
m106*m1872*0.1
nodelay
--
0
PMID: 18086372, 16858409 Recently, TRAF3 was shown to be critically involved in IPS-1-mediated IFN-alpha production and antiviral responses through a direct interaction between the TRAF domain of TRAF3 and a TRAF interaction motif within IPS-1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c210 : 1
stoichiometry:c211 : 1
stoichiometry:c277 : 1
stoichiometry:c212 : 1
m106*m107*0.1
nodelay
--
0
PMID: 18086372, 16153868 Coimmunoprecipitation experiments suggest that IPS-1 interacts with TBK1 and recruits endogenous IRF3 in a virus-inducible manner. PMID: 18086372, 17079289 Furthermore, it was observed that NS1 colocalizes with RIG-I (Mibayashi et al., 2007), suggesting that NS1 forms a complex with RIG-I and IPS-1 during viral infection, resulting in inhibition of further downstream signaling.
p76
p76
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c209 : 1
stoichiometry:c284 : 1
stoichiometry:c287 : 1
stoichiometry:c288 : 1
stoichiometry:c213 : 1
stoichiometry:c214 : 1
m111*0.1
nodelay
--
0
PMID: 18086372, 16127453 This receptor?adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes. PMID: 18086372, 12885884 Two viral proteins of RSV, NS1 and NS2, are involved in blocking the pathway leading to IRF3 phosphorylation, although the activation of NFkappaB and AP-1 is unaffected. PMID: 18086372, 15919920 IRF3 phosphorylation by TBK1 was identified as target of the Rabies virus phosphoprotein P.
p77
p77
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c216 : 1
stoichiometry:c217 : 1
stoichiometry:c215 : 1
m98717*m109*0.1
nodelay
--
0
PMID: 18086372, 16858409 Recently, TRAF3 was shown to be critically involved in IPS-1-mediated IFN-alpha production and antiviral responses through a direct interaction between the TRAF domain of TRAF3 and a TRAF interaction motif within IPS-1.
p78
p78
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c218 : 1
stoichiometry:c219 : 1
stoichiometry:c220 : 1
stoichiometry:c221 : 1
m36*m106*m1814*0.1
nodelay
--
0
PMID: 18086372, 15549108 RIP1 and FADD are additional molecules that have been reported to be required for type I IFN production in response to dsRNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c222 : 1
stoichiometry:c224 : 1
stoichiometry:c223 : 1
m43*m112*0.1
nodelay
--
0
PMID: 18086372, 15549108 RIP1 and FADD are additional molecules that have been reported to be required for type I IFN production in response to dsRNA.
p8
p8
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c22 : 1
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m21*m19940*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
p80
p80
cso30:i:ME_UnknownActivation
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c225 : 1
stoichiometry:c227 : 1
stoichiometry:c228 : 1
stoichiometry:c226 : 1
m107*m109*m3897*0.1
nodelay
--
0
PMID: 18086372, 17327220 There is evidence that the TBK1/IKK-epsilon adaptor protein TANK plays a role in IPS-1-TRAF3-mediated activation of TBK1/IKK-epsilon.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c229 : 1
stoichiometry:c230 : 1
stoichiometry:c231 : 1
m183*m106*0.1
nodelay
--
0
PMID: 18086372, 16125763, 16153868 IPS-1 binds to TRAF6 upon overexpression in mammalian cells and in a yeast-two hybrid screen reported that endogenous IPS-1 also interacts with TRAF6.
p82
p82
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c232 : 1
stoichiometry:c234 : 1
stoichiometry:c233 : 1
m1637*m114*0.1
nodelay
--
0
PMID: 18086372 Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c236 : 1
stoichiometry:c235 : 1
m42*0.1
nodelay
--
0
PMID: 18086372 Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta.
p84
p84
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c237 : 1
stoichiometry:c238 : 1
stoichiometry:c239 : 1
m101*m115*0.1
nodelay
--
0
PMID: 18086372, 17038590 Taken together, the results of Hornung et al.(2006) show that RIG-I directly recognizes 5¡ì-triphosphate single stranded or double stranded RNA independently of viral replication.
p85
p85
cso30:i:ME_ProteinCleavage
cso30:i:CC_Cell_WithoutCellWall_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c240 : 1
stoichiometry:c243 : 1
stoichiometry:c241 : 1
stoichiometry:c242 : 1
m76904*m1822*0.1
nodelay
--
0
PMID: 18086372, 12015121 It was reported in a previous publication, that MDA5, which was then called Helicard, is cleaved by caspases upon induction of apoptosis, thereby separating the CARD domains from the C-terminal helicase domain, which localizes to the nucleus where it is involved in DNA degradation and nuclear remodelling during apoptotic cell death.
p86
p86
cso30:i:ME_Translocation
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c244 : 1
stoichiometry:c245 : 1
m118*0.1
nodelay
--
0
PMID: 18086372, 12015121 It was reported in a previous publication, that MDA5, which was then called Helicard, is cleaved by caspases upon induction of apoptosis, thereby separating the CARD domains from the C-terminal helicase domain, which localizes to the nucleus where it is involved in DNA degradation and nuclear remodelling during apoptotic cell death.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c250 : 1
stoichiometry:c247 : 1
m66*0.1
nodelay
--
0
PMID: 18086372 MDA5 is ubiquitously expressed in low abundance and similarly to RIG-I and LGP2 its expression is induced by type I IFN.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c251 : 1
stoichiometry:c248 : 1
m66*0.1
nodelay
--
0
PMID: 18086372 MDA5 is ubiquitously expressed in low abundance and similarly to RIG-I and LGP2 its expression is induced by type I IFN.
p89
p89
cso30:i:ME_DNAFragmentationDuringApoptosis
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
PMID: 18086372, 12015121 It was reported in a previous publication, that MDA5, which was then called Helicard, is cleaved by caspases upon induction of apoptosis, thereby separating the CARD domains from the C-terminal helicase domain, which localizes to the nucleus where it is involved in DNA degradation and nuclear remodelling during apoptotic cell death.
p9
p9
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
stoichiometry:c27 : 1
m21*m19823*0.1
nodelay
--
0
PMID: 18086372, 14976262, 11812998, 14976261 GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c252 : 1
stoichiometry:c249 : 1
m66*0.1
nodelay
--
0
PMID: 18086372 MDA5 is ubiquitously expressed in low abundance and similarly to RIG-I and LGP2 its expression is induced by type I IFN.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c253 : 1
stoichiometry:c254 : 1
stoichiometry:c302 : 1
stoichiometry:c255 : 1
m103*m68199*0.1
nodelay
--
0
PMID: 18086372 Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively. PMID: 18086372, 16301520, 16177806 Hepatitis C virus (HCV) encodes the protease NS3/4A which targets IPS-1 by cleaving it at position Cys-508, thereby dislocating it from the mitochondrial membrane and thus abrogating further downstream signaling to type I IFN and NFkappaB-dependent target gene expression.
p92
p92
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c256 : 1
stoichiometry:c257 : 1
stoichiometry:c258 : 1
stoichiometry:c259 : 1
m123*m3902*m1599*0.1
nodelay
--
0
PMID: 18086372 Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
p93
p93
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c260 : 1
stoichiometry:c267 : 1
stoichiometry:c261 : 1
m980*m124*0.1
nodelay
--
0
PMID: 18086372 Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
p94
p94
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c262 : 1
stoichiometry:c264 : 1
stoichiometry:c263 : 1
m1637*m123*0.1
nodelay
--
0
PMID: 18086372 Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
p95
p95
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c265 : 1
stoichiometry:c268 : 1
stoichiometry:c283 : 1
stoichiometry:c286 : 1
stoichiometry:c289 : 1
stoichiometry:c266 : 1
m977*m124*0.1
nodelay
--
0
PMID: 18086372 Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively. PMID: 18086372, 12885884 Two viral proteins of RSV, NS1 and NS2, are involved in blocking the pathway leading to IRF3 phosphorylation, although the activation of NFkappaB and AP-1 is unaffected. PMID: 18086372, 15919920 IRF3 phosphorylation by TBK1 was identified as target of the Rabies virus phosphoprotein P.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c270 : 1
stoichiometry:c269 : 1
m123*0.1
nodelay
--
0
PMID: 18086372 In addition, it was shown that MDA5 might also play a role in the measles virus (MV) induced activation of IFN-beta mRNA synthesis since A549 cells transfected with MDA5 showed a strong activation of the IFN-beta promoter upon infection with MV.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c271 : 1
stoichiometry:c272 : 1
stoichiometry:c273 : 1
m69*m119368*0.1
nodelay
--
0
PMID: 18086372, 15298172, 10933707 By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c274 : 1
stoichiometry:c275 : 1
stoichiometry:c276 : 1
m69*m106*0.1
nodelay
--
0
PMID: 18086372, 17079289 Furthermore, it was observed that NS1 colocalizes with RIG-I (Mibayashi et al., 2007), suggesting that NS1 forms a complex with RIG-I and IPS-1 during viral infection, resulting in inhibition of further downstream signaling.
p99
p99
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c290 : 1
stoichiometry:c291 : 1
stoichiometry:c292 : 1
m76904*m130*0.1
nodelay
--
0
PMID: 18086372, 15563593, 17049367 The V proteins of this diverse group of viruses bind MDA5 via their highly conserved cysteine-rich C-terminal domain.This suggests that paramyxoviruses use this interaction to reduce the amount of IFN released by infected cells.
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: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:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
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:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputProcess
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:InputProcess
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
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: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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
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0
1,
--
cso30:c:InputProcess
threshold
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0
1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:OutputProcess
threshold
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0
1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:InputProcess
threshold
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1,
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cso30:c:InputProcess
threshold
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1,
--
cso30:c:OutputProcess
threshold
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1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:OutputProcess
threshold
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1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:InputProcess
threshold
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0
1,
--
cso30:c:InputProcess
threshold
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1,
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cso30:c:InputAssociation
threshold
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1,
--
cso30:c:InputProcess
threshold
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1,
--
cso30:c:InputAssociation
threshold
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1,
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cso30:c:OutputProcess
threshold
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1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:InputAssociation
threshold
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1,
--
cso30:c:InputAssociation
threshold
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0
1,
--
cso30:c:InputProcess
threshold
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1,
--
cso30:c:InputProcess
threshold
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1,
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cso30:c:InputProcess
threshold
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1,
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cso30:c:InputProcess
threshold
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cso30:c:InputProcess
threshold
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cso30:c:InputProcess
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:InputAssociation
threshold
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cso30:c:InputProcess
threshold
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cso30:c:InputAssociation
threshold
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1,
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cso30:c:InputAssociation
threshold
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cso30:c:InputAssociation
threshold
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cso30:c:InputProcess
threshold
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cso30:c:InputProcess
threshold
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cso30:c:InputProcess
threshold
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cso30:c:InputInhibitor
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cso30:c:InputInhibitor
threshold
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0
1,
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cso30:c:InputInhibitor
threshold
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0
1,
--
cso30:c:InputProcess
threshold
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0
1,
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cso30:c:InputInhibitor
threshold
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cso30:c:InputInhibitor
threshold
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cso30:c:InputInhibitor
threshold
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cso30:c:InputInhibitor
threshold
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cso30:c:InputInhibitor
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cso30:c:InputInhibitor
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cso30:c:InputInhibitor
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cso30:c:InputInhibitor
threshold
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cso30:c:InputInhibitor
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cso30:c:InputInhibitor
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputInhibitor
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputAssociation
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cso30:c:InputProcess
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cso30:c:OutputProcess
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cso30:c:InputInhibitor
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cso30:c:InputInhibitor
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cso30:c:OutputProcess
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:OutputProcess
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cso30:c:OutputProcess
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cso30:c:InputProcess
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:OutputProcess
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cso30:c:InputProcess
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cso30:c:InputAssociation
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:OutputProcess
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:InputAssociation
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:InputAssociation
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cso30:c:InputProcess
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cso30:c:InputProcess
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cso30:c:OutputProcess
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cso30:c:OutputProcess
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cso30:c:OutputProcess
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cso30:c:InputAssociation
threshold
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cso30:c:InputAssociation
threshold
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cso30:c:InputAssociation
threshold
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1,
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cso30:c:OutputProcess
threshold
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1,
--
cso30:c:InputAssociation
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0
1,
--
cso30:c:InputAssociation
threshold
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--