_enti_e1
_enti_e10
_enti_e2
_enti_e3
_enti_e4
_enti_e5
_enti_e55
_enti_e7
_enti_e6
_enti_e59
_enti_e53
_enti_e54
_enti_e52
_enti_e51
_enti_e50
_enti_e56
_enti_e57
_enti_e61
_enti_e58
_enti_e60
_enti_e62
g1_fact_g2
g1_fact_g1
g2_fact_g12
g2_fact_g13
g1_fact_g14
p1_propro_p1
PMID: 17307033,11752661
The first dsRNA-binding protein to be described was PKR
(Table 1), a key mediator of the antiviral action of type I
interferon (IFN)
PMID: 17307033
A pair of dsRNA-binding domains in
the N-terminal portion of PKR binds to dsRNA.
c1 cso30:c:InputProcess connector
c2 cso30:c:InputProcess connector
c3 cso30:c:OutputProcess connector
p8_propro_p8
PMID: 17307033,15961631,16043704
The TLR3 ectodomain
senses dsRNA both extracellularly and in endosomes,
and its structure has been solved recently
c4 cso30:c:InputProcess connector
c5 cso30:c:InputProcess connector
c6 cso30:c:OutputProcess connector
p2_propro_p2
PMID: 17307033
A pair of dsRNA-binding domains in
the N-terminal portion of PKR binds to dsRNA. PKR
functions to phosphorylate the a subunit of the translation
initiation factor eIF2, thereby inhibiting protein
synthesisA pair of dsRNA-binding domains in
the N-terminal portion of PKR binds to dsRNA. PKR
functions to phosphorylate the a subunit of the translation
initiation factor eIF2, thereby inhibiting protein
synthesis
c7 cso30:c:InputProcess connector
c50 cso30:c:InputAssociation connector
c9 cso30:c:OutputProcess connector
p8_propro_p3
PMID: 17307033,15961631,16043704
The TLR3 ectodomain
senses dsRNA both extracellularly and in endosomes,
and its structure has been solved recently
c10 cso30:c:InputProcess connector
c11 cso30:c:InputProcess connector
c12 cso30:c:OutputProcess connector
p4_propro_p4
PMID: 17307033
Single-stranded RNA of ssRNA viruses is detected
through TLR7 and TLR8, which are located in the endosomal
compartment
c13 cso30:c:InputProcess connector
c14 cso30:c:InputProcess connector
c17 cso30:c:OutputProcess connector
p4_propro_p5
PMID: 17307033
Single-stranded RNA of ssRNA viruses is detected
through TLR7 and TLR8, which are located in the endosomal
compartment
c15 cso30:c:InputProcess connector
c16 cso30:c:InputProcess connector
c18 cso30:c:OutputProcess connector
p6_propro_p6
PMID: 17307033,17038590
Artificial capping or base modification of this 50-triphosphate
(as would occur in host RNA) abolished this
response, which they showed was mediated by direct binding
to RIG-I
PMID: 17307033
Moreover, they found that
ssRNA such as that from the influenza virus genome,
which is uncapped and has a 50-triphosphate moiety,
associated with and activated RIG-I.
c19 cso30:c:InputProcess connector
c34 cso30:c:InputProcess connector
c20 cso30:c:OutputProcess connector
p7_propro_p7
PMID: 17307033,16672351,16625202,16714379
However, a current paradox is that, although negative-stranded paramyxoviruses do not produce detectable amounts of
dsRNA, and are detected by RIG-I and not MDA5 their V proteins bind to Mda5 (and not RIG-I) and inhibit downstream signaling
c22 cso30:c:InputProcess connector
c23 cso30:c:InputProcess connector
c24 cso30:c:OutputProcess connector
p9_propro_p9
PMID: 17307033,17038589
The Pichlmair study also demonstrated that the IAV NS1 protein, which was
thought to block IFN induction by sequestering dsRNA,
instead blocks by forming a complex with RIG-I to abrogate
RIG-I signaling
c25 cso30:c:InputProcess connector
c26 cso30:c:InputProcess connector
c27 cso30:c:OutputProcess connector
p10_propro_p10
PMID: 17307033,17038589
The Pichlmair study also demonstrated that the IAV NS1 protein, which was
thought to block IFN induction by sequestering dsRNA,
instead blocks by forming a complex with RIG-I to abrogate
RIG-I signaling
c28 cso30:c:InputAssociation connector
c30 cso30:c:InputInhibitor connector
c29 cso30:c:OutputProcess connector
p11_propro_p11
PMID: 17303033
Therefore, during infection, RIG-I probably mediates local
IFNa production, which is crucial for the initial antiviral
response, whereas TLR7 controls systemic IFNa levels, as
pDCs make a substantial contribution to the total IFNa
produced during an infection.
c31 cso30:c:InputAssociation connector
c8 cso30:c:InputAssociation connector
c32 cso30:c:OutputProcess connector
p13_propro_p13
PMID: 17303033,17008311
An additional antiviral effector mechanism involves the
production of the inflammatory cytokines interleukin (IL)-1
and IL-18, which are generated by proteolytic processing of
their pro-forms through the action of caspase-1
c35 cso30:c:InputProcess connector
c48 cso30:c:InputAssociation connector
c36 cso30:c:OutputProcess connector
p13_propro_p12
PMID: 17303033,17008311
An additional antiviral effector mechanism involves the
production of the inflammatory cytokines interleukin (IL)-1
and IL-18, which are generated by proteolytic processing of
their pro-forms through the action of caspase-1
c38 cso30:c:InputProcess connector
c49 cso30:c:InputAssociation connector
c39 cso30:c:OutputProcess connector
p14_propro_p14
PMID: 17307033,17008311
Poly(I:C), viral dsRNA and Sendai virus (SeV) all activated
caspase-1 through the nucleotide oligomerization domainlike
receptor protein Nalp3 (also known as cryopyrin)
c40 cso30:c:InputAssociation connector
c41 cso30:c:InputProcess connector
c43 cso30:c:InputAssociation connector
c42 cso30:c:OutputProcess connector
p14_propro_p15
PMID: 17307033,17008311
Poly(I:C), viral dsRNA and Sendai virus (SeV) all activated
caspase-1 through the nucleotide oligomerization domainlike
receptor protein Nalp3 (also known as cryopyrin)
c44 cso30:c:InputAssociation connector
c45 cso30:c:InputAssociation connector
c46 cso30:c:InputProcess connector
c47 cso30:c:OutputProcess connector
p16_propro_p16
PMID: 17307033
Moreover, they found that
ssRNA such as that from the influenza virus genome,
which is uncapped and has a 50-triphosphate moiety,
associated with and activated RIG-I.
c21 cso30:c:InputProcess connector
c37 cso30:c:OutputProcess connector
dsRNA_enti_MO000022224
dsRNA
PKR_enti_MO000008179
PKR
dsRNA:PKR_enti_MO000022225
dsRNA:PKR
TLR3_enti_MO000019398
TLR3
dsRNA:TLR3_enti_MO000041446
dsRNA:TLR3
eIF-2alpha_enti_MO000022570
eIF-2alpha
eIF-2alpha{p}_enti_e8
eIF-2alpha{p}
TLR7_enti_MO000042126
TLR7
TLR8_enti_MO000042007
TLR8
ssRNA_enti_e11
ssRNA
ssRNA:TLR7_enti_e12
ssRNA:TLR7
ssRNA:TLR8_enti_e13
ssRNA:TLR8
DDX58_enti_MO000066987
DDX58
IFIH1_enti_MO000103999
IFIH1
V proteins_enti_e16
V proteins
MDA5:V proteins_enti_e17
MDA5:V proteins
IAV NS1_enti_e18
IAV NS1
DDX58:IAV NS1_enti_e19
DDX58:IAV NS1
IFN_enti_e20
IFN
IFN_enti_e21
IFN
TLR3_enti_e9
TLR3
dsRNA:TLR3_enti_e22
dsRNA:TLR3
IFN-alpha_enti_e23
IFN-alpha
IFN alpha _enti_e24
IFN alpha
IL-1_enti_MO000000214
IL-1
Caspase-1_enti_MO000016828
Caspase-1
IL-18_enti_MO000016625
IL-18
proIL-18_enti_MO000007330
proIL-18
Pro IL-1_enti_e25
Pro IL-1
Nalp3_enti_e26
Nalp3
Caspase-1{active}_enti_e27
Caspase-1{active}
Poly I:C_enti_e28
Poly I:C
DDX58:ssRNA_enti_e14
DDX58:ssRNA
DDX58{active}:ssRNA_enti_e15
DDX58{active}:ssRNA