anti-DDX58 (DDX58) Antikörper

Human DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 58 (DDX58) Interaktionspartner

1. FBXW7 (zeige FBXW7 Antikörper) is critical for RIG-I stabilization during antiviral responses.

2. These findings imply a novel function for DDX6 (zeige DDX6 Antikörper) as an RNA co-sensor and signaling enhancer for RIG-I.

3. Identification of a second binding site on the RIG-I TRIM25 (zeige TRIM25 Antikörper) B30.2 domain has been reported.

4. Aging thus compromises both the primary and secondary RIG-I signaling pathways that govern expression of type I IFN genes, thereby impairing antiviral resistance to IAV.

5. RIG-I-like receptors have a role in induction of interferon-beta1 in antiviral gene expression

6. MCCC1 (zeige MCCC1 Antikörper) plays an essential role in virus-triggered, MAVS (zeige MAVS Antikörper)-mediated activation of NF-kappaB (zeige NFKB1 Antikörper) signaling.

7. The authors find that KHSRP (zeige KHSRP Antikörper) associates with the regulatory domain of RIG-I to maintain the receptor in an inactive state and attenuate its sensing of viral RNA (vRNA).

8. In this study, the authors determined that, in contrast to the RIG-I CARD domain, full-length RIG-I must undergo K63-linked ubiquitination at multiple sites to reach full activity.

9. RIG-1 (zeige RARRES3 Antikörper) overexpression is protective for cigarette smoke exposure enhanced susceptibility to influenza infection.

10. These results showed that the knockdown of RIGI reduced the inhibition of cell proliferation, cell cycle arrest and apoptosis in the alltrans retinoic acid induced NB4 acute promyelocytic leukemia (zeige PML Antikörper) cells via the AKTFOXO3A signaling pathway.

Mouse (Murine) DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 58 (DDX58) Interaktionspartner

1. FBXW7 (zeige FBXW7 Antikörper) is critical for RIG-I stabilization during antiviral responses.

2. Identification of a second binding site on the RIG-I TRIM25 (zeige TRIM25 Antikörper) B30.2 domain has been reported.

3. Elevated retinoic acid-inducible gene 1 (zeige RARRES3 Antikörper) (RIG-I) modulated the interaction of activated proto-oncogene c-Src (Src (zeige SRC Antikörper)) and STAT3 (zeige STAT3 Antikörper) by competitive binding to STAT3 (zeige STAT3 Antikörper).

4. RNF122 (zeige RNF122 Antikörper) suppresses antiviral type I interferon production by targeting RIG-I caspase (zeige CASP3 Antikörper) activation and recruitment domains to mediate RIG-I degradation.

5. innate immune signaling mediated by RLR (zeige DHX58 Antikörper) plays a critical role in nuclear reprogramming.

6. RIG-I expression is markedly increased in the affected skin derived from psoriasis patients and from both IL-23 (zeige IL23A Antikörper)- and imiquimod -induced psoriasis-like mouse model.

7. 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.

8. Collectively, these results uncover an independent functional contribution of the apo (zeige C9orf3 Antikörper)-Rig-I/Stat3 (zeige STAT3 Antikörper) interaction in the maintenance of Treg/Th17 cell balance.

9. The RIG-I, as well as the adaptor protein mitochondrial antiviral signaling protein (zeige MAVS Antikörper), regulates NF-kappaB (zeige NFKB1 Antikörper)-mediated induction of adhesion molecules and proinflammatory cytokine expression in response to LPS (zeige TLR4 Antikörper).

10. Data suggest that activation of either RIG-I/MAVS (zeige MAVS Antikörper) or STING pathways during acute intestinal tissue injury in mice resulted in IFN-I signaling that maintained gut (zeige GUSB Antikörper) epithelial barrier integrity and reduced GVHD severity.

Pig (Porcine) DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 58 (DDX58) Interaktionspartner

1. Key regulators involved in Porcine circovirus 2 infection were identified as IFNbeta, DDX58 (RIG-I), and IRF7 (zeige IRF7 Antikörper).

2. RIG-I and TLR3 interact with the pseudoknot of Porcine Reproductive and Respiratory Syndrome Virus 3' untranslated regions. Both RIG-I and TLR3 are required for the pseudoknot to induce interferon response.

3. Viral RNA polymerase components PB2, PB1, and PA directly target RIG-I.

4. These data indicate that classical swine fever virus can be recognized by both RIG-I and MDA5 (zeige IFIH1 Antikörper) to initiate the RIG-I signaling pathway to trigger innate defenses against infection.

5. DDX58 had two nonsynonymous SNPs in the helicase (zeige DNA2 Antikörper) domain.