Original Literature | Model OverView |
---|---|
Publication
Title
NOD-like receptors (NLRs): bona fide intracellular microbial sensors.
Affiliation
Department of Pathology and Comprehensive Cancer Center, University of MichiganMedical School, Ann Arbor, MI 48109, USA.
Abstract
The nucleotide-binding oligomerization domain (NOD)-like receptor (NLR)(nucleotide-binding domain leucine-rich repeat containing) family of proteinshas been demonstrated to function as regulators of innate immune responseagainst microbial pathogens. Stimulation of NOD1 and NOD2, two prototypic NLRs,results in the activation of MAPK and NF-kappaB. On the other hand, a differentset of NLRs induces caspase-1 activation through the assembly of aninflammasome. This review discusses recent findings regarding the signalingpathways utilized by NLR proteins in the control of caspase-1 and NF-kappaBactivation, as well as the nonredundant role of NLRs in pathogen clearance. Thereview also covers advances regarding the cellular localization of theseproteins and the implications this may have on pathogen sensing and signaltransduction.
PMID
18585455
|
Entity
p38
--
MO000000022
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m33
10
infinite
0
TRANSPATH | MO000000022 |
--
NF-kappaB
--
MO000000058
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m53
10
infinite
0
TRANSPATH | MO000000058 |
--
IKK-alpha:IKK-beta:Nemo
--
MO000000210
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m181
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000210 |
--
Caspase-1
--
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 |
--
--
e1
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane
--
--
--
csml-variable:Double
m1
0
infinite
0
--
Nod1{oligo}:PGN
--
e11
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m11
0
infinite
0
--
Nod2{oligo}:PGN
--
e12
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m12
0
infinite
0
--
Nod1{oligo}:PGN:RIP2
--
e13
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m13
0
infinite
0
--
Nod2{oligo}:PGN:RIP2
--
e14
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m14
0
infinite
0
--
Nod1{oligo}:PGN:RIP2{ub}
--
e15
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m15
0
infinite
0
--
Nod2{oligo}:PGN:RIP2{ub}
--
e16
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m16
0
infinite
0
--
Nod1{oligo}:PGN:RIP2{ub}:TAK1
--
e17
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m17
0
infinite
0
--
Nod2{oligo}:PGN:RIP2{ub}:TAK1
--
e18
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m18
0
infinite
0
--
--
e2
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m2
0
infinite
0
--
Nod1{oligo}:PGN:RIP2{ub}:TAK1:IKK
--
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
--
Nod2{oligo}:PGN:RIP2{ub}:TAK1:IKK
--
e30
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m30
0
infinite
0
--
Nod1{oligo}:PGN:RIP2{ub}:TAK1:IKK{active}
--
e31
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m31
0
infinite
0
--
Nod2{oligo}:PGN:RIP2{ub}:TAK1:IKK{active}
--
e32
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m32
0
infinite
0
--
Nod2:CARD9
--
e35
cso30:c:Complex
cso30:i:CC_Cell
--
--
csml-variable:Double
m35
0
infinite
0
--
L.momocytogenes
--
e36
cso30:c:Cell
cso30:i:CC_Cell
--
--
csml-variable:Double
m36
0
infinite
0
--
NF-kappaB{active}
--
e37
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m37
10
infinite
0
TRANSPATH | MO000000058 |
--
p38{p}
--
e39
cso30:c:Protein
cso30:i:CC_Cell
--
--
csml-variable:Double
m42
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
TLR
--
e40
cso30:c:Complex
cso30:i:CC_Cell
--
--
csml-variable:Double
m43
0
infinite
0
--
Caspase-1{active}
--
e41
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m44
10
infinite
0
TRANSPATH | MO000016828 |
--
NLRC4
--
e42
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m45
0
infinite
0
--
csml-variable:Double
m46
0
infinite
0
--
Nod1:PGN
--
e5
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m5
0
infinite
0
--
Nod2:PGN
--
e6
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m6
0
infinite
0
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m155701*m4923*0.1
nodelay
--
0
PMID: 18585455,12796777,12791997 NOD1 activity is triggered by g-Dglutamyl- meso-diaminopimelic acid (meso-DAP) 1), which is unique to PGN structures from all Gram-negative bacteria and certain Gram-positive bacteria, including the genus Listeria and Bacillus
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c26 : 1
stoichiometry:c27 : 1
stoichiometry:c28 : 1
m15*m1573*0.1
nodelay
--
0
PMID: 18585455 K63-linked regulatory ubiquitination of RICK leads to the recruitment of TAK1. PMID: 18585455,18079694,18342009 Similar to TLR signaling, recent studies have demonstrated that K63-linked regulatory ubiquitination of RICK is essential for the recruitment of TAK1
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c29 : 1
stoichiometry:c30 : 1
stoichiometry:c31 : 1
m16*m1573*0.1
nodelay
--
0
PMID: 18585455 K63-linked regulatory ubiquitination of RICK leads to the recruitment of TAK1. PMID: 18585455,18079694,18342009 Similar to TLR signaling, recent studies have demonstrated that K63-linked regulatory ubiquitination of RICK is essential for the recruitment of TAK1
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c32 : 1
stoichiometry:c33 : 1
stoichiometry:c34 : 1
m17*m181*0.1
nodelay
--
0
PMID: 18585455 The activation and recruitment of TAK1 complex to RICK further recruits the IKK complex
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c35 : 1
stoichiometry:c36 : 1
stoichiometry:c37 : 1
m18*m181*0.1
nodelay
--
0
PMID: 18585455 The activation and recruitment of TAK1 complex to RICK further recruits the IKK complex
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c38 : 1
stoichiometry:c39 : 1
m29*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c40 : 1
stoichiometry:c41 : 1
m30*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1
p14
p16
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c42 : 1
stoichiometry:c47 : 1
stoichiometry:c55 : 1
m31*m33*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1 PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c45 : 1
stoichiometry:c71 : 1
stoichiometry:c72 : 1
m15*m1585*0.1
nodelay
--
0
PMID: 18585455,18079694,18342009 As in the case of TLRs, this modification can be removed by the deubiquitinating enzyme A20, thus dampening NOD1/NOD2-induced NF-kB activation
p18
p18
cso30:i:ME_Binding
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c48 : 1
stoichiometry:c49 : 1
stoichiometry:c51 : 1
stoichiometry:c50 : 1
m4947*m21914*m36*0.1
nodelay
--
0
PMID: 18585455 Recently it was demonstrated that ectopically expressed CARD9, an essential protein in antifungal responses and TLR signaling, interacts with NOD2 after challenge with L. monocytogenes.
p19
p19
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c52 : 1
stoichiometry:c53 : 1
stoichiometry:c54 : 1
m31*m53*0.1
nodelay
--
0
PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m155701*m4947*0.1
nodelay
--
0
PMID: 18585455,12527755,12514169 In contrast, NOD2 is activated by muramyl dipeptide (MDP), a peptidogylcan motif present in all Gram-positive and Gram-negative bacteria
p19
p20
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c43 : 1
stoichiometry:c44 : 1
stoichiometry:c46 : 1
m32*m53*0.1
nodelay
--
0
PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
p14
p21
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c57 : 1
stoichiometry:c58 : 1
m31*m34*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1 PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
p14
p22
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c59 : 1
stoichiometry:c60 : 1
stoichiometry:c61 : 1
m31*m38*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1 PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
p14
p23
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c62 : 1
stoichiometry:c63 : 1
stoichiometry:c64 : 1
m32*m38*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1 PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
p14
p24
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c65 : 1
stoichiometry:c66 : 1
stoichiometry:c67 : 1
m32*m34*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1 PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
p14
p25
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c69 : 1
stoichiometry:c70 : 1
m32*m33*0.1
nodelay
--
0
PMID: 18585455 The interaction between RICK and NEMO ultimately results in the activation of IKKs and MKK by TAK1 PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c73 : 1
stoichiometry:c75 : 1
stoichiometry:c74 : 1
m16*m1585*0.1
nodelay
--
0
PMID: 18585455,18079694,18342009 As in the case of TLRs, this modification can be removed by the deubiquitinating enzyme A20, thus dampening NOD1/NOD2-induced NF-kB activation
p27
p27
cso30:i:ME_Phosphorylation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c76 : 1
stoichiometry:c78 : 1
stoichiometry:c77 : 1
m33*m21914*0.1
nodelay
--
0
PMID: 18585455,17187069 Furthermore, CARD9-deficient macrophages exhibited impaired phosphorylation of p38 after MDP stimulation, suggesting that CARD9 is another essential intermediate in the NOD2-signaling cascade that acts downstream of TAK1
p28
p28
cso30:i:ME_UnknownActivation
cso30:i:CC_Cell
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c79 : 1
stoichiometry:c81 : 1
stoichiometry:c80 : 1
m53*m43*0.1
nodelay
--
0
PMID: 18585455,17433728 TLR-mediated NF-kB is required for the production of pro-IL-1b while the cleavage of pro-IL-1b into its biologically active form is dependent on NLR-mediated caspase-1 activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c82 : 1
stoichiometry:c83 : 1
m37*0.1
nodelay
--
0
PMID: 18585455,17433728 TLR-mediated NF-kB is required for the production of pro-IL-1b while the cleavage of pro-IL-1b into its biologically active form is dependent on NLR-mediated caspase-1 activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
m5*0.1
nodelay
--
0
PMID: 18585455 Upon ligand recognition, NOD1 and NOD2 undergo conformational changes and selfoligomerization.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c84 : 1
stoichiometry:c89 : 1
stoichiometry:c85 : 1
m4012*m44*0.1
nodelay
--
0
PMID: 18585455,17433728 TLR-mediated NF-kB is required for the production of pro-IL-1b while the cleavage of pro-IL-1b into its biologically active form is dependent on NLR-mediated caspase-1 activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c87 : 1
stoichiometry:c86 : 1
stoichiometry:c88 : 1
m1765*m5*0.1
nodelay
--
0
PMID: 18585455,17433728 TLR-mediated NF-kB is required for the production of pro-IL-1b while the cleavage of pro-IL-1b into its biologically active form is dependent on NLR-mediated caspase-1 activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c91 : 1
stoichiometry:c99 : 1
stoichiometry:c92 : 1
m1765*m6*0.1
nodelay
--
0
PMID: 18585455,17433728 TLR-mediated NF-kB is required for the production of pro-IL-1b while the cleavage of pro-IL-1b into its biologically active form is dependent on NLR-mediated caspase-1 activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c93 : 1
stoichiometry:c94 : 1
stoichiometry:c95 : 1
m45*m1765*0.1
nodelay
--
0
PMID: 18585455 NLRC4 has been demonstrated to mediate caspase-1 activation, independent of TLR5, following cytosolic delivery of flagellin. PMID: 18585455 Various intracellular bacteria have the ability to activate caspase-1 in a NLRC4-dependent manner
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c96 : 1
stoichiometry:c97 : 1
stoichiometry:c98 : 1
m46*m1765*0.1
nodelay
--
0
PMID: 18585455 NLRP3 mediates activation of caspase-1 in response to a variety of structurally unrelated stimuli, not limiting to those of bacterial origin.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c9 : 1
stoichiometry:c10 : 1
m6*0.1
nodelay
--
0
PMID: 18585455 Upon ligand recognition, NOD1 and NOD2 undergo conformational changes and selfoligomerization.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c11 : 1
stoichiometry:c12 : 1
stoichiometry:c13 : 1
m2684*m11*0.1
nodelay
--
0
PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c14 : 1
stoichiometry:c16 : 1
stoichiometry:c15 : 1
m2684*m12*0.1
nodelay
--
0
PMID: 18585455,10880512,11463746,17277144,17579072 This is followed by the recruitment and activation of the serine threonine kinase RICK (RIP2), essential for the activation of NF-kB and MAPKs
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c17 : 1
stoichiometry:c18 : 1
stoichiometry:c19 : 1
m13*m180*0.1
nodelay
--
0
PMID: 18585455 Although, both NOD1 and NOD2 induce similar K63-linked ubiquitination of RICK for NF-kB activation, Nod2-signaling appears to preferentially utilize the E3 ligase TRAF6, whereas TRAF2 and TRAF5 were shown to be important for NOD1-mediated signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c20 : 1
stoichiometry:c21 : 1
stoichiometry:c22 : 1
m13*m1874*0.1
nodelay
--
0
PMID: 18585455 Although, both NOD1 and NOD2 induce similar K63-linked ubiquitination of RICK for NF-kB activation, Nod2-signaling appears to preferentially utilize the E3 ligase TRAF6, whereas TRAF2 and TRAF5 were shown to be important for NOD1-mediated signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c23 : 1
stoichiometry:c24 : 1
stoichiometry:c25 : 1
m14*m183*0.1
nodelay
--
0
PMID: 18585455 Although, both NOD1 and NOD2 induce similar K63-linked ubiquitination of RICK for NF-kB activation, Nod2-signaling appears to preferentially utilize the E3 ligase TRAF6, whereas TRAF2 and TRAF5 were shown to be important for NOD1-mediated signaling.
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: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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c: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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c: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:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputAssociation
threshold
--
0
1,
--