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DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. Additionally we are shipping DDX58 Proteins (9) and DDX58 Kits (8) and many more products for this protein.
Showing 10 out of 172 products:
Human Polyclonal DDX58 Primary Antibody for WB - ABIN388602
Bao, Liu, Shan, Li, Garofalo, Casola: Human metapneumovirus glycoprotein G inhibits innate immune responses. in PLoS pathogens 2008
Show all 9 references for ABIN388602
Human Monoclonal DDX58 Primary Antibody for FACS - ABIN2664928
Kolakofsky, Kowalinski, Cusack: A structure-based model of RIG-I activation. in RNA (New York, N.Y.) 2012
Show all 6 references for ABIN2664928
Human Polyclonal DDX58 Primary Antibody for EIA, WB - ABIN357195
Li, Chen, Kato, Gale, Lemon: Distinct poly(I-C) and virus-activated signaling pathways leading to interferon-beta production in hepatocytes. in The Journal of biological chemistry 2005
Show all 5 references for ABIN357195
Human Polyclonal DDX58 Primary Antibody for EIA, WB - ABIN357193
Breiman, Grandvaux, Lin, Ottone, Akira, Yoneyama, Fujita, Hiscott, Meurs: Inhibition of RIG-I-dependent signaling to the interferon pathway during hepatitis C virus expression and restoration of signaling by IKKepsilon. in Journal of virology 2005
Show all 5 references for ABIN357193
Human Monoclonal DDX58 Primary Antibody for IP, IHC - ABIN1169336
Gack, Nistal-Villán, Inn, García-Sastre, Jung: Phosphorylation-mediated negative regulation of RIG-I antiviral activity. in Journal of virology 2010
Show all 4 references for ABIN1169336
Human Polyclonal DDX58 Primary Antibody for EIA, IHC (p) - ABIN500606
Akira, Uematsu, Takeuchi: Pathogen recognition and innate immunity. in Cell 2006
Human Polyclonal DDX58 Primary Antibody for WB - ABIN2775222
Miyazaki, Kanto, Inoue, Itose, Miyatake, Sakakibara, Yakushijin, Kakita, Hiramatsu, Takehara, Kasahara, Hayashi: Impaired cytokine response in myeloid dendritic cells in chronic hepatitis C virus infection regardless of enhanced expression of Toll-like receptors and retinoic acid inducible gene-I. in Journal of medical virology 2008
Study demonstrates how the coordinated interplay of RIG-I, TRIM25 (show TRIM25 Antibodies), and FAT10 (show UBD Antibodies) regulate the antiviral innate inflammatory response.
Pyruvate carboxylase (show PC Antibodies) activates the RIG-I-like receptor-mediated antiviral immune response by targeting the MAVS (show MAVS Antibodies) signalosome.
This study shows that RIG-I activation results in MKP-1 (show DUSP1 Antibodies)-mediated inhibition of cell proliferation in melanoma cells via controlling the p38 (show CRK Antibodies)-HSP27 (show HSPB1 Antibodies), c-Jun (show JUN Antibodies) and rpS6 (show RPS6 Antibodies) pathways
HepaRG cells express a similar pattern of functional TLR/RLR (show DHX58 Antibodies) as compared to PHH, thus qualifying HepaRG cells as a surrogate model to study pathogen interactions within a hepatocyte innate system.
COPD (show ARCN1 Antibodies) patients had higher interleukin (IL)-1 (show IL1A Antibodies) and IL-8 (show IL8 Antibodies) mRNA expression levels, and these inflammatory cytokines positively correlate with MDA-5 (show IFIH1 Antibodies) levels. However, there was no difference in the expression of RIG-I between COPD (show ARCN1 Antibodies) patients and control subjects.
In cell culture, Marburg virus infection results in a greater upregulation of IFN responses as compared to Ebolavirus infection, which correlates with differences in the efficiencies by which EBOV and MARV VP35s antagonize RIG-I signaling.
These findings collectively support the conclusion that IKK (show CHUK Antibodies) modulates innate immune signaling cascades via phosphorylating the RIG-I cytosolic sensor, providing a feedback regulatory mechanism.
ATP hydrolysis displaces wild-type RIG-I from this self-RNA but not from 5' triphosphate dsRNA.
that miR-4516 mediated down-regulation of UBE2N promotes p53 nuclear translocation and pro-apoptotic activity of PUVA is independent of IRF3 but is mediated by the RIG-I in a p53 and NFkappaB dependent manner
Data show that the NS3 protein of dengue virus bound to 14-3-3 epsilon protein (14-3-3varepsilon) and prevented translocation of retinoic acid-inducible gene-I protein (RIG-I) to the adaptor MAVS (show MAVS Antibodies) protein and thereby blocked antiviral signaling.
RIG-I subsequently localized to antiviral stress granules induced after viral replication complexes formation
identifies DDX58 and MTHFSD as two TDP-43 (show TARDBP Antibodies) targets that are misregulated in amyotrophic lateral sclerosis. 1
Data show that preconditioning with poly(I:C) alters toll (show TLR4 Antibodies)-like receptors (TLR) and RIG-I-like receptors (RLRs) responses in opposite directions.
Cytosolic LMW FGF2 (show FGF2 Antibodies) functions as a negative regulator in RIG-I-mediated antiviral signaling.
results indicate that Lyn (show LYN Antibodies) plays a positive regulatory role in RIG-I-mediated interferon (show IFNA Antibodies) expression as a downstream component of IPS-1 (show ISYNA1 Antibodies)
In lung epithelial cells, retinoic acid-inducible gene-1 (show RARRES3 Antibodies) (RIG-I) was identified as the major RIG-I-like receptor required for RSV-induced protease expression via MAVS (show MAVS Antibodies).
findings suggest that RIG-I directs a typical IFN-dependent antiviral response against an RNA virus capable of suppressing the RNAi response
The results describe a novel, interactive relationship between RIG-I downstream signalling molecules resulting in efficient anti-viral immunity.
senses hepatitis B virus RNA, and counteracts HBV polymerase
RIG-I-like receptor (RLR (show DHX58 Antibodies)) signaling pathway was significantly affected by Yersinia pestis infection
Viral RNA polymerase components PB2, PB1, and PA directly target RIG-I.
These data indicate that classical swine fever virus can be recognized by both RIG-I and MDA5 (show IFIH1 Antibodies) to initiate the RIG-I signaling pathway to trigger innate defenses against infection.
DDX58 had two nonsynonymous SNPs in the helicase (show DNA2 Antibodies) domain.
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. This gene encodes a protein containing RNA helicase-DEAD box protein motifs and a caspase recruitment domain (CARD). It is involved in viral double-stranded (ds) RNA recognition and the regulation of immune response.
DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide RIG-I
, probable ATP-dependent RNA helicase DDX58
, putative ATP-dependent RNA helicase DDX58
, retinoic acid-inducible protein I
, DEAD (Asp-Glu-Ala-Asp) box polypeptide 58
, probable ATP-dependent RNA helicase DDX58-like
, DEAD box protein 58
, DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide
, RIG-I-like receptor 1
, RNA helicase RIG-I
, retinoic acid inducible gene I
, retinoic acid-inducible gene 1 protein
, retinoic acid-inducible gene I protein
, DEAD-box protein 58
, DEAD/H box polypeptide RIG-I
, retinoic acid-inducible gene-I
, RNA helicase induced by virus