Original Literature | Model OverView |
---|---|
Publication
Title
Antiviral innate immunity pathways.
Affiliation
Howard Hughes Medical Institute, Department of Molecular Biology, University ofTexas Southwestern Medical Center, Dallas, TX 75390-9148, USA.
Abstract
Recent studies have uncovered two signaling pathways that activate the hostinnate immunity against viral infection. One of the pathways utilizes members ofthe Toll-like receptor (TLR) family to detect viruses that enter the endosomethrough endocytosis. The TLR pathway induces interferon production throughseveral signaling proteins that ultimately lead to the activation of thetranscription factors NF-kappaB, IRF3 and IRF7. The other antiviral pathway usesthe RNA helicase RIG-I as the receptor for intracellular viral double-strandedRNA. RIG-I activates NF-kappaB and IRFs through the recently identified adaptorprotein MAVS, a CARD domain containing protein that resides in the mitochondrialmembrane. MAVS is essential for antiviral innate immunity, but it also serves asa target of Hepatitis C virus (HCV), which employs a viral protease to cleaveMAVS off the mitochondria, thereby allowing HCV to escape the host immunesystem.
PMID
16474426
|
Entity
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(IRAK-1)
--
MO000000213
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m184
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000213 |
--
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 |
--
ISGF-3gamma(IRF9)
--
MO000007758
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m991
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007758 |
--
STAT1
--
MO000013119
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1357
10
infinite
0
InterPro | IPR008967 |
TRANSPATH | MO000013119 |
--
STAT2
--
MO000013120
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1358
10
infinite
0
InterPro | IPR008967 |
TRANSPATH | MO000013120 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
IKK-i
--
MO000016608
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1599
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016608 |
--
TRAF3
--
MO000016963
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1872
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000016963 |
--
TBK1
--
MO000019331
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3902
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000019331 |
--
protein remnants
--
MO000019479
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m360980
10
infinite
0
TRANSPATH | MO000019479 |
--
STAT1{p}
--
MO000019704
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m4238
10
infinite
0
TRANSPATH | MO000019704 |
--
IKK-beta{p}
--
MO000038329
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m16544
10
infinite
0
TRANSPATH | MO000038329 |
--
TRIF
--
MO000041125
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m18998
10
infinite
0
TRANSPATH | MO000041125 |
--
dsRNA:TLR3
--
MO000041446
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19314
10
infinite
0
TRANSPATH | MO000041446 |
--
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 |
--
ATF-2:c-Jun
--
MO000055971
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m31298
10
infinite
0
TRANSPATH | MO000055971 |
--
MAVS
--
MO000094908
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m68199
10
infinite
0
TRANSPATH | MO000094908 |
--
--
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
--
IL-1betaR
--
e11
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m11
0
infinite
0
--
IL-1beta:IL-1betaR
--
e12
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m12
0
infinite
0
--
TNF-alpha:TNFR
--
e13
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m13
0
infinite
0
--
NF-kappaB:IkappaB
--
e14
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m14
0
infinite
0
--
NF-kappaB:IkappaB{p}
--
e15
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m15
0
infinite
0
--
NF-kappaB:IkappaB{p}{ub}
--
e16
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m16
0
infinite
0
--
NF-kappaB{active}
--
e17
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m18
10
infinite
0
TRANSPATH | MO000000058 |
--
(IRF-3{p})2
--
e18
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m19
0
infinite
0
--
(IRF-3{p})2
--
e19
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m20
0
infinite
0
--
--
e2
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m2
0
infinite
0
--
MAVS:DDX58
--
e21
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m22
0
infinite
0
--
ATF-2{p}:c-Jun{p}
--
e23
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m26
10
infinite
0
TRANSPATH | MO000055971 |
--
csml-variable:Double
m27
0
infinite
0
--
IFN-beta:enhanceosome complex
--
e25
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m28
0
infinite
0
--
enhancesome complex
--
e26
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m29
0
infinite
0
--
IFN-beta:IFN-betaR
--
e28
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m31
0
infinite
0
--
IFN-betaR
--
e29
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m32
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
Jak1{active}
--
e30
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m33
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000145 |
--
Tyk2{active}
--
e31
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m34
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000148 |
--
STAT2{p}
--
e32
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m35
0
infinite
0
--
STAT1{p}:STAT2{p}:IRF9
--
e34
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m37
0
infinite
0
--
csml-variable:Double
m38
0
infinite
0
--
csml-variable:Double
m39
0
infinite
0
--
csml-variable:Double
m40
0
infinite
0
--
csml-variable:Double
m41
0
infinite
0
--
csml-variable:Double
m42
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
LPS:TLR4
--
e40
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m43
0
infinite
0
--
flagellin:TLR5
--
e41
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m44
0
infinite
0
--
LPS:TLR4:MYD88
--
e42
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m45
0
infinite
0
--
LPS:TLR4:MYD88:IRAK1:IRAK4:TRAF6
--
e44
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m47
0
infinite
0
--
LPS:TLR4:MYD88:IRAK1:IRAK4:TRAF6{ub}
--
e45
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m48
0
infinite
0
--
Ubc13:Uev1A
--
e46
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m49
0
infinite
0
--
TAK1:TAB1:TAB2
--
e47
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m63
0
infinite
0
--
TAK1:TAB1:TAB2 {active}
--
e48
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m64
0
infinite
0
--
dsRNA:TLR3:TRIF
--
e49
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m65
0
infinite
0
--
dsRNA:DDX58
--
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
--
--
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:TRIF
--
e63
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m66
0
infinite
0
--
dsRNA:TLR3:TRIF:RIP1:TRAF6
--
e64
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m67
0
infinite
0
--
NF-kappaB{active}
--
e65
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m69
10
infinite
0
TRANSPATH | MO000000058 |
--
dsRNA:TLR3:TRIF:RIP1:TRAF6:TBK1
--
e66
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m70
0
infinite
0
--
MYD88:TRAF3
--
e67
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m71
0
infinite
0
--
TRIF:TRAF3
--
e68
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m72
0
infinite
0
--
--
e69
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
csml-variable:Double
m73
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_Endosome
--
--
--
csml-variable:Double
m74
0
infinite
0
--
--
e71
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m75
0
infinite
0
--
ssRNA
--
e72
cso30:c:Rna
cso30:i:CC_Cytosol
--
csml-variable:Double
m76
0
infinite
0
--
ssRNA:TLR8
--
e73
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m77
0
infinite
0
--
ssRNA:TLR7
--
e74
cso30:c:Complex
cso30:i:CC_EndosomeMembrane
--
--
csml-variable:Double
m78
0
infinite
0
--
csml-variable:Double
m79
0
infinite
0
--
CpG DNA: TLR9
--
e76
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m80
0
infinite
0
--
MYD88:TRAF6:IRF7
--
e77
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m81
0
infinite
0
--
MYD88:TRAF6:IRF7:IRAK1
--
e78
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m82
0
infinite
0
--
MYD88:TRAF6{ub}:IRF7:IRAK1
--
e79
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m83
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
MAVS:TRAF6
--
e81
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m85
0
infinite
0
--
FADD:RIP1:MAVS
--
e82
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m86
0
infinite
0
--
MAVS:IKK-alpha
--
e83
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m87
0
infinite
0
--
MAVS:IKK-i
--
e84
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m88
0
infinite
0
--
csml-variable:Double
m89
0
infinite
0
--
MAVS:NS3/4A
--
e86
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m90
0
infinite
0
--
MYD88:TRAF6{ub}:IRAK1
--
e88
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m92
0
infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0
infinite
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m119368*m41844*0.1
nodelay
--
0
PMID: 16474426, 15208624 retinoic acid inducible gene ? I (RIG-I) has been identified as a cytosolic receptor for intracellular dsRNA.
p10
p10
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c26 : 1
stoichiometry:c28 : 1
stoichiometry:c27 : 1
m977*m1599*0.1
nodelay
--
0
PMID: 16474426, 12692549, 12702806 In response to a viral challenge, IRF3 is phosphorylated by the IKK-like kinases TBK-1 and IKKe.
p11
p11
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c29 : 1
stoichiometry:c31 : 1
stoichiometry:c30 : 1
m977*m3902*0.1
nodelay
--
0
PMID: 16474426, 12692549, 12702806 In response to a viral challenge, IRF3 is phosphorylated by the IKK-like kinases TBK-1 and IKKe.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c32 : 1
stoichiometry:c33 : 1
m19324*0.1
nodelay
--
0
PMID: 16474426 Phosphorylation of IRF3 leads to its dimerization and translocation into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c34 : 1
stoichiometry:c35 : 1
m19*0.1
nodelay
--
0
PMID: 16474426 Phosphorylation of IRF3 leads to its dimerization and translocation into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c36 : 1
stoichiometry:c37 : 1
m21*0.1
nodelay
--
0
PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c38 : 1
stoichiometry:c39 : 1
m24*0.1
nodelay
--
0
PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus.
p16
p16
cso30:i:ME_Phosphorylation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c40 : 1
stoichiometry:c45 : 1
stoichiometry:c41 : 1
m31298*m25*0.1
nodelay
--
0
PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus.
p17
p17
cso30:i:ME_Phosphorylation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c42 : 1
stoichiometry:c44 : 1
stoichiometry:c43 : 1
m31298*m23*0.1
nodelay
--
0
PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c46 : 1
stoichiometry:c53 : 1
stoichiometry:c47 : 1
m27*m29*0.1
nodelay
--
0
PMID: 16474426 Together with the nuclear architectural protein HMG-I (Y), NF-kappaB, IRF3 and ATF2/c-Jun assemble into a stereospecific enhanceosome complex that remodels the chromatin in the promoter of IFN-beta, resulting in its transcriptional initiation.
p19
p19
cso30:i:ME_Binding
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c48 : 1
stoichiometry:c49 : 1
stoichiometry:c50 : 1
stoichiometry:c51 : 1
stoichiometry:c52 : 1
m23351*m18*m20*m26*0.1
nodelay
--
0
PMID: 16474426 Together with the nuclear architectural protein HMG-I (Y), NF-kappaB, IRF3 and ATF2/c-Jun assemble into a stereospecific enhanceosome complex that remodels the chromatin in the promoter of IFN-beta, resulting in its transcriptional initiation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c12 : 1
stoichiometry:c5 : 1
m207*m12*0.1
nodelay
--
0
PMID: 16474426 In the presence of diverse stimuli, such as IL-1beta, TNF-alpha, and viruses, the IkappaB kinase (IKK) is activated and it then phosphorylates IkappaB.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c55 : 1
stoichiometry:c54 : 1
m28*0.1
nodelay
--
0
PMID: 16474426 Together with the nuclear architectural protein HMG-I (Y), NF-kappaB, IRF3 and ATF2/c-Jun assemble into a stereospecific enhanceosome complex that remodels the chromatin in the promoter of IFN-beta, resulting in its transcriptional initiation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c57 : 1
stoichiometry:c163 : 1
stoichiometry:c58 : 1
m32*m1636*0.1
nodelay
--
0
PMID: 16474426, 16214811 IFN-beta binds to the IFNalpha/beta receptor (IFNAR) in autocrine and paracrine manner to initiate a positive feedback loop that results in further production of type I IFNs.
p22
p22
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c70 : 1
stoichiometry:c69 : 1
m1357*m34*0.1
nodelay
--
0
PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins.
p23
p23
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c59 : 1
stoichiometry:c63 : 1
stoichiometry:c60 : 1
m129*m31*0.1
nodelay
--
0
PMID: 16474426 IFNARs trigger the activation of the janus kinase (JAK) family members JAK1 and Tyk-2.
p24
p24
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c61 : 1
stoichiometry:c64 : 1
stoichiometry:c62 : 1
m132*m31*0.1
nodelay
--
0
PMID: 16474426 IFNARs trigger the activation of the janus kinase (JAK) family members JAK1 and Tyk-2.
p25
p25
cso30:i:ME_Phosphorylation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c65 : 1
stoichiometry:c67 : 1
stoichiometry:c66 : 1
m1357*m33*0.1
nodelay
--
0
PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins.
p26
p26
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c71 : 1
stoichiometry:c73 : 1
stoichiometry:c72 : 1
m1358*m33*0.1
nodelay
--
0
PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins.
p27
p27
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c74 : 1
stoichiometry:c76 : 1
stoichiometry:c75 : 1
m1358*m34*0.1
nodelay
--
0
PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins.
p28
p28
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c78 : 1
stoichiometry:c79 : 1
stoichiometry:c56 : 1
stoichiometry:c80 : 1
m35*m4238*m991*0.1
nodelay
--
0
PMID: 16474426 These transcription factors associate with IRF9 to form a heterotrimeric complex, IFN-stimulated gene factor 3 (ISGF3).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c81 : 1
stoichiometry:c83 : 1
stoichiometry:c82 : 1
m38*m37*0.1
nodelay
--
0
PMID: 16474426 ISGF3 initiates the transcription of several interferon stimulated genes (ISGs) by binding to the IFN-stimulated response elements (ISRE) in their promoter regions.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c6 : 1
stoichiometry:c7 : 1
stoichiometry:c8 : 1
m1591*m11*0.1
nodelay
--
0
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c84 : 1
stoichiometry:c115 : 1
m93217*0.1
nodelay
--
0
PMID: 16474426 IFN-beta produced in response to a viral challenge by the IRF3 dependent pathway described above, induces transcription of IRF-7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c88 : 1
stoichiometry:c89 : 1
m93631*0.1
nodelay
--
0
PMID: 16474426 IFN-beta produced in response to a viral challenge by the IRF3 dependent pathway described above, induces transcription of IRF-7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c87 : 1
stoichiometry:c86 : 1
m31*0.1
nodelay
--
0
PMID: 16474426 IFN-beta produced in response to a viral challenge by the IRF3 dependent pathway described above, induces transcription of IRF-7.
p33
p33
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c90 : 1
stoichiometry:c95 : 1
stoichiometry:c91 : 1
m980*m1599*0.1
nodelay
--
0
PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene.
p34
p34
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c92 : 1
stoichiometry:c94 : 1
stoichiometry:c93 : 1
m980*m3902*0.1
nodelay
--
0
PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene.
p35
p35
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c101 : 1
stoichiometry:c102 : 1
stoichiometry:c103 : 1
m3965*m119368*0.1
nodelay
--
0
PMID: 16474426 TLR3 recognizes viral double-stranded RNA, TLR4 recognizes bacterial lipopolysaccharides (LPS), whereas TLR5 is a receptor for bacterial flagellin.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c96 : 1
stoichiometry:c171 : 1
stoichiometry:c97 : 1
m40*m84*0.1
nodelay
--
0
PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c99 : 1
stoichiometry:c100 : 1
m41*0.1
nodelay
--
0
PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene.
p38
p38
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c105 : 1
stoichiometry:c106 : 1
stoichiometry:c104 : 1
m3961*m155666*0.1
nodelay
--
0
PMID: 16474426 TLR3 recognizes viral double-stranded RNA, TLR4 recognizes bacterial lipopolysaccharides (LPS), whereas TLR5 is a receptor for bacterial flagellin.
p39
p39
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c107 : 1
stoichiometry:c108 : 1
stoichiometry:c109 : 1
m6485*m3966*0.1
nodelay
--
0
PMID: 16474426 TLR3 recognizes viral double-stranded RNA, TLR4 recognizes bacterial lipopolysaccharides (LPS), whereas TLR5 is a receptor for bacterial flagellin.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c9 : 1
stoichiometry:c10 : 1
stoichiometry:c11 : 1
m230*m176*0.1
nodelay
--
0
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c110 : 1
stoichiometry:c111 : 1
stoichiometry:c112 : 1
m43*m1572*0.1
nodelay
--
0
PMID: 16474426 Except for TLR3, all TLRs utilize MyD88 as an adaptor protein to recruit downstream signaling molecules including the protein kinases IRAK4 and IRAK1, and the RING domain ubiquitin ligase TRAF6.
p41
p41
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c113 : 1
stoichiometry:c114 : 1
stoichiometry:c116 : 1
stoichiometry:c204 : 1
stoichiometry:c117 : 1
m45*m17258*m183*m184*0.1
nodelay
--
0
PMID: 16474426 Except for TLR3, all TLRs utilize MyD88 as an adaptor protein to recruit downstream signaling molecules including the protein kinases IRAK4 and IRAK1, and the RING domain ubiquitin ligase TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c118 : 1
stoichiometry:c120 : 1
stoichiometry:c119 : 1
m47*m49*0.1
nodelay
--
0
PMID: 16474426, 11057907, 11460167 TRAF6 functions together with a dimeric ubiquitin conjugating enzyme complex Ubc13-Uev1A to catalyze the synthesis of Lys63-linked polyubiquitin chains that lead to the activation of a protein kinase complex consisting of TAK1, TAB1 and TAB2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c121 : 1
stoichiometry:c123 : 1
stoichiometry:c122 : 1
m63*m48*0.1
nodelay
--
0
PMID: 16474426, 11057907, 11460167 TRAF6 functions together with a dimeric ubiquitin conjugating enzyme complex Ubc13-Uev1A to catalyze the synthesis of Lys63-linked polyubiquitin chains that lead to the activation of a protein kinase complex consisting of TAK1, TAB1 and TAB2.
p44
p44
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c124 : 1
stoichiometry:c126 : 1
stoichiometry:c125 : 1
m182*m64*0.1
nodelay
--
0
PMID: 16474426 The activated TAK1 kinase phosphorylates IKKbeta in the activation loop, resulting in the activation of IKK and subsequent nuclear translocation of NF-kappaB.
p45
p45
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c127 : 1
stoichiometry:c128 : 1
stoichiometry:c129 : 1
m19314*m18998*0.1
nodelay
--
0
PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c131 : 1
stoichiometry:c132 : 1
stoichiometry:c130 : 1
m18998*m43*0.1
nodelay
--
0
PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB.
p47
p47
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c133 : 1
stoichiometry:c134 : 1
stoichiometry:c136 : 1
stoichiometry:c135 : 1
m65*m183*m68*0.1
nodelay
--
0
PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB.
p48
p48
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c139 : 1
stoichiometry:c138 : 1
m17*m67*0.1
nodelay
--
0
PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c140 : 1
stoichiometry:c141 : 1
stoichiometry:c142 : 1
m3902*m67*0.1
nodelay
--
0
PMID: 16474426 TRIF can also bind to TBK1, which phosphorylates and activates IRF3 and IRF7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c15 : 1
stoichiometry:c14 : 1
m207*m13*0.1
nodelay
--
0
PMID: 16474426 In the presence of diverse stimuli, such as IL-1beta, TNF-alpha, and viruses, the IkappaB kinase (IKK) is activated and it then phosphorylates IkappaB.
p50
p50
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c143 : 1
stoichiometry:c144 : 1
stoichiometry:c145 : 1
m1872*m1572*0.1
nodelay
--
0
PMID: 16474426, 16306937, 16306936 Recent studies have also shown that TRIF and MyD88 can bind to TRAF3.
p51
p51
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c146 : 1
stoichiometry:c147 : 1
stoichiometry:c148 : 1
m18998*m1872*0.1
nodelay
--
0
PMID: 16474426, 16306937, 16306936 Recent studies have also shown that TRIF and MyD88 can bind to TRAF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c149 : 1
stoichiometry:c150 : 1
stoichiometry:c151 : 1
m19823*m76*0.1
nodelay
--
0
PMID: 16474426 TLR7 and TLR8 are receptors for G/U-rich ssRNA associated with viruses that enter cells through endocytosis.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c152 : 1
stoichiometry:c153 : 1
stoichiometry:c154 : 1
m19940*m76*0.1
nodelay
--
0
PMID: 16474426 TLR7 and TLR8 are receptors for G/U-rich ssRNA associated with viruses that enter cells through endocytosis.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c155 : 1
stoichiometry:c156 : 1
stoichiometry:c157 : 1
m19828*m79*0.1
nodelay
--
0
PMID: 16474426 TLR9 recognizes unmethylated CpG DNA present in DNA viruses such as herpesvirus.
p55
p55
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c159 : 1
stoichiometry:c160 : 1
stoichiometry:c158 : 1
stoichiometry:c161 : 1
m183*m980*m1572*0.1
nodelay
--
0
PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c162 : 1
stoichiometry:c205 : 1
stoichiometry:c164 : 1
m81*m184*0.1
nodelay
--
0
PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7.
p57
p57
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c165 : 1
stoichiometry:c166 : 1
stoichiometry:c197 : 1
m83*0.1
nodelay
--
0
PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c167 : 1
stoichiometry:c169 : 1
stoichiometry:c168 : 1
m82*m49*0.1
nodelay
--
0
PMID: 16474426, 15361868 TRAF6 appears to induce the phosphorylation of IRF7 through a mechanism that involves Ubc13-catalyzed K63 polyubiquitination.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c98 : 1
stoichiometry:c170 : 1
m19325*0.1
nodelay
--
0
PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c18 : 1
stoichiometry:c17 : 1
m14*m6*0.1
nodelay
--
0
PMID: 16474426 In the presence of diverse stimuli, such as IL-1beta, TNF-alpha, and viruses, the IkappaB kinase (IKK) is activated and it then phosphorylates IkappaB.
p60
p60
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c172 : 1
stoichiometry:c173 : 1
stoichiometry:c174 : 1
m68199*m41844*0.1
nodelay
--
0
PMID: 16474426 MAVS has been shown to interact with RIG-I in over-expression experiments.
p61
p61
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
m68199*m183*0.1
nodelay
--
0
PMID: 16474426, 16125763, 16153868 MAVS can interact with TRAF6 and both identified TRAF6 binding sites within MAVS.
p62
p62
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c178 : 1
stoichiometry:c179 : 1
stoichiometry:c180 : 1
stoichiometry:c181 : 1
m68199*m1814*m68*0.1
nodelay
--
0
PMID: 16474426, 16127453 MAVS interacted with RIP-1 and FADD, and proposed that these molecules linked MAVS to IKK activation.
p63
p63
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c182 : 1
stoichiometry:c184 : 1
stoichiometry:c183 : 1
m207*m86*0.1
nodelay
--
0
PMID: 16474426, 16127453 MAVS interacted with RIP-1 and FADD, and proposed that these molecules linked MAVS to IKK activation.
p64
p64
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c185 : 1
stoichiometry:c186 : 1
stoichiometry:c187 : 1
m181*m68199*0.1
nodelay
--
0
PMID: 16474426 MAVS bound to IKK alpha and IKK-epsilon directly.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c191 : 1
stoichiometry:c192 : 1
stoichiometry:c193 : 1
m68199*m89*0.1
nodelay
--
0
PMID: 16474426 NS3/4A binds to and co-localizes with MAVS in the mitochondrial membrane, and it can cleave MAVS directly in vitro.
p66
p66
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c188 : 1
stoichiometry:c189 : 1
stoichiometry:c190 : 1
m68199*m1599*0.1
nodelay
--
0
PMID: 16474426 MAVS bound to IKK alpha and IKK-epsilon directly.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c194 : 1
stoichiometry:c196 : 1
stoichiometry:c195 : 1
m90*0.1
nodelay
--
0
PMID: 16474426 NS3/4A binds to and co-localizes with MAVS in the mitochondrial membrane, and it can cleave MAVS directly in vitro.
p68
p68
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c198 : 1
stoichiometry:c200 : 1
stoichiometry:c199 : 1
m17*m5*0.1
nodelay
--
0
PMID: 16474426 Over-expression of the N-terminal region of RIG-I comprising the two CARD domains is sufficient to activate NF-kappaB and IRF3 in the absence of a viral challenge, whereas the full-length RIG-I is activated only in the presence of dsRNA.
p69
p69
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c201 : 1
stoichiometry:c203 : 1
stoichiometry:c202 : 1
m977*m5*0.1
nodelay
--
0
PMID: 16474426 Over-expression of the N-terminal region of RIG-I comprising the two CARD domains is sufficient to activate NF-kappaB and IRF3 in the absence of a viral challenge, whereas the full-length RIG-I is activated only in the presence of dsRNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c20 : 1
m15*0.1
nodelay
--
0
PMID: 16474426 Once phosphorylated, IkappaB is ubiquitinated and subsequently degraded by the proteasome.
p8
p8
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c21 : 1
stoichiometry:c22 : 1
stoichiometry:c23 : 1
m16*0.1
nodelay
--
0
PMID: 16474426 Once phosphorylated, IkappaB is ubiquitinated and subsequently degraded by the proteasome.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c24 : 1
stoichiometry:c25 : 1
m69*0.1
nodelay
--
0
PMID: 16474426 Free NF-kappaB then translocates into the nucleus and turns on its target genes.
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: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:InputAssociation
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: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: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: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: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: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:InputProcess
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: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: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:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
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:InputProcess
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: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: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: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: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:OutputProcess
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,
--