Entity
Process
PI3K
--
MO000000030
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m73
10
infinite
0
TRANSPATH | MO000000030 |
--
NF-kappaB
--
MO000000058
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m69
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 |
--
IKK
--
MO000000248
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m207
10
infinite
0
TRANSPATH | MO000000248 |
--
TNF-alpha
--
MO000000289
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m230
10
infinite
0
InterPro | IPR003636 |
TRANSPATH | MO000000289 |
--
IRF-3
--
MO000007694
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m977
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007694 |
--
IRAK-2
--
MO000016566
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1569
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016566 |
--
IRAK-M
--
MO000016569
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1571
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016569 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
fibrinogen
--
MO000017426
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m2254
10
infinite
0
TRANSPATH | MO000017426 |
--
fibronectin
--
MO000017549
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m2341
10
infinite
0
InterPro | IPR006209 |
TRANSPATH | MO000017549 |
--
TLR4
--
MO000019394
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3961
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000019394 |
--
LPS:LBP:CD14
--
MO000021929
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m6255
10
infinite
0
TRANSPATH | MO000021929 |
--
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 |
--
SIGIRR
--
MO000066718
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m41575
10
infinite
0
TRANSPATH | MO000066718 |
--
--
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
--
MKK
--
e100
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m103
0
infinite
0
--
MKK{p}
--
e101
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m104
0
infinite
0
--
LPS:TLR4:MD2:TRAM
--
e102
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m105
0
infinite
0
--
LPS:TLR4:MYD88:IRAK4{p}
--
e103
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m106
0
infinite
0
--
MYD88s
--
e104
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m107
0
infinite
0
--
diacylated lipopeptide:TLR2:TLR6:PI3K
--
e105
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m108
0
infinite
0
--
LPS:TLR4:MD2:Tollip
--
e106
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m109
0
infinite
0
--
MDP
--
e107
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m110
0
infinite
0
--
MDP:Nod2
--
e108
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m111
0
infinite
0
--
ST2L:MYD88
--
e109
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m112
0
infinite
0
--
diacylated lipopeptide
--
e11
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m11
0
infinite
0
--
ST2s
--
e110
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m113
0
infinite
0
--
LPS:TLR4:MD2:SIGIRR
--
e111
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m114
0
infinite
0
--
IL-1R
--
e112
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m115
0
infinite
0
--
IL-1:IL-1R
--
e113
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m116
0
infinite
0
--
IL-1
--
e114
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m117
0
infinite
0
--
IL-1:IL-1R:SIGIRR
--
e115
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m118
0
infinite
0
--
MAL
--
e116
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m119
0
infinite
0
--
ST2L:MAL
--
e117
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m120
0
infinite
0
--
diacylated lipoprotein:TLR2:TLR6
--
e12
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m12
0
infinite
0
--
triacylated lipopeptide
--
e13
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m13
0
infinite
0
--
triacylated lipopeptide:TLR1:TLR2
--
e14
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m14
0
infinite
0
--
taxol
--
e15
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m15
0
infinite
0
--
taxol:TLR4
--
e16
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m16
0
infinite
0
--
viral fusion protein
--
e17
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m17
0
infinite
0
--
viral fusion protein:TLR4
--
e18
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m18
0
infinite
0
--
hsp60:TLR4
--
e19
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m19
0
infinite
0
--
--
e2
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m2
0
infinite
0
--
hsp70:TLR4
--
e20
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m20
0
infinite
0
--
fibronectin:TLR4
--
e21
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m21
0
infinite
0
--
flagellin:TLR5
--
e22
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m22
0
infinite
0
--
hyaluronic acid:TLR4
--
e23
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m23
0
infinite
0
--
hyaluronic acid
--
e24
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m24
0
infinite
0
--
fibrinogen:TLR4
--
e25
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m25
0
infinite
0
--
heparan sulfate:TLR4
--
e26
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m26
0
infinite
0
--
heparan sulfate
--
e27
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m27
0
infinite
0
--
TLR4:CD14
--
e28
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m28
0
infinite
0
--
LPS:TLR4:MD2
--
e29
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m29
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
csml-variable:Double
m30
0
infinite
0
--
CpG DNA:TLR9
--
e31
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m31
0
infinite
0
--
ssRNA:TLR7
--
e32
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m32
0
infinite
0
--
type I interferons
--
e33
cso30:c:mRNA
cso30:i:CC_Cytosol
--
csml-variable:Double
m33
0
infinite
0
--
type I interferon
--
e34
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m34
0
infinite
0
--
--
e35
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
csml-variable:Double
m35
0
infinite
0
--
--
e36
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
csml-variable:Double
m36
0
infinite
0
--
--
e37
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m37
0
infinite
0
--
IRF-3{active}
--
e38
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m38
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007694 |
--
IRF-7{active}
--
e39
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m39
10
infinite
0
TRANSPATH | MO000007702 |
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
cytokine
--
e40
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m40
0
infinite
0
--
cytokine
--
e41
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m41
0
infinite
0
--
LPS:TLR4:MD2:MYD88
--
e42
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m42
0
infinite
0
--
diacylated lipopeptide:TLR2:TLR6:MYD88
--
e43
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m43
0
infinite
0
--
flagellin:TLR5:MYD88
--
e44
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m44
0
infinite
0
--
CpG DNA:TLR9:MYD88
--
e45
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m45
0
infinite
0
--
ssRNA:TLR8:MYD88
--
e46
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m46
0
infinite
0
--
ssRNA:TLR7:MYD88
--
e47
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m47
0
infinite
0
--
IRAK1
--
e48
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m48
0
infinite
0
--
LPS:TLR4:MD2:MYD88:IRAK4
--
e49
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m49
0
infinite
0
--
TLR1:TLR2
--
e5
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m5
0
infinite
0
--
--
e50
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelopeLumen
--
--
--
csml-variable:Double
m50
0
infinite
0
--
--
e51
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearPore
--
--
--
csml-variable:Double
m51
0
infinite
0
--
--
e52
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearInnerMembrane
--
--
--
csml-variable:Double
m52
0
infinite
0
--
--
e53
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearLumen
--
--
--
csml-variable:Double
m53
0
infinite
0
--
--
e54
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearOuterMembrane
--
--
--
csml-variable:Double
m54
0
infinite
0
--
--
e55
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleus
--
--
--
csml-variable:Double
m55
0
infinite
0
--
--
e56
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleoplasm
--
--
--
csml-variable:Double
m56
0
infinite
0
--
--
e57
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearBody
--
--
--
csml-variable:Double
m57
0
infinite
0
--
--
e58
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleolus
--
--
--
csml-variable:Double
m58
0
infinite
0
--
--
e59
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelope
--
--
--
csml-variable:Double
m59
0
infinite
0
--
TLR2:TLR6
--
e6
cso30:c:Complex
cso30:i:CC_Cytosol
--
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
--
diacylated lipopeptide:TLR2:TLR6:MYD88:IRAK1:TRAF6
--
e63
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m63
0
infinite
0
--
flagellin:TLR5:MYD88:IRAK1:TRAF6
--
e64
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m64
0
infinite
0
--
Ikappa-B alpha:NF-kappaB
--
e66
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m66
0
infinite
0
--
Ikappa-B alpha{p}:NF-kappaB
--
e67
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m67
0
infinite
0
--
protein remnants
--
e68
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m68
0
infinite
0
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
adhesion molecule
--
e70
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m71
0
infinite
0
--
LPS:TLR4:MD2:TRIF:PI3K
--
e71
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m72
0
infinite
0
--
diacylated lipopeptide:TLR2:TLR6:TRIF:PI3K
--
e72
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m74
0
infinite
0
--
dsRNA:TLR3:TRIF
--
e73
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m75
0
infinite
0
--
TBK1:IKK-epsilon
--
e74
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m76
0
infinite
0
--
TBK1:IKK-epsilon {active}
--
e75
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m77
0
infinite
0
--
IRF
--
e76
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m78
0
infinite
0
--
IRF{active}
--
e77
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m79
0
infinite
0
--
PI3K{active}
--
e78
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m80
10
infinite
0
TRANSPATH | MO000000030 |
--
IFN-alpha
--
e79
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m81
0
infinite
0
--
ssRNA
--
e8
cso30:c:Rna
cso30:i:CC_Cytosol
--
csml-variable:Double
m8
0
infinite
0
--
IFN-alpha
--
e80
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m82
0
infinite
0
--
IFN-beta
--
e81
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m83
0
infinite
0
--
TLR4:CD14:MD2
--
e82
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m84
0
infinite
0
--
sTLR4
--
e83
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m85
0
infinite
0
--
NF-kappaB{active}
--
e84
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m86
10
infinite
0
TRANSPATH | MO000000058 |
--
dsRNA:TLR3:PI3K
--
e86
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m88
0
infinite
0
--
LPS:TLR4:MD2:MYD88:IRAK4{p}:IRAK1
--
e88
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m91
0
infinite
0
--
LPS:TLR4:MD2:MYD88:IRAK4{p}:IRAK1{p}
--
e89
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m92
0
infinite
0
--
ssRNA:TLR8
--
e9
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m9
0
infinite
0
--
LPS:TLR4:MD2:MYD88:IRAK4:IRAK1{p}:TRAF6
--
e90
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m93
0
infinite
0
--
IRAK1{p}:TRAF6
--
e91
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m94
0
infinite
0
--
TAK1:TAB1:TAB2
--
e92
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m95
0
infinite
0
--
IRAK1{p}:TRAF6:TAK1:TAB1:TAB2
--
e93
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m96
0
infinite
0
--
IRAK1{p}:TRAF6:TAK1:TAB1{p}:TAB2{p}
--
e94
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m97
0
infinite
0
--
TRAF6:TAK1:TAB1{p}:TAB2{p}
--
e95
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m98
0
infinite
0
--
IRAK1{p}
--
e96
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m99
0
infinite
0
--
UevlA
--
e97
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m100
0
infinite
0
--
TRAF6:UVEIa:Ubc13:TAK1:TAB1{p}:TAB2{p}
--
e98
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m101
0
infinite
0
--
IKK{p}
--
e99
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m102
0
infinite
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m3963*m3964*0.1
nodelay
--
0
PMID: 18064347, 11431423, 12077222 the association between TLR1 and TLR6 which were demonstrated to form heterodimeric complexes with TLR2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c28 : 1
stoichiometry:c30 : 1
stoichiometry:c29 : 1
m24*m3961*0.1
nodelay
--
0
PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate.
p11
p11
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c32 : 1
stoichiometry:c33 : 1
stoichiometry:c31 : 1
m3961*m2254*0.1
nodelay
--
0
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c34 : 1
stoichiometry:c35 : 1
stoichiometry:c36 : 1
m3961*m27*0.1
nodelay
--
0
PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate.
p13
p13
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c37 : 1
stoichiometry:c38 : 1
stoichiometry:c39 : 1
m3985*m155666*0.1
nodelay
--
0
PMID: 18064347, 11274165 LPS is generally bound to LPS-binding protein (LBP) present in the serum, this complex is firstly recognized by CD14 receptor, strongly expressed in peripheral blood monocytes and macrophages.
p14
p14
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c40 : 1
stoichiometry:c41 : 1
stoichiometry:c42 : 1
m6254*m28*0.1
nodelay
--
0
PMID: 18064347, 11274165 LPS is generally bound to LPS-binding protein (LBP) present in the serum, this complex is firstly recognized by CD14 receptor, strongly expressed in peripheral blood monocytes and macrophages.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c44 : 1
stoichiometry:c43 : 1
stoichiometry:c176 : 1
stoichiometry:c45 : 1
m6438*m28*0.1
nodelay
--
0
PMID: 18064347, 11274165 Once bound to CD14, LPS comes in close proximity with TLR4; however the efficient triggering of an inflammatory response requires the expression of the secreted protein MD-2
p16
p16
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c47 : 1
stoichiometry:c46 : 1
stoichiometry:c48 : 1
stoichiometry:c49 : 1
stoichiometry:c50 : 1
m6255*m84*0.1
nodelay
--
0
PMID: 18064347, 11274165 Once bound to CD14, LPS comes in close proximity with TLR4; however the efficient triggering of an inflammatory response requires the expression of the secreted protein MD-2
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c51 : 1
stoichiometry:c52 : 1
stoichiometry:c53 : 1
m6485*m3966*0.1
nodelay
--
0
PMID: 18064347, 14625549 TLR5 recognizes a flagellin portion derived from Gram-positive and negative bacteria.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c54 : 1
stoichiometry:c55 : 1
stoichiometry:c56 : 1
m30*m19828*0.1
nodelay
--
0
PMID: 18064347, 15345224, 14993594, 12900525, 14563635 TLR9 senses DNA from Murine Cytomegalovirus (MCMV) and Herpes Simplex virus 1 and 2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c57 : 1
stoichiometry:c58 : 1
stoichiometry:c59 : 1
m19940*m8*0.1
nodelay
--
0
PMID: 18064347, 14976262, 15804288, 15661881 TLR7 responds to ssRNA producing interferon type I (IFN type I) and pro-inflammatory cytokines.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m3964*m3987*0.1
nodelay
--
0
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c61 : 1
stoichiometry:c62 : 1
stoichiometry:c60 : 1
m33*m32*0.1
nodelay
--
0
PMID: 18064347, 14976262, 15804288, 15661881 TLR7 responds to ssRNA producing interferon type I (IFN type I) and pro-inflammatory cytokines.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c63 : 1
stoichiometry:c64 : 1
stoichiometry:c65 : 1
m19823*m8*0.1
nodelay
--
0
PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7.
p22
p22
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c66 : 1
stoichiometry:c68 : 1
stoichiometry:c67 : 1
m977*m32*0.1
nodelay
--
0
PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7.
p23
p23
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c69 : 1
stoichiometry:c71 : 1
stoichiometry:c70 : 1
m977*m9*0.1
nodelay
--
0
PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7.
p24
p24
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c72 : 1
stoichiometry:c73 : 1
stoichiometry:c74 : 1
m32*m980*0.1
nodelay
--
0
PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7.
p25
p25
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c75 : 1
stoichiometry:c77 : 1
stoichiometry:c76 : 1
m980*m9*0.1
nodelay
--
0
PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c78 : 1
stoichiometry:c82 : 1
stoichiometry:c79 : 1
m40*m39*0.1
nodelay
--
0
PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c81 : 1
stoichiometry:c83 : 1
stoichiometry:c80 : 1
m40*m38*0.1
nodelay
--
0
PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7.
p28
p28
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c84 : 1
stoichiometry:c86 : 1
stoichiometry:c85 : 1
m3965*m119368*0.1
nodelay
--
0
PMID: 18064347, 16095970, 15829275, 15254159 Adequate host defense against viral infections involves rapid pathogen recognition by TLR3, TLR7, TLR8 and TLR9 among other PRRs. The viral PAMPs recognized by these receptors include: double-stranded RNA (dsRNA), single-stranded RNA (ssRNA) and double-stranded DNA (dsDNA)
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c87 : 1
stoichiometry:c88 : 1
stoichiometry:c89 : 1
m29*m1572*0.1
nodelay
--
0
PMID: 18064347 when TLR2,4 and 5 are activated MYD88 is recruited to TLR/TIR domain to induce pro inflammatory cytokine through a classical signal pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
stoichiometry:c9 : 1
m6*m11*0.1
nodelay
--
0
PMID: 18064347, 11431423, 12077222 TLR6 association with TLR2 induced recognition of diacylated lipopeptide but TLR1-TLR2 heterodimer binds preferentially triacylated lipopeptides.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c90 : 1
stoichiometry:c91 : 1
stoichiometry:c92 : 1
m12*m1572*0.1
nodelay
--
0
PMID: 18064347 When TLR2,4 and 5 are activated MYD88 is recruited to TLR/TIR domain to induce pro inflammatory cytokine through a classical signal pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c93 : 1
stoichiometry:c94 : 1
stoichiometry:c95 : 1
m22*m1572*0.1
nodelay
--
0
PMID: 18064347 When TLR2,4 and 5 are activated MYD88 is recruited to TLR/TIR domain to induce pro inflammatory cytokine through a classical signal pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c96 : 1
stoichiometry:c98 : 1
stoichiometry:c97 : 1
m31*m1572*0.1
nodelay
--
0
PMID: 18064347 During viral recognition in endosome TLR7, 8 and 9 use the cytoplasmic adaptor molecule MYD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c99 : 1
stoichiometry:c101 : 1
stoichiometry:c100 : 1
m9*m1572*0.1
nodelay
--
0
PMID: 18064347 During viral recognition in endosome TLR7, 8 and 9 use the cytoplasmic adaptor molecule MYD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c102 : 1
stoichiometry:c104 : 1
stoichiometry:c103 : 1
m32*m1572*0.1
nodelay
--
0
PMID: 18064347 During viral recognition in endosome TLR7, 8 and 9 use the cytoplasmic adaptor molecule MYD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c105 : 1
stoichiometry:c106 : 1
stoichiometry:c108 : 1
m42*m17258*0.1
nodelay
--
0
PMID: 18064347 A crucial event in pro-inflammatory signaling activation is the interaction of IRAK-4 with MyD88-ID domain that promotes, after recruitment to the receptor TIR domain, the phosphorylation of IRAK-1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c107 : 1
stoichiometry:c109 : 1
stoichiometry:c110 : 1
stoichiometry:c112 : 1
m43*m183*m48*0.1
nodelay
--
0
PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c113 : 1
stoichiometry:c114 : 1
stoichiometry:c115 : 1
stoichiometry:c116 : 1
m44*m48*m183*0.1
nodelay
--
0
PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6.
p38
p38
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c117 : 1
stoichiometry:c237 : 1
stoichiometry:c241 : 1
stoichiometry:c243 : 1
stoichiometry:c118 : 1
m48*m106*0.1
nodelay
--
0
PMID: 18064347 A crucial event in pro-inflammatory signaling activation is the interaction of IRAK-4 with MyD88-ID domain that promotes, after recruitment to the receptor TIR domain, the phosphorylation of IRAK-1. PMID: 18064347, 12150927 IRAK-M and IRAK-2 block pro-inflammatory cytokine expression by dissociating the complex formed by MyD88-IRAK-l/-4 and IRAK-TRAF6. IRAK-M -/- mice show an over-production of inflammatory cytokines in response to LPS and bacterial DNA-like CpG motifs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c120 : 1
stoichiometry:c122 : 1
stoichiometry:c121 : 1
m66*m65*0.1
nodelay
--
0
PMID: 18064347 The IKK complex catalyzes I¦ÊB¦Á phosphorylation and degradation by the proteasome, therefore allowing NF¦ÊB to translocate into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c10 : 1
stoichiometry:c11 : 1
stoichiometry:c12 : 1
m5*m13*0.1
nodelay
--
0
PMID: 18064347, 11431423, 12077222 TLR6 association with TLR2 induced recognition of diacylated lipopeptide but TLR1-TLR2 heterodimer binds preferentially triacylated lipopeptides.
p40
p40
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c123 : 1
stoichiometry:c125 : 1
stoichiometry:c124 : 1
m207*m63*0.1
nodelay
--
0
PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6.
p41
p41
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c126 : 1
stoichiometry:c128 : 1
stoichiometry:c127 : 1
m207*m64*0.1
nodelay
--
0
PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6.
p42
p42
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c129 : 1
stoichiometry:c130 : 1
stoichiometry:c131 : 1
m67*0.1
nodelay
--
0
PMID: 18064347 The IKK complex catalyzes I¦ÊB¦Á phosphorylation and degradation by the proteasome, therefore allowing NF¦ÊB to translocate into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c178 : 1
stoichiometry:c133 : 1
m86*0.1
nodelay
--
0
PMID: 18064347 The IKK complex catalyzes I¦ÊB¦Á phosphorylation and degradation by the proteasome, therefore allowing NF¦ÊB to translocate into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c135 : 1
stoichiometry:c134 : 1
m70*0.1
nodelay
--
0
PMID: 18064347 Once in the nucleus, NF¦ÊB regulates the expression of pro-inflammatory cytokines and adhesion molecules.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c136 : 1
m70*0.1
nodelay
--
0
PMID: 18064347 Once in the nucleus, NF¦ÊB regulates the expression of pro-inflammatory cytokines and adhesion molecules.
p46
p46
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c138 : 1
stoichiometry:c140 : 1
stoichiometry:c139 : 1
stoichiometry:c141 : 1
m18998*m73*m105*0.1
nodelay
--
0
PMID: 18064347 In addition, TLR2 and 4 uses a MyD88-independent pathway that involves PI3K and TRIF recruitment to the TLR/TIR domain.
p47
p47
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c142 : 1
stoichiometry:c143 : 1
stoichiometry:c144 : 1
stoichiometry:c145 : 1
m12*m18998*m73*0.1
nodelay
--
0
PMID: 18064347 In addition, TLR2 and 4 uses a MyD88-independent pathway that involves PI3K and TRIF recruitment to the TLR/TIR domain.
p48
p48
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c146 : 1
stoichiometry:c148 : 1
stoichiometry:c147 : 1
m977*m72*0.1
nodelay
--
0
PMID: 18064347 TLR4 activates a TRIF-dependent pathway that induces the activation of IRF-3 and subsequently the production of type I IFN in response to LPS. PMID: 18064347, 12368275, 14519765 TLR4 utilizes the adaptors TRIF and TRAM independently of Mai and MyD88 to initiate the late phase of NF¦ÊB activation and also to induce the expression of IFN-? and other IFN-inducible genes via the transcription factor IRF-3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c150 : 1
stoichiometry:c151 : 1
stoichiometry:c149 : 1
m33*m38*0.1
nodelay
--
0
PMID: 18064347 TLR4 activates a TRIF-dependent pathway that induces the activation of IRF-3 and subsequently the production of type I IFN in response to LPS.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c14 : 1
stoichiometry:c15 : 1
m3961*m15*0.1
nodelay
--
0
PMID: 18064347, 10644670, 11274165 TLR4 can also recognize taxol (a strong antitumor agent in humans) derived from Taxus brevifolia, and a respiratory syncytial virus fusion protein.
p50
p50
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c152 : 1
stoichiometry:c153 : 1
stoichiometry:c154 : 1
m19314*m18998*0.1
nodelay
--
0
PMID: 18064347 TLR3 triggers a TIR domain-containing adaptor inducing IFN-¦Â (TRIF) signaling pathway independent of MyD88 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c155 : 1
stoichiometry:c157 : 1
stoichiometry:c156 : 1
m76*m75*0.1
nodelay
--
0
PMID: 18064347 TLR3 can also regulate IFN¦Á/¦Â production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c158 : 1
stoichiometry:c160 : 1
stoichiometry:c159 : 1
m78*m77*0.1
nodelay
--
0
PMID: 18064347 TLR3 can also regulate IFN¦Á/¦Â production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation.
p53
p53
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c161 : 1
stoichiometry:c184 : 1
stoichiometry:c162 : 1
m73*m19314*0.1
nodelay
--
0
PMID: 18064347 TLR3 can also regulate IFN¦Á/¦Â production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c164 : 1
stoichiometry:c166 : 1
stoichiometry:c165 : 1
m78*m80*0.1
nodelay
--
0
PMID: 18064347 TLR3 can also regulate IFN¦Á/¦Â production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c168 : 1
stoichiometry:c169 : 1
stoichiometry:c167 : 1
m81*m79*0.1
nodelay
--
0
PMID: 18064347 TLR3 can also regulate IFN¦Á/¦Â production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c171 : 1
stoichiometry:c172 : 1
stoichiometry:c170 : 1
m93217*m79*0.1
nodelay
--
0
PMID: 18064347 TLR3 can also regulate IFN¦Á/¦Â production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation.
p57
p57
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c173 : 1
stoichiometry:c174 : 1
stoichiometry:c175 : 1
m2828*m3961*0.1
nodelay
--
0
PMID: 18064347 The soluble product sTLR4 is an alternative splice variant of TLR4 that was shown to be expressed as a mechanism to inhibit LPS -mediated TNF¦Á production and NF¦ÊB activation, blocking MD-2 recruitment to the TLR4-CD14 complex.
p58
p58
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c179 : 1
stoichiometry:c240 : 1
stoichiometry:c249 : 1
stoichiometry:c268 : 1
stoichiometry:c284 : 1
stoichiometry:c177 : 1
m69*m29*0.1
nodelay
--
0
PMID: 18064347 The soluble product sTLR4 is an alternative splice variant of TLR4 that was shown to be expressed as a mechanism to inhibit LPS -mediated TNF¦Á production and NF¦ÊB activation, blocking MD-2 recruitment to the TLR4-CD14 complex. PMID: 18064347, 12538665 The mechanism by which MyD88s reverts inflammation involves IRAK-4 sequestration by MyD88s that prevents further phosphorylation of IRAK-4 and IRAK-1 and activation of NF¦ÊB. PMID: 18064347, 12154357, 12052830 PI3K has been also implicated in TLRs signaling, suppressing both MAPKs and NF¦ÊB in response to LPS, thereby decreasing TNF¦Á production. PMID: 18064347, 15004556 A possible mechanism for ST2L immune modulation involves its interaction with molecular adaptors of TLR/IL-1 inflammatory pathways. ST2L can sequestrate MyD88 and Mai through their TIR domains, and therefore can block the effect of TLR4-mediated NF¦ÊB activation
p59
p59
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c180 : 1
stoichiometry:c182 : 1
stoichiometry:c230 : 1
stoichiometry:c181 : 1
m93309*m29*0.1
nodelay
--
0
PMID: 18064347 The soluble product sTLR4 is an alternative splice variant of TLR4 that was shown to be expressed as a mechanism to inhibit LPS -mediated TNF¦Á production and NF¦ÊB activation, blocking MD-2 recruitment to the TLR4-CD14 complex. PMID: 18064347, 12154357, 12052830 PI3K has been also implicated in TLRs signaling, suppressing both MAPKs and NF¦ÊB in response to LPS, thereby decreasing TNF¦Á production.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c17 : 1
stoichiometry:c18 : 1
m3961*m17*0.1
nodelay
--
0
PMID: 18064347, 10644670, 11274165 TLR4 can also recognize taxol (a strong antitumor agent in humans) derived from Taxus brevifolia, and a respiratory syncytial virus fusion protein.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c163 : 1
stoichiometry:c183 : 1
m19314*0.1
nodelay
--
0
PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c185 : 1
stoichiometry:c186 : 1
stoichiometry:c187 : 1
m87*m80*0.1
nodelay
--
0
PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation.
p62
p62
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c188 : 1
stoichiometry:c190 : 1
stoichiometry:c189 : 1
m89*m88*0.1
nodelay
--
0
PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation.
p63
p63
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c191 : 1
stoichiometry:c193 : 1
stoichiometry:c192 : 1
m977*m90*0.1
nodelay
--
0
PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation.
p64
p64
cso30:i:ME_Phosphorylation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c119 : 1
stoichiometry:c239 : 1
stoichiometry:c257 : 1
stoichiometry:c194 : 1
m91*0.1
nodelay
--
0
PMID: 18064347 A crucial event in pro-inflammatory signaling activation is the interaction of IRAK-4 with MyD88-ID domain that promotes, after recruitment to the receptor TIR domain, the phosphorylation of IRAK-1. PMID: 18064347, 12538665 The mechanism by which MyD88s reverts inflammation involves IRAK-4 sequestration by MyD88s that prevents further phosphorylation of IRAK-4 and IRAK-1 and activation of NF¦ÊB. PMID: 18064347, 10854325 Tollip is recruited to the TIR domain and decreases IRAK-1 phosphorylation upon LPS activation. IRAK-1 activation by MyD88 promotes Tollip dissociation from the TIR domain.
p65
p65
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c195 : 1
stoichiometry:c196 : 1
stoichiometry:c242 : 1
stoichiometry:c244 : 1
stoichiometry:c197 : 1
m92*m183*0.1
nodelay
--
0
PMID: 18064347 Once IRAK-1 is phosphorylated TRAF6 is recruited to the TLR complex. PMID: 18064347, 12150927 IRAK-M and IRAK-2 block pro-inflammatory cytokine expression by dissociating the complex formed by MyD88-IRAK-l/-4 and IRAK-TRAF6. IRAK-M -/- mice show an over-production of inflammatory cytokines in response to LPS and bacterial DNA-like CpG motifs .
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c198 : 1
stoichiometry:c199 : 1
stoichiometry:c200 : 1
m93*0.1
nodelay
--
0
PMID: 18064347, 11259596 IRAK-1 and TRAF6 dissociate from the TIR/MyD88/IRAK-4 complex and interact with membrane-associated proteins, such as TAK1 (transforming growth factor-(?-activated kinase 1), TAB1 (transforming growth factor-(?-activated protein kinase 1-binding protein 1) and TAB2 that are part of the multicomplex IRAK-1-TRAF6-TAK1-TAB1-TAB2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c201 : 1
stoichiometry:c202 : 1
stoichiometry:c203 : 1
m94*m95*0.1
nodelay
--
0
PMID: 18064347, 11259596 IRAK-1 and TRAF6 dissociate from the TIR/MyD88/IRAK-4 complex and interact with membrane-associated proteins, such as TAK1 (transforming growth factor-(?-activated kinase 1), TAB1 (transforming growth factor-(?-activated protein kinase 1-binding protein 1) and TAB2 that are part of the multicomplex IRAK-1-TRAF6-TAK1-TAB1-TAB2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c204 : 1
stoichiometry:c205 : 1
m96*0.1
nodelay
--
0
PMID: 18064347, 12242293 When TAK1 and TAB2 become phosphorylated they induce IRAK-1 dissociation from the complex and further IKKs and MAPKs activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c206 : 1
stoichiometry:c207 : 1
stoichiometry:c208 : 1
m97*0.1
nodelay
--
0
PMID: 18064347, 12242293 When TAK1 and TAB2 become phosphorylated they induce IRAK-1 dissociation from the complex and further IKKs and MAPKs activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c20 : 1
stoichiometry:c21 : 1
m3961*m4645*0.1
nodelay
--
0
PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate.
p70
p70
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c209 : 1
stoichiometry:c211 : 1
stoichiometry:c210 : 1
m207*m101*0.1
nodelay
--
0
PMID: 18064347, 15147900, 11460167 Recent studies showed that TRAF6 can bind ubiquitin-conjugating enzymes Ubcl3 and UevlA, that are critical in the activation of TAK1 -mediated phosphorylation of IKK and MKK (MAPK Kinases)
p71
p71
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c212 : 1
stoichiometry:c213 : 1
stoichiometry:c214 : 1
stoichiometry:c215 : 1
m98*m6443*m100*0.1
nodelay
--
0
PMID: 18064347, 15147900, 11460167 Recent studies showed that TRAF6 can bind ubiquitin-conjugating enzymes Ubcl3 and UevlA, that are critical in the activation of TAK1 -mediated phosphorylation of IKK and MKK (MAPK Kinases)
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c216 : 1
stoichiometry:c218 : 1
stoichiometry:c248 : 1
stoichiometry:c217 : 1
m103*m101*0.1
nodelay
--
0
PMID: 18064347, 15147900, 11460167 Recent studies showed that TRAF6 can bind ubiquitin-conjugating enzymes Ubcl3 and UevlA, that are critical in the activation of TAK1 -mediated phosphorylation of IKK and MKK (MAPK Kinases). PMID: 18064347, 12154357, 12052830 PI3K has been also implicated in TLRs signaling, suppressing both MAPKs and NF¦ÊB in response to LPS, thereby decreasing TNF¦Á production.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c219 : 1
stoichiometry:c221 : 1
stoichiometry:c220 : 1
m66*m102*0.1
nodelay
--
0
PMID: 18064347 The IKK complex catalyzes I¦ÊB¦Á phosphorylation and degradation by the proteasome, therefore allowing NF¦ÊB to translocate into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c222 : 1
stoichiometry:c223 : 1
stoichiometry:c224 : 1
m29*m19005*0.1
nodelay
--
0
PMID: 18064347 TRAM, like Mai, acts as a bridge to couple TRIF to TLR4 and is absolutely required for TLR4 mediated responses.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c226 : 1
stoichiometry:c225 : 1
m29*0.1
nodelay
--
0
PMID: 18064347 TLR4 activation by LPS may induce the expression of the TRIF-related adaptor molecule (TRAM/TICAM-2) that binds to TLR4 and to TRIF.
p76
p76
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c228 : 1
stoichiometry:c229 : 1
stoichiometry:c227 : 1
m96947*m29*0.1
nodelay
--
0
PMID: 18064347 TLR4 activation by LPS may induce the expression of the TRIF-related adaptor molecule (TRAM/TICAM-2) that binds to TLR4 and to TRIF.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c231 : 1
stoichiometry:c232 : 1
stoichiometry:c250 : 1
m12*m80*0.1
nodelay
--
0
PMID: 18064347, 11101877 Stimulation of TLR2 expressing cells with Staphylococcus aureus promotes PI3K recruitment to the TIR domain and induces transactivation of the NF¦ÊB subunit p65 by a mechanism that seems to be independent of I¦ÊB¦Á proteasomic degradation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c234 : 1
stoichiometry:c235 : 1
stoichiometry:c233 : 1
m93217*m38*0.1
nodelay
--
0
PMID: 18064347, 12368275, 14519765 TLR4 utilizes the adaptors TRIF and TRAM independently of Mai and MyD88 to initiate the late phase of NF¦ÊB activation and also to induce the expression of IFN-? and other IFN-inducible genes via the transcription factor IRF-3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c111 : 1
stoichiometry:c238 : 1
stoichiometry:c236 : 1
m49*0.1
nodelay
--
0
PMID: 18064347, 12538665 The mechanism by which MyD88s reverts inflammation involves IRAK-4 sequestration by MyD88s that prevents further phosphorylation of IRAK-4 and IRAK-1 and activation of NF¦ÊB.
p8
p8
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c22 : 1
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m3961*m5956*0.1
nodelay
--
0
PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate.
p80
p80
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c246 : 1
stoichiometry:c247 : 1
stoichiometry:c245 : 1
m290229*m80*0.1
nodelay
--
0
PMID: 18064347 PI3K is an enzyme that catalyzes the phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2) to phosphatidylinositol 3,4,5-trisphosphate (PIP3).
p81
p81
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c251 : 1
stoichiometry:c253 : 1
stoichiometry:c252 : 1
m69*m108*0.1
nodelay
--
0
PMID: 18064347, 11101877 Stimulation of TLR2 expressing cells with Staphylococcus aureus promotes PI3K recruitment to the TIR domain and induces transactivation of the NF¦ÊB subunit p65 by a mechanism that seems to be independent of I¦ÊB¦Á proteasomic degradation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c254 : 1
stoichiometry:c255 : 1
stoichiometry:c256 : 1
m3973*m29*0.1
nodelay
--
0
PMID: 18064347, 10854325 Tollip is recruited to the TIR domain and decreases IRAK-1 phosphorylation upon LPS activation. IRAK-1 activation by MyD88 promotes Tollip dissociation from the TIR domain.
p83
p83
cso30:i:ME_Dissociation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c258 : 1
stoichiometry:c261 : 1
stoichiometry:c259 : 1
stoichiometry:c260 : 1
m109*m92*0.1
nodelay
--
0
PMID: 18064347, 10854325 Tollip is recruited to the TIR domain and decreases IRAK-1 phosphorylation upon LPS activation. IRAK-1 activation by MyD88 promotes Tollip dissociation from the TIR domain.
p84
p84
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c262 : 1
stoichiometry:c263 : 1
stoichiometry:c264 : 1
m110*m4947*0.1
nodelay
--
0
PMID: 18064347, 12514169, 12527755 NOD2 protein is constituted by two caspase recruitment domains (CARD), a NOD region and a tripartite domain, consisting of a C-terminal LRR. This last domain recognizes and reacts to the bacterial component muramyl dipeptide (MDP), and is the site with major genetic variability.
p85
p85
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c265 : 1
stoichiometry:c266 : 1
stoichiometry:c267 : 1
m22464*m1572*0.1
nodelay
--
0
PMID: 18064347, 15004556 A possible mechanism for ST2L immune modulation involves its interaction with molecular adaptors of TLR/IL-1 inflammatory pathways. ST2L can sequestrate MyD88 and Mai through their TIR domains, and therefore can block the effect of TLR4-mediated NF¦ÊB activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c275 : 1
stoichiometry:c277 : 1
stoichiometry:c276 : 1
m115*m117*0.1
nodelay
--
0
PMID: 18064347, 12925853, 15866876 SIGIRR interacts with IL-1R and TLR4 in a ligand-dependent manner and inhibits their signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c272 : 1
stoichiometry:c273 : 1
stoichiometry:c274 : 1
m41575*m29*0.1
nodelay
--
0
PMID: 18064347, 12925853, 15866876 SIGIRR interacts with IL-1R and TLR4 in a ligand-dependent manner and inhibits their signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c269 : 1
stoichiometry:c271 : 1
stoichiometry:c270 : 1
m29*0.1
nodelay
--
0
PMID: 18064347, 11359817 In LPS-activated macrophages, ST2s downregulates TLR4 mRNA expression.
p89
p89
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c278 : 1
stoichiometry:c280 : 1
stoichiometry:c279 : 1
m116*m41575*0.1
nodelay
--
0
PMID: 18064347, 12925853, 15866876 SIGIRR interacts with IL-1R and TLR4 in a ligand-dependent manner and inhibits their signaling.
p9
p9
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
stoichiometry:c27 : 1
m3961*m2341*0.1
nodelay
--
0
PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate.
p90
p90
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c281 : 1
stoichiometry:c282 : 1
stoichiometry:c283 : 1
m22464*m119*0.1
nodelay
--
0
PMID: 18064347, 15004556 A possible mechanism for ST2L immune modulation involves its interaction with molecular adaptors of TLR/IL-1 inflammatory pathways. ST2L can sequestrate MyD88 and Mai through their TIR domains, and therefore can block the effect of TLR4-mediated NF¦ÊB activation
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: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:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
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: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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c: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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
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1,
--
cso30:c:OutputProcess
threshold
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0
1,
--
cso30:c:InputInhibitor
threshold
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1,
--
cso30:c:OutputProcess
threshold
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cso30:c:InputProcess
threshold
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cso30:c:InputAssociation
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:InputAssociation
threshold
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cso30:c:OutputProcess
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cso30:c:InputAssociation
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cso30:c:OutputProcess
threshold
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cso30:c:InputAssociation
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cso30:c:InputProcess
threshold
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cso30:c:OutputProcess
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cso30:c:InputAssociation
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cso30:c:OutputProcess
threshold
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cso30:c:InputAssociation
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cso30:c:OutputProcess
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:OutputProcess
threshold
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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
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:InputAssociation
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cso30:c:OutputProcess
threshold
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cso30:c:InputAssociation
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cso30:c:OutputProcess
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cso30:c:InputAssociation
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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:InputAssociation
threshold
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cso30:c:OutputProcess
threshold
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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:InputInhibitor
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:InputAssociation
threshold
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cso30:c:InputAssociation
threshold
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cso30:c:InputInhibitor
threshold
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cso30:c:InputInhibitor
threshold
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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:InputInhibitor
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cso30:c:InputInhibitor
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cso30:c:InputInhibitor
threshold
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cso30:c:OutputProcess
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cso30:c:InputAssociation
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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:OutputProcess
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cso30:c:InputAssociation
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cso30:c:InputProcess
threshold
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cso30:c:InputProcess
threshold
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cso30:c:OutputProcess
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cso30:c:InputInhibitor
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cso30:c:InputProcess
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cso30:c:OutputProcess
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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: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:OutputProcess
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cso30:c:OutputProcess
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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:OutputProcess
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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:InputProcess
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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:OutputProcess
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cso30:c:OutputProcess
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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: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:InputProcess
threshold
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cso30:c:InputProcess
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cso30:c:OutputProcess
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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: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:InputAssociation
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cso30:c:InputProcess
threshold
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cso30:c:OutputProcess
threshold
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cso30:c:InputAssociation
threshold
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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
threshold
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cso30:c:OutputProcess
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:InputProcess
threshold
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cso30:c:InputProcess
threshold
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cso30:c:OutputProcess
threshold
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--
cso30:c:InputProcess
threshold
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1,
--
cso30:c:OutputProcess
threshold
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0
1,
--
cso30:c:InputProcess
threshold
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0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--