_enti_e7
_enti_e8
_enti_e9
_enti_e1
_enti_e10
_enti_e2
_enti_e4
_enti_e3
_enti_e55
_enti_e59
_enti_e53
_enti_e51
_enti_e56
_enti_e52
_enti_e50
_enti_e54
_enti_e57
_enti_e58
_enti_e61
_enti_e62
_enti_e60
g2_fact_g2
g1_fact_g1
g1_fact_g14
g2_fact_g12
g2_fact_g13
p1_propro_p1
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.
c1 cso30:c:InputProcess connector
c2 cso30:c:InputProcess connector
c3 cso30:c:OutputProcess connector
p2_propro_p2
PMID: 17967410, 12527755, 12514169
In contrast, NOD2 is activated by muramyl dipeptide (MDP), a component of virtually all types of PGN.
c4 cso30:c:InputProcess connector
c5 cso30:c:InputProcess connector
c6 cso30:c:OutputProcess connector
p3_propro_p3
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.
c9 cso30:c:InputProcess connector
c10 cso30:c:OutputProcess connector
p4_propro_p4
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.
c7 cso30:c:InputProcess connector
c8 cso30:c:OutputProcess connector
p5_propro_p5
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.
c13 cso30:c:InputProcess connector
c14 cso30:c:InputProcess connector
c16 cso30:c:OutputProcess connector
p6_propro_p6
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.
c11 cso30:c:InputProcess connector
c12 cso30:c:InputProcess connector
c15 cso30:c:OutputProcess connector
p7_propro_p7
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.
c17 cso30:c:InputProcess connector
c18 cso30:c:InputProcess connector
c19 cso30:c:OutputProcess connector
p8_propro_p8
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.
c20 cso30:c:InputProcess connector
c21 cso30:c:InputProcess connector
c22 cso30:c:OutputProcess connector
p9_propro_p9
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.
c23 cso30:c:InputProcess connector
c24 cso30:c:OutputProcess connector
p10_propro_p10
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.
c25 cso30:c:InputProcess connector
c26 cso30:c:OutputProcess connector
p11_propro_p11
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
c27 cso30:c:InputProcess connector
c28 cso30:c:InputProcess connector
c29 cso30:c:OutputProcess connector
p12_propro_p12
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.
c32 cso30:c:InputProcess connector
c34 cso30:c:InputAssociation connector
c33 cso30:c:OutputProcess connector
p13_propro_p13
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
c30 cso30:c:InputProcess connector
c35 cso30:c:InputAssociation connector
c31 cso30:c:OutputProcess connector
p14_propro_p14
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.
c36 cso30:c:InputProcess connector
c38 cso30:c:InputAssociation connector
c37 cso30:c:OutputProcess connector
p15_propro_p15
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.
c39 cso30:c:InputProcess connector
c41 cso30:c:InputAssociation connector
c40 cso30:c:OutputProcess connector
p16_propro_p16
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.
c42 cso30:c:InputProcess connector
c44 cso30:c:InputAssociation connector
c43 cso30:c:OutputProcess connector
p17_propro_p17
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-κB-dependent target genes occurs.
c48 cso30:c:InputAssociation connector
c202 cso30:c:InputProcess connector
c47 cso30:c:OutputProcess connector
c205 cso30:c:OutputProcess connector
p18_propro_p18
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-κB-dependent target genes occurs.
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c45 cso30:c:InputProcess connector
c46 cso30:c:OutputProcess connector
p19_propro_p19
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-κB-dependent target genes occurs.
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c65 cso30:c:InputAssociation connector
c52 cso30:c:OutputProcess connector
p20_propro_p20
PMID: 17967410
Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
c53 cso30:c:InputProcess connector
c55 cso30:c:InputProcess connector
c54 cso30:c:OutputProcess connector
p21_propro_p21
PMID: 17967410
Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
c56 cso30:c:InputProcess connector
c58 cso30:c:InputAssociation connector
c57 cso30:c:OutputProcess connector
p22_propro_p22
PMID: 17967410
Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
c59 cso30:c:InputProcess connector
c61 cso30:c:InputAssociation connector
c60 cso30:c:OutputProcess connector
p23_propro_p23
PMID: 17967410
Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.
c62 cso30:c:InputProcess connector
c64 cso30:c:InputAssociation connector
c63 cso30:c:OutputProcess connector
p24_propro_p24
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c68 cso30:c:InputAssociation connector
c203 cso30:c:InputProcess connector
c66 cso30:c:OutputProcess connector
c206 cso30:c:OutputProcess connector
p25_propro_p25
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c69 cso30:c:InputProcess connector
c71 cso30:c:InputAssociation connector
c70 cso30:c:OutputProcess connector
p26_propro_p26
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c72 cso30:c:InputProcess connector
c74 cso30:c:InputAssociation connector
c73 cso30:c:OutputProcess connector
p27_propro_p27
PMID: 17967410, 16513653
Moreover, H. pylori-induced production of beta-defensins was abolished in Nod1/ mice.
c76 cso30:c:InputAssociation connector
c77 cso30:c:InputAssociation connector
c75 cso30:c:OutputProcess connector
p28_propro_p28
PMID: 17967410
Recognition of PAMPs by TLRs induces synthesis of the IL-1beta precursor through activation of NF-kappaB.
c49 cso30:c:InputAssociation connector
c78 cso30:c:OutputProcess connector
p29_propro_p29
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.
c80 cso30:c:InputProcess connector
c81 cso30:c:InputProcess connector
c82 cso30:c:OutputProcess connector
p30_propro_p30
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.
c83 cso30:c:InputProcess connector
c104 cso30:c:InputProcess connector
c85 cso30:c:OutputProcess connector
p31_propro_p31
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c86 cso30:c:InputAssociation connector
c89 cso30:c:OutputProcess connector
p32_propro_p32
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c87 cso30:c:InputAssociation connector
c90 cso30:c:OutputProcess connector
p33_propro_p33
PMID: 17967410
The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.
c88 cso30:c:InputAssociation connector
c91 cso30:c:OutputProcess connector
p34_propro_p34
PMID: 17967410
The inflammasome adaptor ASC is required for recruitment of caspase-1, although its role in the Nalp1b inflammasome needs to be confirmed.
c92 cso30:c:InputProcess connector
c93 cso30:c:InputProcess connector
c94 cso30:c:OutputProcess connector
p35_propro_p35
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.
c132 cso30:c:InputProcess connector
c96 cso30:c:OutputProcess connector
c97 cso30:c:OutputProcess connector
p36_propro_p36
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.
c84 cso30:c:InputAssociation connector
c204 cso30:c:InputProcess connector
c100 cso30:c:OutputProcess connector
c207 cso30:c:OutputProcess connector
p37_propro_p37
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.
c101 cso30:c:InputProcess connector
c103 cso30:c:InputAssociation connector
c185 cso30:c:InputAssociation connector
c102 cso30:c:OutputProcess connector
p38_propro_p38
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.
c105 cso30:c:InputProcess connector
c106 cso30:c:InputProcess connector
c107 cso30:c:OutputProcess connector
p39_propro_p39
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.
c108 cso30:c:InputProcess connector
c109 cso30:c:InputProcess connector
c110 cso30:c:OutputProcess connector
p40_propro_p40
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.
c111 cso30:c:InputProcess connector
c112 cso30:c:InputProcess connector
c113 cso30:c:OutputProcess connector
p41_propro_p41
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.
c125 cso30:c:InputInhibitor connector
c126 cso30:c:InputInhibitor connector
c114 cso30:c:InputProcess connector
c115 cso30:c:OutputProcess connector
c136 cso30:c:OutputProcess connector
p42_propro_p42
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.
c137 cso30:c:InputProcess connector
c118 cso30:c:OutputProcess connector
c138 cso30:c:OutputProcess connector
p43_propro_p43
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.
c120 cso30:c:InputProcess connector
c121 cso30:c:InputProcess connector
c122 cso30:c:OutputProcess connector
p44_propro_p44
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.
c123 cso30:c:InputProcess connector
c124 cso30:c:OutputProcess connector
p45_propro_p45
PMID: 17967410
Salmonella and Legionella flagellin are sensed by Ipaf, whereas mouse Nalp1b recognizes anthrax lethal toxin.
c127 cso30:c:InputProcess connector
c129 cso30:c:InputProcess connector
c128 cso30:c:OutputProcess connector
p46_propro_p46
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 “inflammasomes” through homotypic interactions with the CARD motif in the adaptor ASC.
c95 cso30:c:InputProcess connector
c130 cso30:c:InputProcess connector
c131 cso30:c:OutputProcess connector
p47_propro_p47
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.
c133 cso30:c:InputProcess connector
c134 cso30:c:InputProcess connector
c135 cso30:c:OutputProcess connector
p48_propro_p48
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.
c116 cso30:c:InputProcess connector
c117 cso30:c:InputProcess connector
c119 cso30:c:OutputProcess connector
p49_propro_p49
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.
c139 cso30:c:InputProcess connector
c140 cso30:c:InputProcess connector
c141 cso30:c:OutputProcess connector
p50_propro_p50
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.
c142 cso30:c:InputProcess connector
c143 cso30:c:InputProcess connector
c144 cso30:c:OutputProcess connector
p51_propro_p51
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.
c145 cso30:c:InputProcess connector
c146 cso30:c:InputProcess connector
c147 cso30:c:OutputProcess connector
p52_propro_p52
PMID: 17967410, 17433728
Nevertheless, TLRs are still essential for NF-kappaB-dependent production of pro-IL-1beta.
c149 cso30:c:InputAssociation connector
c148 cso30:c:OutputProcess connector
p53_propro_p53
PMID: 17967410, 17433728, 15507117
Indeed, the TLR4 ligand LPS induced activation of caspase-1 in macrophages deficient in MyD88, TRIF, or TLR4.
c150 cso30:c:InputProcess connector
c152 cso30:c:InputAssociation connector
c151 cso30:c:OutputProcess connector
p54_propro_p54
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.
c153 cso30:c:InputProcess connector
c155 cso30:c:InputAssociation connector
c154 cso30:c:OutputProcess connector
p55_propro_p55
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.
c156 cso30:c:InputProcess connector
c157 cso30:c:InputProcess connector
c158 cso30:c:OutputProcess connector
p56_propro_p56
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.
c159 cso30:c:InputProcess connector
c160 cso30:c:InputProcess connector
c161 cso30:c:OutputProcess connector
p57_propro_p57
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.
c162 cso30:c:InputProcess connector
c186 cso30:c:InputAssociation connector
c163 cso30:c:OutputProcess connector
c164 cso30:c:OutputProcess connector
p59_propro_p59
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.
c168 cso30:c:InputProcess connector
c170 cso30:c:InputAssociation connector
c169 cso30:c:OutputProcess connector
p60_propro_p60
PMID: 17967410
Francisella induce ASC-dependent caspase-1 activation through an NLR, the identity of which is unknown.
c171 cso30:c:InputProcess connector
c173 cso30:c:InputAssociation connector
c172 cso30:c:OutputProcess connector
p61_propro_p61
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.
c174 cso30:c:InputProcess connector
c176 cso30:c:InputAssociation connector
c175 cso30:c:OutputProcess connector
p62_propro_p62
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.
c179 cso30:c:InputProcess connector
c181 cso30:c:InputAssociation connector
c184 cso30:c:InputAssociation connector
c180 cso30:c:OutputProcess connector
p63_propro_p63
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.
c177 cso30:c:InputProcess connector
c182 cso30:c:InputAssociation connector
c183 cso30:c:InputAssociation connector
c178 cso30:c:OutputProcess connector
p64_propro_p64
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.
c190 cso30:c:InputProcess connector
c192 cso30:c:InputAssociation connector
c191 cso30:c:OutputProcess connector
p66_propro_p66
PMID: 17967410, 17121814
ATP triggers the potassium-selective channel of the purinergic P2X7 receptor to open.
c187 cso30:c:InputProcess connector
c189 cso30:c:InputAssociation connector
c188 cso30:c:OutputProcess connector
p58_propro_p58
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.
c165 cso30:c:InputAssociation connector
c166 cso30:c:InputAssociation connector
c167 cso30:c:InputProcess connector
c193 cso30:c:OutputProcess connector
p65_propro_p65
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.
c194 cso30:c:InputProcess connector
c199 cso30:c:InputAssociation connector
c200 cso30:c:InputAssociation connector
c195 cso30:c:OutputProcess connector
p67_propro_p67
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.
c196 cso30:c:InputProcess connector
c198 cso30:c:InputAssociation connector
c201 cso30:c:InputAssociation connector
c197 cso30:c:OutputProcess connector
Nod1_enti_MO000020434
Nod1
Nod2_enti_MO000020461
Nod2
iE-DAP_enti_e5
iE-DAP
iE-DAP: Nod1_enti_e6
iE-DAP: Nod1
MDP: Nod2_enti_e11
MDP: Nod2
MDP_enti_e12
MDP
iE-DAP: Nod1{oligomer}_enti_e13
iE-DAP: Nod1{oligomer}
MDP: Nod2{oligomer}_enti_e14
MDP: Nod2{oligomer}
RICK_enti_MO000017949
RICK
iE-DAP: Nod1{oligomer}: RICK_enti_e15
iE-DAP: Nod1{oligomer}: RICK
MDP: Nod2{oligomer}: RICK_enti_e16
MDP: Nod2{oligomer}: RICK
IKK-gamma_enti_MO000016599
IKK-gamma
iE-DAP: Nod1{oligomer}: RICK: IKK-gamma_enti_e17
iE-DAP: Nod1{oligomer}: RICK: IKK-gamma
MDP: Nod2{oligomer}: RICK: IKK-gamma_enti_e18
MDP: Nod2{oligomer}: RICK: IKK-gamma
iE-DAP: Nod1{oligomer}: RICK: IKK-gamma{ubK63}_enti_e19
iE-DAP: Nod1{oligomer}: RICK: IKK-gamma{ubK63}
MDP: Nod2{oligomer}: RICK: IKK-gamma{ubK63}_enti_e20
MDP: Nod2{oligomer}: RICK: IKK-gamma{ubK63}
CARD9_enti_MO000044196
CARD9
MDP: Nod2{oligomer}: RICK: CARD9_enti_e22
MDP: Nod2{oligomer}: RICK: CARD9
TAK1_enti_MO000016574
TAK1
TAK1 {activated}_enti_e23
TAK1 {activated}
p38_enti_MO000000022
p38
p38 {activated}_enti_e24
p38 {activated}
ERK_enti_MO000000011
ERK
ERK{activated}_enti_e25
ERK{activated}
JNK_enti_MO000000023
JNK
JNK{activated}_enti_e26
JNK{activated}
protein remnants_enti_MO000019479
protein remnants
proinflammatory genes_enti_e28
proinflammatory genes
TLRs_enti_MO000019395
TLRs
TLR5_enti_MO000019399
TLR5
TLR ligand_enti_e29
TLR ligand
TLR ligand: TLR_enti_e30
TLR ligand: TLR
MyD88_enti_MO000016573
MyD88
IRAK-1_enti_MO000000213
IRAK-1
MyD88{activated}_enti_e31
MyD88{activated}
IRAK-1{activated}_enti_e32
IRAK-1{activated}
TRAF6_enti_MO000000212
TRAF6
TRAF6{activated}_enti_e33
TRAF6{activated}
CARD9{activated}_enti_e21
CARD9{activated}
DEFB1_enti_G023188
DEFB1
DEFB1_enti_MO000061796
DEFB1
ASC_enti_MO000044014
ASC
IL-1beta_enti_G010389
IL-1beta
flagellin_enti_MO000022185
flagellin
flagellin: TLR5_enti_e34
flagellin: TLR5
IPAF_enti_MO000044055
IPAF
flagellin: IPAF_enti_e35
flagellin: IPAF
Caspase-1{activated}_enti_MO000016828
Caspase-1{activated}
Caspase-1_enti_e36
Caspase-1
flagellin: IPAF: ASC_enti_e37
flagellin: IPAF: ASC
proIL-1beta_enti_MO000019449
proIL-1beta
IL-1beta_enti_MO000016597
IL-1beta
flagellin{cytosolic}_enti_e38
flagellin{cytosolic}
NALP1b_enti_e39
NALP1b
NALP1_enti_e40
NALP1
MDP: NALP1_enti_e41
MDP: NALP1
MDP: NALP1: ASC_enti_e42
MDP: NALP1: ASC
CARDINAL_enti_MO000061612
CARDINAL
MDP: NALP1: ASC: CARDINAL_enti_e43
MDP: NALP1: ASC: CARDINAL
Caspase-5_enti_MO000017601
Caspase-5
Caspase-5{activated}_enti_e44
Caspase-5{activated}
Bcl-2_enti_MO000000039
Bcl-2
Bcl-2: NALP1_enti_e45
Bcl-2: NALP1
Bcl-xL_enti_MO000017151
Bcl-xL
Bcl-xL: NALP1_enti_e46
Bcl-xL: NALP1
Anthrax LT_enti_e47
Anthrax LT
Anthrax LT: NALP1b_enti_e48
Anthrax LT: NALP1b
flagellin: IPAF: ASC: Caspase-1_enti_e49
flagellin: IPAF: ASC: Caspase-1
MDP: NALP1: ASC: CARDINAL: Caspase-5_enti_e63
MDP: NALP1: ASC: CARDINAL: Caspase-5
MDP: NALP1: ASC: CARDINAL: Caspase-1_enti_e64
MDP: NALP1: ASC: CARDINAL: Caspase-1
NALP3_enti_e65
NALP3
LPS_enti_MO000016882
LPS
LPS: NALP3_enti_e66
LPS: NALP3
peptidoglycan_enti_e67
peptidoglycan
peptidoglycan: NALP3_enti_e68
peptidoglycan: NALP3
lipoteic acid: ATP_enti_e69
lipoteic acid: ATP
lipoteic acid: ATP: NALP3_enti_e70
lipoteic acid: ATP: NALP3
LPS{extracellular}_enti_e71
LPS{extracellular}
PANX1{activated}_enti_MO000064988
PANX1{activated}
LPS: NALP3: ASC_enti_e72
LPS: NALP3: ASC
LPS: NALP3: ASC: Caspase-1_enti_e73
LPS: NALP3: ASC: Caspase-1
ATP_enti_e74
ATP
PANX1_enti_e75
PANX1
Pore Formng Toxins_enti_e76
Pore Formng Toxins
bacterial ligand_enti_e77
bacterial ligand
bacterial ligand {extracellular}_enti_e78
bacterial ligand {extracellular}
Francisella: unknown NLR: ASC_enti_e80
Francisella: unknown NLR: ASC
proIL-18_enti_MO000007330
proIL-18
IL-18_enti_MO000016625
IL-18
R848_enti_e79
R848
R837_enti_e81
R837
P2RX7_enti_MO000063086
P2RX7
potasium_enti_e82
K
potasium
P2RX7{openned}_enti_e83
P2RX7{openned}
potasium{extracellular}_enti_e84
K
potasium{extracellular}
CPPD_enti_e85
CPPD
MSU_enti_e86
MSU
p50:RelA-p65:IkappaB-alpha_enti_MO000038724
p50:RelA-p65:IkappaB-alpha
p50:RelA-p65_enti_MO000016632
p50:RelA-p65
p50:RelA-p65{nucleus}_enti_e87
p50:RelA-p65{nucleus}