HUMAN:DDX58

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	DDX58
Protein Name(s)	Probable ATP-dependent RNA helicase DDX58 DEAD box protein 58 RIG-I-like receptor 1 RLR-1 Retinoic acid-inducible gene 1 protein RIG-1 Retinoic acid-inducible gene I protein RIG-I
External Links
UniProt	O95786
EMBL	AF038963 AL353671 AL161783 AL161783 AL353671 CH471071 BC132786 BC136610 BX647917 AL137608
CCDS	CCDS6526.1
PIR	T46312
RefSeq	NP_055129.2
UniGene	Hs.190622
PDB	2LWD 2LWE 2QFB 2QFD 2RMJ 2YKG 3LRN 3LRR 3NCU 3OG8 3TMI 3ZD6 3ZD7 4AY2 4BPB 4NQK 4ON9 4P4H
PDBsum	2LWD 2LWE 2QFB 2QFD 2RMJ 2YKG 3LRN 3LRR 3NCU 3OG8 3TMI 3ZD6 3ZD7 4AY2 4BPB 4NQK 4ON9 4P4H
ProteinModelPortal	O95786
SMR	O95786
BioGrid	117121
DIP	DIP-35444N
IntAct	O95786
MINT	MINT-2799116
STRING	9606.ENSP00000369213
PhosphoSite	O95786
MaxQB	O95786
PaxDb	O95786
PRIDE	O95786
Ensembl	ENST00000379883
GeneID	23586
KEGG	hsa:23586
UCSC	uc003zra.3 uc010mjk.1
CTD	23586
GeneCards	GC09M032447
HGNC	HGNC:19102
HPA	CAB012643 HPA047193
MIM	609631
neXtProt	NX_O95786
PharmGKB	PA134994272
eggNOG	COG1111
GeneTree	ENSGT00510000046789
HOGENOM	HOG000230911
HOVERGEN	HBG052325
InParanoid	O95786
KO	K12646
OMA	KCKAFAC
PhylomeDB	O95786
TreeFam	TF330258
Reactome	REACT_115831 REACT_24938 REACT_24969 REACT_25026 REACT_25039 REACT_25271 REACT_25359
ChiTaRS	DDX58
EvolutionaryTrace	O95786
GeneWiki	RIG-I
GenomeRNAi	23586
NextBio	46208
PRO	PR:O95786
Proteomes	UP000005640
Bgee	O95786
CleanEx	HS_DDX58
ExpressionAtlas	O95786
Genevestigator	O95786
GO	GO:0015629 GO:0005737 GO:0005829 GO:0032587 GO:0005923 GO:0005524 GO:0003690 GO:0003725 GO:0004386 GO:0042802 GO:0003727 GO:0008270 GO:0039528 GO:0009597 GO:0045087 GO:0032480 GO:0002230 GO:0032727 GO:0032728 GO:0051091 GO:0042993 GO:0045944 GO:0030334 GO:0034344 GO:0043330 GO:0009615 GO:0039529 GO:0016032
Gene3D	1.10.533.10 3.40.50.300
InterPro	IPR003593 IPR011545 IPR011029 IPR014001 IPR001650 IPR027417 IPR021673
Pfam	PF00270 PF00271 PF11648
SMART	SM00382 SM00487 SM00490
SUPFAM	SSF52540
PROSITE	PS51192 PS51194

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
acts_upstream_of_or_within	GO:0043330	response to exogenous dsRNA	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6Q899	P		Seeded From UniProt	complete
involved_in	GO:0002735	positive regulation of myeloid dendritic cell cytokine production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6Q899	P		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	PMID:21478870^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902741	positive regulation of interferon-alpha secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071360	cellular response to exogenous dsRNA	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060760	positive regulation of response to cytokine stimulus	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035549	positive regulation of interferon-beta secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904469	positive regulation of tumor necrosis factor secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000778	positive regulation of interleukin-6 secretion	PMID:21957149^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:26471729^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96EQ8	F		Seeded From UniProt	complete
involved_in	GO:0032725	positive regulation of granulocyte macrophage colony-stimulating factor production	PMID:24409285^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:24409285^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032757	positive regulation of interleukin-8 production	PMID:24409285^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032755	positive regulation of interleukin-6 production	PMID:24409285^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	PMID:17079289^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q14653)	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:17079289^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:17079289^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009597	detection of virus	PMID:17079289^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	PMID:19631370^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	PMID:19609254^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0039529	RIG-I signaling pathway	PMID:19211564^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:19211564^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:19609254^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032728	positive regulation of interferon-beta production	PMID:19631370^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032727	positive regulation of interferon-alpha production	PMID:19609254^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032727	positive regulation of interferon-alpha production	PMID:19576794^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	PMID:19122199^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030334	regulation of cell migration	PMID:19122199^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:19122199^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:18243112^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005923	bicellular tight junction	PMID:19122199^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21102435^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003727	single-stranded RNA binding	PMID:19211564^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:19211564^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:19576794^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002230	positive regulation of defense response to virus by host	PMID:19609254^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21102435^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95786	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	P		Seeded From UniProt	complete
	GO:0032755	positive regulation of interleukin-6 production	PMID:24409285^[4]	ECO:0000314			P		In Figure 2A agonists of RIG-I poly LL and CpG-ODN show that RIG-I increases the production of Interleukin 6 in End1/E6E7 cells as shown by ELISA test.	complete CACAO 9273
involved_in	GO:0043330	response to exogenous dsRNA	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	P		Seeded From UniProt	complete
	GO:0032757	positive regulation of interleukin-8 production	PMID:24409285^[4]	ECO:0000314			P		In Figure 2A agonists of RIG-I poly LL and CpG-ODN show that RIG-I increases the production of Interleukin 8 in End1/E6E7 cells as shown by ELISA test	complete CACAO 9274
involved_in	GO:0032728	positive regulation of interferon-beta production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	P		Seeded From UniProt	complete
	GO:0010628	positive regulation of gene expression	PMID:24409285^[4]	ECO:0000314			P		Figure 3 A graph 1 and Figure 3b show that when RIG-I agonists are applied there is an increased expression of p65-NF-kB when compared to the control thus showingthat RIG-I increases expression of p65 NF-kB in End1/E6E7 cells.	complete CACAO 9277
involved_in	GO:0009615	response to virus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	P		Seeded From UniProt	complete
	GO:0032725	positive regulation of granulocyte macrophage colony-stimulating factor production	PMID:24409285^[4]	ECO:0000314			P		Figure 4 A and B show that when subjected to agonists RIG-I increases the production of GM-CSF in End1/E6E7 cells when compared to the control.	complete CACAO 9284
enables	GO:0003727	single-stranded RNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	F		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	F		Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	F		Seeded From UniProt	complete
involved_in	GO:0002735	positive regulation of myeloid dendritic cell cytokine production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q6Q899 ensembl:ENSMUSP00000042433	P		Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011545	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011545	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24590070^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95786-1	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20581823^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95786-1	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17190814^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95786-1	F		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:17079289^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0039528	cytoplasmic pattern recognition receptor signaling pathway in response to virus	PMID:21616437^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034344	regulation of type III interferon production	PMID:21616437^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	PMID:21616437^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	Reactome:R-HSA-8983711	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	Reactome:R-HSA-168249	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032480	negative regulation of type I interferon production	Reactome:R-HSA-936440	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-NUL-936401 Reactome:R-HSA-990528 Reactome:R-HSA-990526 Reactome:R-HSA-937343 Reactome:R-HSA-936563 Reactome:R-HSA-936475 Reactome:R-HSA-936390 Reactome:R-HSA-936381 Reactome:R-HSA-933539 Reactome:R-HSA-933538 Reactome:R-HSA-933537 Reactome:R-HSA-933532 Reactome:R-HSA-933530 Reactome:R-HSA-933527 Reactome:R-HSA-933526 Reactome:R-HSA-933525 Reactome:R-HSA-933523 Reactome:R-HSA-918232 Reactome:R-HSA-918230 Reactome:R-HSA-918229 Reactome:R-HSA-918227 Reactome:R-HSA-918225 Reactome:R-HSA-918224 Reactome:R-HSA-8985153 Reactome:R-HSA-5696600 Reactome:R-HSA-5696564 Reactome:R-HSA-5690159 Reactome:R-HSA-168935 Reactome:R-HSA-168934 Reactome:R-HSA-168909	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0399	P		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003	C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F		Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
part_of	GO:0005923	bicellular tight junction	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0796 UniProtKB-SubCell:SL-0265	C		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0051	P		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0301	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Schoggins, JW et al. (2011) A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472 481-5 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Zhang, Z et al. (2011) DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells. J. Immunol. 187 4501-8 PubMed GONUTS page
↑ Hao, Q et al. (2015) A non-canonical role of the p97 complex in RIG-I antiviral signaling. EMBO J. 34 2903-20 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 Sathe, A & Reddy, KV (2014) TLR9 and RIG-I signaling in human endocervical epithelial cells modulates inflammatory responses of macrophages and dendritic cells in vitro. PLoS ONE 9 e83882 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 Mibayashi, M et al. (2007) Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J. Virol. 81 514-24 PubMed GONUTS page
↑ ^6.0 ^6.1 Chiu, YH et al. (2009) RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell 138 576-91 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Ablasser, A et al. (2009) RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat. Immunol. 10 1065-72 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Bamming, D & Horvath, CM (2009) Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J. Biol. Chem. 284 9700-12 PubMed GONUTS page
↑ ^9.0 ^9.1 Schlee, M et al. (2009) Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity 31 25-34 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Mukherjee, A et al. (2009) Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions. J. Biol. Chem. 284 6486-94 PubMed GONUTS page
↑ Cui, S et al. (2008) The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of RIG-I. Mol. Cell 29 169-79 PubMed GONUTS page
↑ ^12.0 ^12.1 Hayakawa, S et al. (2011) ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses. Nat. Immunol. 12 37-44 PubMed GONUTS page
↑ Peisley, A et al. (2014) Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature 509 110-4 PubMed GONUTS page
↑ Wang, Y et al. (2010) Structural and functional insights into 5'-ppp RNA pattern recognition by the innate immune receptor RIG-I. Nat. Struct. Mol. Biol. 17 781-7 PubMed GONUTS page
↑ Saito, T et al. (2007) Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. Proc. Natl. Acad. Sci. U.S.A. 104 582-7 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Loo, YM & Gale, M Jr (2011) Immune signaling by RIG-I-like receptors. Immunity 34 680-92 PubMed GONUTS page

[PMID:21478870-1] Schoggins, JW et al. (2011) A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472 481-5 PubMed GONUTS page

[PMID:21957149-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Zhang, Z et al. (2011) DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells. J. Immunol. 187 4501-8 PubMed GONUTS page

[PMID:26471729-3] Hao, Q et al. (2015) A non-canonical role of the p97 complex in RIG-I antiviral signaling. EMBO J. 34 2903-20 PubMed GONUTS page

[PMID:24409285-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 Sathe, A & Reddy, KV (2014) TLR9 and RIG-I signaling in human endocervical epithelial cells modulates inflammatory responses of macrophages and dendritic cells in vitro. PLoS ONE 9 e83882 PubMed GONUTS page

[PMID:17079289-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 Mibayashi, M et al. (2007) Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J. Virol. 81 514-24 PubMed GONUTS page

[PMID:19631370-6] 6.0 ^6.1 Chiu, YH et al. (2009) RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell 138 576-91 PubMed GONUTS page

[PMID:19609254-7] 7.0 ^7.1 ^7.2 ^7.3 Ablasser, A et al. (2009) RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat. Immunol. 10 1065-72 PubMed GONUTS page

[PMID:19211564-8] 8.0 ^8.1 ^8.2 ^8.3 Bamming, D & Horvath, CM (2009) Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J. Biol. Chem. 284 9700-12 PubMed GONUTS page

[PMID:19576794-9] 9.0 ^9.1 Schlee, M et al. (2009) Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity 31 25-34 PubMed GONUTS page

[PMID:19122199-10] 10.0 ^10.1 ^10.2 ^10.3 Mukherjee, A et al. (2009) Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions. J. Biol. Chem. 284 6486-94 PubMed GONUTS page

[PMID:18243112-11] Cui, S et al. (2008) The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of RIG-I. Mol. Cell 29 169-79 PubMed GONUTS page

[PMID:21102435-12] 12.0 ^12.1 Hayakawa, S et al. (2011) ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses. Nat. Immunol. 12 37-44 PubMed GONUTS page

[PMID:24590070-13] Peisley, A et al. (2014) Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature 509 110-4 PubMed GONUTS page

[PMID:20581823-14] Wang, Y et al. (2010) Structural and functional insights into 5'-ppp RNA pattern recognition by the innate immune receptor RIG-I. Nat. Struct. Mol. Biol. 17 781-7 PubMed GONUTS page

[PMID:17190814-15] Saito, T et al. (2007) Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. Proc. Natl. Acad. Sci. U.S.A. 104 582-7 PubMed GONUTS page

[PMID:21616437-16] 16.0 ^16.1 ^16.2 Loo, YM & Gale, M Jr (2011) Immune signaling by RIG-I-like receptors. Immunity 34 680-92 PubMed GONUTS page

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HUMAN:DDX58

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