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Human DDX58 Protein expressed in HEK-293 Cells - ABIN2719304
Zhao, Tian, Edeh, Brasier: Quantitation of the dynamic profiles of the innate immune response using multiplex selected reaction monitoring-mass spectrometry. in Molecular & cellular proteomics : MCP 2013
These findings demonstrate how IFNgamma induced CK2 (show CSNK2A1 Proteins) regulates RIG-I to drive a complex program of metabolic adaptation and redox homeostasis, crucial for determining glioma cell fate.
IFNgamma induced PPAR gamma coactivator-1 alpha (PGC-1alpha) positively regulated RIG-I; with PRMT-1 and G9a affecting PGC-1alpha in a counter-regulatory manner.
Data show that host-derived RNAs, most prominently 5S ribosomal RNA pseudogene 141 (RNA5SP141), bound to RIG-I during infection with herpes simplex virus 1 (HSV-1).
RIG-I expression is markedly increased in the affected skin derived from psoriasis patients and from both IL-23 (show IL23A Proteins)- and imiquimod -induced psoriasis-like mouse model.
DDX58 was confirmed to be the downstream target of TRIM24 (show TRIM24 Proteins), whose downregulation is essential for the migratory phenotype induced by GLUT4 (show SLC2A4 Proteins)-TRIM24 (show TRIM24 Proteins) activation in head and neck squamous cell carcinoma cells.
TRIM25 (show TRIM25 Proteins) actively participates in higher-order assembly of the RIG-I signalosome.
This study evaluation the roles of SOCS1 (show SOCS1 Proteins), the regulator of TLR9 (show TLR9 Proteins), RIG-I, and CD152 (show CTLA4 Proteins) in patients with liver fibrosis/cirrhosis; the use of polymorphisms as markers for genetic risk is reported.
study documents that recombinant measles virus produce defective interfering genomes that have high immunostimulatory properties via their binding to RIG-I and LGP2 (show DHX58 Proteins) proteins, both of which are cytosolic nonself RNA sensors of innate immunity.
findings define the WHIP (show WRNIP1 Proteins)-TRIM14 (show TRIM14 Proteins)-PPP6C (show PPP6C Proteins) mitochondrial signalosome required for RIG-I-mediated innate antiviral immunity.
both IL-6 (show IL6 Proteins) and RIG-I are downstream molecules of STING along the DNA sensor pathway.
Toll-like receptor 2 (TLR2) and retinoic acid-inducible gene I (RIG-I) cooperatively initiate innate immune responses to MuV infection in mouse ovarian granulosa cells.
Collectively, these results uncover an independent functional contribution of the apo (show C9orf3 Proteins)-Rig-I/Stat3 (show STAT3 Proteins) interaction in the maintenance of Treg/Th17 cell balance.
The RIG-I, as well as the adaptor protein mitochondrial antiviral signaling protein (show MAVS Proteins), regulates NF-kappaB (show NFKB1 Proteins)-mediated induction of adhesion molecules and proinflammatory cytokine expression in response to LPS (show TLR4 Proteins).
Data suggest that activation of either RIG-I/MAVS (show MAVS Proteins) or STING pathways during acute intestinal tissue injury in mice resulted in IFN-I signaling that maintained gut (show GUSB Proteins) epithelial barrier integrity and reduced GVHD severity.
RIG-I subsequently localized to antiviral stress granules induced after viral replication complexes formation
identifies DDX58 and MTHFSD as two TDP-43 (show TARDBP Proteins) targets that are misregulated in amyotrophic lateral sclerosis. 1
Data show that preconditioning with poly(I:C) alters toll (show TLR4 Proteins)-like receptors (TLR) and RIG-I-like receptors (RLRs) responses in opposite directions.
Cytosolic LMW FGF2 (show FGF2 Proteins) functions as a negative regulator in RIG-I-mediated antiviral signaling.
results indicate that Lyn (show LYN Proteins) plays a positive regulatory role in RIG-I-mediated interferon (show IFNA Proteins) expression as a downstream component of IPS-1 (show ISYNA1 Proteins)
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 Proteins) to initiate the RIG-I signaling pathway to trigger innate defenses against infection.
DDX58 had two nonsynonymous SNPs in the helicase 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