Original Literature | Model OverView |
---|---|
Publication
Title
Intracellular NOD-like receptors in host defense and disease.
Affiliation
Department of Pathology and Comprehensive Cancer Center, University of MichiganMedical School, Ann Arbor, MI 48109, USA.
Abstract
The innate immune system comprises several classes of pattern recognitionreceptors, including Toll-like receptors (TLRs), NOD-like receptors (NLRs), andRIG-1-like receptors (RLRs). TLRs recognize microbes on the cell surface and inendosomes, whereas NLRs and RLRs detect microbial components in the cytosol.Here we discuss the recent understanding in NLRs. Two NLRs, NOD1 and NOD2, sensethe cytosolic presence of the peptidoglycan fragments meso-DAP and muramyldipeptide, respectively, and drive the activation of mitogen-activated proteinkinase (MAPK) and the transcription factor NF-kappaB. A different set of NLRsinduces caspase-1 activation through the assembly of large protein complexesnamed inflammasomes. Genetic variations in several NLR members are associatedwith the development of inflammatory disorders. Further understanding of NLRsshould provide new insights into the mechanisms of host defense and thepathogenesis of inflammatory diseases.
PMID
17967410
|
Entity
TAK1
--
MO000016574
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1573
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016574 |
--
IKK-gamma
--
MO000016599
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1593
10
infinite
0
InterPro | IPR007087 |
TRANSPATH | MO000016599 |
--
p50:RelA-p65
--
MO000016632
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1617
10
infinite
0
TRANSPATH | MO000016632 |
--
Caspase-1{activated}
--
MO000016828
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1765
10
infinite
0
TRANSPATH | MO000016828 |
--
proIL-1beta
--
MO000019449
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m4012
10
infinite
0
InterPro | IPR003297 |
TRANSPATH | MO000019449 |
--
protein remnants
--
MO000019479
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m360980
10
infinite
0
TRANSPATH | MO000019479 |
--
p50:RelA-p65:IkappaB-alpha
--
MO000038724
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m16910
10
infinite
0
TRANSPATH | MO000038724 |
--
ASC
--
MO000044014
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m21736
10
infinite
0
InterPro | IPR004020 |
TRANSPATH | MO000044014 |
--
PANX1{activated}
--
MO000064988
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m39857
10
infinite
0
TRANSPATH | MO000064988 |
--
--
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
--
MDP: Nod2
--
e11
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m11
0
infinite
0
--
MDP
--
e12
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
csml-variable:Double
m12
0
infinite
0
--
iE-DAP: Nod1{oligomer}
--
e13
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m13
0
infinite
0
--
MDP: Nod2{oligomer}
--
e14
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m14
0
infinite
0
--
iE-DAP: Nod1{oligomer}: RICK
--
e15
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m15
0
infinite
0
--
MDP: Nod2{oligomer}: RICK
--
e16
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m16
0
infinite
0
--
iE-DAP: Nod1{oligomer}: RICK: IKK-gamma
--
e17
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m17
0
infinite
0
--
MDP: Nod2{oligomer}: RICK: IKK-gamma
--
e18
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m18
0
infinite
0
--
iE-DAP: Nod1{oligomer}: RICK: IKK-gamma{ubK63}
--
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
--
MDP: Nod2{oligomer}: RICK: IKK-gamma{ubK63}
--
e20
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m20
0
infinite
0
--
MDP: Nod2{oligomer}: RICK: CARD9
--
e22
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m22
0
infinite
0
--
TAK1 {activated}
--
e23
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m23
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016574 |
--
proinflammatory genes
--
e28
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m32
0
infinite
0
--
TLR ligand
--
e29
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m33
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
TLR ligand: TLR
--
e30
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m34
0
infinite
0
--
IRAK-1{activated}
--
e32
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m36
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000213 |
--
TRAF6{activated}
--
e33
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m37
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000000212 |
--
flagellin: TLR5
--
e34
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m38
0
infinite
0
--
flagellin: IPAF
--
e35
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m39
0
infinite
0
--
Caspase-1
--
e36
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m40
10
infinite
0
TRANSPATH | MO000016828 |
--
flagellin: IPAF: ASC
--
e37
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m41
0
infinite
0
--
flagellin{cytosolic}
--
e38
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m42
10
infinite
0
TRANSPATH | MO000022185 |
--
NALP1b
--
e39
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m43
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
NALP1
--
e40
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m44
0
infinite
0
--
MDP: NALP1
--
e41
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m45
0
infinite
0
--
csml-variable:Double
m46
0
infinite
0
--
MDP: NALP1: ASC: CARDINAL
--
e43
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m47
0
infinite
0
--
Caspase-5{activated}
--
e44
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m48
10
infinite
0
TRANSPATH | MO000017601 |
--
Bcl-2: NALP1
--
e45
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m63
0
infinite
0
--
Bcl-xL: NALP1
--
e46
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m64
0
infinite
0
--
Anthrax LT
--
e47
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m65
0
infinite
0
--
Anthrax LT: NALP1b
--
e48
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m66
0
infinite
0
--
flagellin: IPAF: ASC: Caspase-1
--
e49
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m67
0
infinite
0
--
iE-DAP
--
e5
cso30:c:SmallMolecule
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
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
--
iE-DAP: Nod1
--
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
--
MDP: NALP1: ASC: CARDINAL: Caspase-5
--
e63
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m68
0
infinite
0
--
MDP: NALP1: ASC: CARDINAL: Caspase-1
--
e64
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m69
0
infinite
0
--
NALP3
--
e65
cso30:c:Protein
cso30:i:CC_Cell
--
csml-variable:Double
m70
0
infinite
0
--
LPS: NALP3
--
e66
cso30:c:Complex
cso30:i:CC_Cell_WithoutCellWall_
--
csml-variable:Double
m71
0
infinite
0
--
csml-variable:Double
m72
0
infinite
0
--
peptidoglycan: NALP3
--
e68
cso30:c:Complex
cso30:i:CC_Cell_WithoutCellWall_
--
--
csml-variable:Double
m73
0
infinite
0
--
lipoteic acid: ATP
--
e69
cso30:c:SmallMolecule
cso30:i:CC_Cytoplasm
--
--
csml-variable:Double
m74
0
infinite
0
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
lipoteic acid: ATP: NALP3
--
e70
cso30:c:Complex
cso30:i:CC_Cell_WithoutCellWall_
--
--
csml-variable:Double
m75
0
infinite
0
--
LPS{extracellular}
--
e71
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m76
10
infinite
0
TRANSPATH | MO000016882 |
--
LPS: NALP3: ASC
--
e72
cso30:c:Complex
cso30:i:CC_Cell
--
csml-variable:Double
m77
0
infinite
0
--
LPS: NALP3: ASC: Caspase-1
--
e73
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m78
0
infinite
0
--
ATP
--
e74
cso30:c:SmallMolecule
cso30:i:CC_Cell
--
csml-variable:Double
m79
0
infinite
0
--
Pore Formng Toxins
--
e76
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m81
0
infinite
0
--
bacterial ligand
--
e77
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m82
0
infinite
0
--
bacterial ligand {extracellular}
--
e78
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m83
0
infinite
0
--
csml-variable:Double
m84
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
Francisella: unknown NLR: ASC
--
e80
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m85
0
infinite
0
--
csml-variable:Double
m86
0
infinite
0
--
potasium
--
e82
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m87
0
infinite
0
--
P2RX7{openned}
--
e83
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m88
10
infinite
0
TRANSPATH | MO000063086 |
--
potasium{extracellular}
--
e84
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m89
0
infinite
0
--
CPPD
--
e85
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m90
0
infinite
0
--
csml-variable:Double
m91
0
infinite
0
--
p50:RelA-p65{nucleus}
--
e87
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m30
10
infinite
0
TRANSPATH | MO000016632 |
--
--
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
m5*m4923*0.1
nodelay
--
0
PMID: 17967410, 12796777, 1279199716870615 NOD1 recognizes the dipeptide gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), which is produced by most Gram-negative and specific Gram-positive bacteria.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
m18*0.1
nodelay
--
0
PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c27 : 1
stoichiometry:c28 : 1
stoichiometry:c29 : 1
m21914*m16*0.1
nodelay
--
0
PMID: 17967410 The NLR proteins NOD1 and NOD2 sense intracellular iE-DAP and MDP, respectively, leading to recruitment of the adaptor proteins RICK and CARD9. PMID: 17967410, 17187069 The CARD-containing adaptor protein CARD9 was found to be important for the activation of p38 and JNK downstream of NOD2, although it was dispensable for NF-kappaB activation
p12
p12
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c32 : 1
stoichiometry:c34 : 1
stoichiometry:c33 : 1
m1573*m15*0.1
nodelay
--
0
PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.
p13
p13
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c30 : 1
stoichiometry:c35 : 1
stoichiometry:c31 : 1
m1573*m22*0.1
nodelay
--
0
PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex. PMID: 17967410, 17187069 The CARD-containing adaptor protein CARD9 was found to be important for the activation of p38 and JNK downstream of NOD2, although it was dispensable for NF-kappaB activation
p14
p14
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c36 : 1
stoichiometry:c38 : 1
stoichiometry:c37 : 1
m24*m23*0.1
nodelay
--
0
PMID: 17967410, 11463746, 15692051, 14560001 In addition to the NF-kappaB pathway, NOD1 or NOD2 stimulation results in the activation of the MAP kinases p38, ERK, and JNK. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
p15
p15
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c39 : 1
stoichiometry:c41 : 1
stoichiometry:c40 : 1
m26*m23*0.1
nodelay
--
0
PMID: 17967410, 11463746, 15692051, 14560001 In addition to the NF-kappaB pathway, NOD1 or NOD2 stimulation results in the activation of the MAP kinases p38, ERK, and JNK. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
p16
p16
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c42 : 1
stoichiometry:c44 : 1
stoichiometry:c43 : 1
m28*m23*0.1
nodelay
--
0
PMID: 17967410, 11463746, 15692051, 14560001 In addition to the NF-kappaB pathway, NOD1 or NOD2 stimulation results in the activation of the MAP kinases p38, ERK, and JNK. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
p17
p17
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c48 : 1
stoichiometry:c202 : 1
stoichiometry:c47 : 1
stoichiometry:c205 : 1
m19*m16910*0.1
nodelay
--
0
PMID: 17967410 These events result in the degradation of the NF-kappaB inhibitor IkappaB-alpha and the subsequent translocation of NF-kappaB to the nucleus, where transcription of NF-¦ÊB-dependent target genes occurs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c45 : 1
stoichiometry:c46 : 1
m1617*0.1
nodelay
--
0
PMID: 17967410 These events result in the degradation of the NF-kappaB inhibitor IkappaB-alpha and the subsequent translocation of NF-kappaB to the nucleus, where transcription of NF-¦ÊB-dependent target genes occurs. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c65 : 1
stoichiometry:c52 : 1
m30*0.1
nodelay
--
0
PMID: 17967410 These events result in the degradation of the NF-kappaB inhibitor IkappaB-alpha and the subsequent translocation of NF-kappaB to the nucleus, where transcription of NF-¦ÊB-dependent target genes occurs. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
p2
p2
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m12*m4947*0.1
nodelay
--
0
PMID: 17967410, 12527755, 12514169 In contrast, NOD2 is activated by muramyl dipeptide (MDP), a component of virtually all types of PGN.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c53 : 1
stoichiometry:c55 : 1
stoichiometry:c54 : 1
m33*m3962*0.1
nodelay
--
0
PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
p21
p21
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c58 : 1
stoichiometry:c57 : 1
m1572*m34*0.1
nodelay
--
0
PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
p22
p22
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c59 : 1
stoichiometry:c61 : 1
stoichiometry:c60 : 1
m184*m35*0.1
nodelay
--
0
PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
p23
p23
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c62 : 1
stoichiometry:c64 : 1
stoichiometry:c63 : 1
m183*m36*0.1
nodelay
--
0
PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
p24
p24
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c203 : 1
stoichiometry:c66 : 1
stoichiometry:c206 : 1
m37*m16910*0.1
nodelay
--
0
PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
p25
p25
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
m21914*m37*0.1
nodelay
--
0
PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
p26
p26
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c72 : 1
stoichiometry:c74 : 1
stoichiometry:c73 : 1
m1573*m21*0.1
nodelay
--
0
PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
p27
p27
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c76 : 1
stoichiometry:c77 : 1
stoichiometry:c75 : 1
m101900*m13*0.1
nodelay
--
0
PMID: 17967410, 16513653 Moreover, H. pylori-induced production of beta-defensins was abolished in Nod1¡Ý/¡Ý mice.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c49 : 1
stoichiometry:c78 : 1
m30*0.1
nodelay
--
0
PMID: 17967410 Recognition of PAMPs by TLRs induces synthesis of the IL-1beta precursor through activation of NF-kappaB.
p29
p29
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c80 : 1
stoichiometry:c81 : 1
stoichiometry:c82 : 1
m3966*m6485*0.1
nodelay
--
0
PMID: 17967410 These results demonstrate that TLR5 and Ipaf represent two flagellin receptors that have evolved to control distinct signaling pathways (NF-kappaB activation and caspase-1 activation, respectively) when the host is infected with Salmonella or Legionella.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c9 : 1
stoichiometry:c10 : 1
m11*0.1
nodelay
--
0
PMID: 17967410 The current model proposes that when PAMPs are sensed by the C-terminal LRRs, the molecule undergoes conformational rearrangements triggering oligomerization via the NOD domain.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c83 : 1
stoichiometry:c104 : 1
stoichiometry:c85 : 1
m21777*m42*0.1
nodelay
--
0
PMID: 17967410, 16984919, 16648852, 16648853 Flagellin was identified as the bacterial molecule that is sensed by Ipaf, and flagellin-deficient bacteria are compromised in their capability to induce caspase-1 activation and secretion of IL-1beta. PMID: 17967410, 16984919, 16648852, 16648853 The finding that recombinant purified flagellin induces Ipaf-dependent caspase-1 activation when delivered directly into the cytosol indicates that the cytosolic presence of flagellin is essential and sufficient for Ipaf activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c86 : 1
stoichiometry:c89 : 1
m25*0.1
nodelay
--
0
PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c87 : 1
stoichiometry:c90 : 1
m27*0.1
nodelay
--
0
PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c88 : 1
stoichiometry:c91 : 1
m29*0.1
nodelay
--
0
PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c92 : 1
stoichiometry:c93 : 1
stoichiometry:c94 : 1
m39*m21736*0.1
nodelay
--
0
PMID: 17967410 The inflammasome adaptor ASC is required for recruitment of caspase-1, although its role in the Nalp1b inflammasome needs to be confirmed.
p35
p35
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c96 : 1
stoichiometry:c97 : 1
m67*0.1
nodelay
--
0
PMID: 17967410 Ipaf rapidly activates caspase-1 when it senses the intracellular pathogens Salmonella typhimurium or Legionella pneumophila. PMID: 17967410, 16984919, 16648852, 16648853 Flagellin was identified as the bacterial molecule that is sensed by Ipaf, and flagellin-deficient bacteria are compromised in their capability to induce caspase-1 activation and secretion of IL-1beta.
p36
p36
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c84 : 1
stoichiometry:c204 : 1
stoichiometry:c100 : 1
stoichiometry:c207 : 1
m38*m16910*0.1
nodelay
--
0
PMID: 17967410 These results demonstrate that TLR5 and Ipaf represent two flagellin receptors that have evolved to control distinct signaling pathways (NF-kappaB activation and caspase-1 activation, respectively) when the host is infected with Salmonella or Legionella.
p37
p37
cso30:i:ME_ProteinCleavage
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c101 : 1
stoichiometry:c103 : 1
stoichiometry:c185 : 1
stoichiometry:c102 : 1
m4012*m1765*m79*0.1
nodelay
--
0
PMID: 17967410, 16984919, 16648852, 16648853 Flagellin was identified as the bacterial molecule that is sensed by Ipaf, and flagellin-deficient bacteria are compromised in their capability to induce caspase-1 activation and secretion of IL-1beta. PMID: 17967410 Active caspase-1 processes the IL-1beta precursor into the mature cytokine, which is secreted through an unknown mechanism. PMID: 17967410, 15190255, 12191486 This bipartite CARD-PYD protein bridges the association of caspase-1 to the NLR proteins Nalp1 and Cryopyrin in the inflammasomes and therefore plays a major role in the activation of caspase-1 and the subsequent maturation of the inflammatory cytokines IL-1beta and IL-18. PMID: 17967410, 16407888 Bacterial RNA and the imidazoquinoline compounds R837 and R848 alone induce IL-1beta secretion, but a brief pulse with ATP markedly enhances caspase-1 activation and IL-1beta maturation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c105 : 1
stoichiometry:c106 : 1
stoichiometry:c107 : 1
m12*m44*0.1
nodelay
--
0
PMID: 17967410, 17349957 Although there is no evidence for a physical interaction between cryopyrin and microbial molecules, purified NALP1 has been shown to mediate caspase-1 activation in response to MDP.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c108 : 1
stoichiometry:c109 : 1
stoichiometry:c110 : 1
m21736*m45*0.1
nodelay
--
0
PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
m6*0.1
nodelay
--
0
PMID: 17967410 The current model proposes that when PAMPs are sensed by the C-terminal LRRs, the molecule undergoes conformational rearrangements triggering oligomerization via the NOD domain.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c111 : 1
stoichiometry:c112 : 1
stoichiometry:c113 : 1
m46*m36509*0.1
nodelay
--
0
PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.
p41
p41
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c125 : 1
stoichiometry:c126 : 1
stoichiometry:c114 : 1
stoichiometry:c115 : 1
stoichiometry:c136 : 1
m69*0.1
nodelay
--
0
PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5. PMID: 17967410, 17418785 Recently, Reed and colleagues showed that the antiapoptotic Bcl-2 members Bcl-2 and Bcl-XL specifically interact with human Nalp1 and prevent Nalp1-mediated caspase-1 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c118 : 1
stoichiometry:c138 : 1
m68*0.1
nodelay
--
0
PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c120 : 1
stoichiometry:c121 : 1
stoichiometry:c122 : 1
m44*m49*0.1
nodelay
--
0
PMID: 17967410, 17418785 Recently, Reed and colleagues showed that the antiapoptotic Bcl-2 members Bcl-2 and Bcl-XL specifically interact with human Nalp1 and prevent Nalp1-mediated caspase-1 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c123 : 1
stoichiometry:c124 : 1
m2028*0.1
nodelay
--
0
PMID: 17967410, 17418785 Recently, Reed and colleagues showed that the antiapoptotic Bcl-2 members Bcl-2 and Bcl-XL specifically interact with human Nalp1 and prevent Nalp1-mediated caspase-1 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c127 : 1
stoichiometry:c129 : 1
stoichiometry:c128 : 1
m65*m43*0.1
nodelay
--
0
PMID: 17967410 Salmonella and Legionella flagellin are sensed by Ipaf, whereas mouse Nalp1b recognizes anthrax lethal toxin.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c95 : 1
stoichiometry:c130 : 1
stoichiometry:c131 : 1
m41*m40*0.1
nodelay
--
0
PMID: 17967410, 12191486 The prodomain of the prototypical inflammatory caspase-1 encodes a CARD, also present in the C terminus of NOD1, NOD2, and RICK. Caspase-1 is recruited to large multiprotein complexes known as ¡Èinflammasomes¡É through homotypic interactions with the CARD motif in the adaptor ASC.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c133 : 1
stoichiometry:c134 : 1
stoichiometry:c135 : 1
m47*m40*0.1
nodelay
--
0
PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c116 : 1
stoichiometry:c117 : 1
stoichiometry:c119 : 1
m2380*m47*0.1
nodelay
--
0
PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c139 : 1
stoichiometry:c140 : 1
stoichiometry:c141 : 1
m70*m155666*0.1
nodelay
--
0
PMID: 17967410, 17008311, 17433728, 16407890 Cryopyrin and the inflammasome adaptor ASC are required for caspase-1 activation in response to microbial products with diverse molecular structures such as LPS, peptidoglycan, and lipoteichoic acid when combined with millimolar concentrations of ATP.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c14 : 1
stoichiometry:c16 : 1
m2684*m14*0.1
nodelay
--
0
PMID: 17967410, 10329646, 11087742 Direct or indirect ligand recognition by the LRRs of NOD1 and NOD2 induces the recruitment of RICK through homotypic CARD interactions.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c142 : 1
stoichiometry:c143 : 1
stoichiometry:c144 : 1
m70*m72*0.1
nodelay
--
0
PMID: 17967410, 17008311, 17433728, 16407890 Cryopyrin and the inflammasome adaptor ASC are required for caspase-1 activation in response to microbial products with diverse molecular structures such as LPS, peptidoglycan, and lipoteichoic acid when combined with millimolar concentrations of ATP.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c145 : 1
stoichiometry:c146 : 1
stoichiometry:c147 : 1
m70*m74*0.1
nodelay
--
0
PMID: 17967410, 17008311, 17433728, 16407890 Cryopyrin and the inflammasome adaptor ASC are required for caspase-1 activation in response to microbial products with diverse molecular structures such as LPS, peptidoglycan, and lipoteichoic acid when combined with millimolar concentrations of ATP.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c149 : 1
stoichiometry:c148 : 1
m93364*0.1
nodelay
--
0
PMID: 17967410, 17433728 Nevertheless, TLRs are still essential for NF-kappaB-dependent production of pro-IL-1beta.
p53
p53
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c150 : 1
stoichiometry:c152 : 1
stoichiometry:c151 : 1
m40*m155666*0.1
nodelay
--
0
PMID: 17967410, 17433728, 15507117 Indeed, the TLR4 ligand LPS induced activation of caspase-1 in macrophages deficient in MyD88, TRIF, or TLR4.
p54
p54
cso30:i:ME_Translocation
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c153 : 1
stoichiometry:c155 : 1
stoichiometry:c154 : 1
m76*m39857*0.1
nodelay
--
0
PMID: 17967410 In this model, pannexin-1 delivers bacterial molecules into the cytosol where they are sensed by cryopyrin. PMID: 17967410, 17036048 Notably, pannexin-1 was found to be critical for caspase-1 activation and IL-1beta secretion in LPS-stimulated macrophages pulsed with ATP.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c156 : 1
stoichiometry:c157 : 1
stoichiometry:c158 : 1
m21736*m71*0.1
nodelay
--
0
PMID: 17067410 Another NLR protein, the CIITA transcription factor, is required for the transcription of genes encoding MHC II, whereas the NLR family members Nalp1 and Cryopyrin recruit the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD) to activate caspase-1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c159 : 1
stoichiometry:c160 : 1
stoichiometry:c161 : 1
m77*m40*0.1
nodelay
--
0
PMID: 17067410 Another NLR protein, the CIITA transcription factor, is required for the transcription of genes encoding MHC II, whereas the NLR family members Nalp1 and Cryopyrin recruit the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD) to activate caspase-1.
p57
p57
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c162 : 1
stoichiometry:c186 : 1
stoichiometry:c163 : 1
stoichiometry:c164 : 1
m78*m79*0.1
nodelay
--
0
PMID: 17967410 Cryopyrin/Nalp3 mediates caspase-1 activation in response to a wide variety of microbial components and the endogenous danger signal uric acid. PMID: 17967410 The latter is more consistent with the fact that cryopyrin induces caspase-1 activation in response to a plethora of bacterial ligands in the presence of ATP.
p58
p58
cso30:i:ME_ChannelOpening_ClosingInThePlasmaMembrane
cso30:i:CC_Cell_WithoutCellWall_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c165 : 1
stoichiometry:c166 : 1
stoichiometry:c167 : 1
stoichiometry:c193 : 1
m79*m88*m80*0.1
nodelay
--
0
PMID: 17967410 Bacteria and bacterial products enter the cytosol via pore-forming toxins, type III or IV secretion systems, or ATP-mediated activation of the pannexin-1 pore. PMID: 17967410, 17240370, 17121814, 17036048 Recent studies have revealed that the rapid activation of P2X7 receptor is followed by the gradual opening of a larger pore attributed to the hemichannel pannexin-1, which is recruited upon P2X7 receptor activation.
p59
p59
cso30:i:ME_Translocation
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c168 : 1
stoichiometry:c170 : 1
stoichiometry:c169 : 1
m82*m81*0.1
nodelay
--
0
PMID: 17967410 Bacteria and bacterial products enter the cytosol via pore-forming toxins, type III or IV secretion systems, or ATP-mediated activation of the pannexin-1 pore.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c11 : 1
stoichiometry:c12 : 1
stoichiometry:c15 : 1
m13*m2684*0.1
nodelay
--
0
PMID: 17967410, 10329646, 11087742 Direct or indirect ligand recognition by the LRRs of NOD1 and NOD2 induces the recruitment of RICK through homotypic CARD interactions.
p60
p60
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell_WithoutCellWall_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c171 : 1
stoichiometry:c173 : 1
stoichiometry:c172 : 1
m40*m85*0.1
nodelay
--
0
PMID: 17967410 Francisella induce ASC-dependent caspase-1 activation through an NLR, the identity of which is unknown.
p61
p61
cso30:i:ME_ProteinCleavage
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c174 : 1
stoichiometry:c176 : 1
stoichiometry:c175 : 1
m841*m1765*0.1
nodelay
--
0
PMID: 17967410, 15190255, 12191486 This bipartite CARD-PYD protein bridges the association of caspase-1 to the NLR proteins Nalp1 and Cryopyrin in the inflammasomes and therefore plays a major role in the activation of caspase-1 and the subsequent maturation of the inflammatory cytokines IL-1beta and IL-18.
p62
p62
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell_WithoutCellWall_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c179 : 1
stoichiometry:c181 : 1
stoichiometry:c184 : 1
stoichiometry:c180 : 1
m40*m84*m79*0.1
nodelay
--
0
PMID: 17967410, 16407888 Bacterial RNA and the imidazoquinoline compounds R837 and R848 alone induce IL-1beta secretion, but a brief pulse with ATP markedly enhances caspase-1 activation and IL-1beta maturation.
p63
p63
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c177 : 1
stoichiometry:c182 : 1
stoichiometry:c183 : 1
stoichiometry:c178 : 1
m40*m86*m79*0.1
nodelay
--
0
PMID: 17967410, 16407888 Bacterial RNA and the imidazoquinoline compounds R837 and R848 alone induce IL-1beta secretion, but a brief pulse with ATP markedly enhances caspase-1 activation and IL-1beta maturation.
p64
p64
cso30:i:ME_IonTransportThroughIonChannel
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c190 : 1
stoichiometry:c192 : 1
stoichiometry:c191 : 1
m87*m88*0.1
nodelay
--
0
PMID: 17967410, 17491021 Stimulation of the P2X7 receptor with ATP induces K+ efflux, a signal that has been implicated in cryopyrin-mediated caspase-1 activation.
p65
p65
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c194 : 1
stoichiometry:c199 : 1
stoichiometry:c200 : 1
stoichiometry:c195 : 1
m40*m70*m90*0.1
nodelay
--
0
PMID: 17967410, 16407889 The finding that monosodium urate (MSU) and calcium pyrophosphate dehydrate (CPPD) crystals require cryopyrin, but not ATP, to activate caspase-1 suggests a role for the cryopyrin inflammasome in the pathogenesis of gout and pseudogout.
p66
p66
cso30:i:ME_ChannelOpening_ClosingInThePlasmaMembrane
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c187 : 1
stoichiometry:c189 : 1
stoichiometry:c188 : 1
m37969*m79*0.1
nodelay
--
0
PMID: 17967410, 17121814 ATP triggers the potassium-selective channel of the purinergic P2X7 receptor to open.
p67
p67
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c196 : 1
stoichiometry:c198 : 1
stoichiometry:c201 : 1
stoichiometry:c197 : 1
m40*m70*m91*0.1
nodelay
--
0
PMID: 17967410, 16407889 The finding that monosodium urate (MSU) and calcium pyrophosphate dehydrate (CPPD) crystals require cryopyrin, but not ATP, to activate caspase-1 suggests a role for the cryopyrin inflammasome in the pathogenesis of gout and pseudogout.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c17 : 1
stoichiometry:c18 : 1
stoichiometry:c19 : 1
m15*m1593*0.1
nodelay
--
0
PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c20 : 1
stoichiometry:c21 : 1
stoichiometry:c22 : 1
m1593*m16*0.1
nodelay
--
0
PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m17*0.1
nodelay
--
0
PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.
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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c: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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c: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: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: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:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
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: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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c: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:InputAssociation
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,
--