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RIPK1 inhibits the transcriptional activity of VDR.
Results show that downregulation of RIP1 results in increased resistance to SN38, implying a requirement for RIP1 in mediating cytotoxicity through the TNF (show TNF ELISA Kits)/TNFR (show TNFRSF1A ELISA Kits) signaling pathway.
Renal clear cell carcinoma cells cells express increased amounts of RIPK1 and RIPK3 (show RIPK3 ELISA Kits) and are poised to undergo necroptosis in response to TNFR1 (show TNFRSF1A ELISA Kits) signaling.
Data suggest that pro-death signals through TIR-domain-containing adapter-inducing interferon-beta (show IFNB1 ELISA Kits) (TRIF (show TRIM69 ELISA Kits)) are regulated by autophagy and propose that pro-apoptotic signalling through TRIF (show TRIM69 ELISA Kits)/RIPK1/caspase-8 (show CASP8 ELISA Kits) occurs in fibrillary platforms.
UL45 promoted the UL48-RIP1 interaction and re-localization of RIP1 to the UL48-containing virion assembly complex.
we provide evidence that p62 (show GTF2H1 ELISA Kits) is implicated in the activation of NF-kappaB (show NFKB1 ELISA Kits) signaling that is partly dependent on RIP1
inactivation of RIP1/RIP3 (show RIPK3 ELISA Kits) resulted in reduction of SOCS1 (show SOCS1 ELISA Kits) protein levels and partial differentiation of AML (show RUNX1 ELISA Kits) cells. AML (show RUNX1 ELISA Kits) cells with inactivated RIP1/RIP3 (show RIPK3 ELISA Kits) signaling show increased sensitivity to IFN-gamma-induced (show SAMHD1 ELISA Kits) differentiation.
Data show that pan-caspase (show CASP3 ELISA Kits) inhibitors facilitated 5-fluorouracil (5-FU)-induced necroptosis mediated by secretion of tumor necrosis factor alpha (TNF-alpha (show TNF ELISA Kits)) driven by nuclear factor kappaB (NF-kappaB (show NFKB1 ELISA Kits)) and required RIP1 kinase.
RIPK1 kinase activity is a pertinent therapeutic target to protect liver against excessive cell death in liver diseases.
Ripk1 is directly involved in apoptosis/necroptosis. In osteosarcoma cells( OS) , small interfering RNA against Ripk1 prevented cell death induced by the sequestration of miR (show MLXIP ELISA Kits)-155-5p. Collectively, we show that miR (show MLXIP ELISA Kits)-148a-3p and miR (show MLXIP ELISA Kits)-155-5p are species-conserved deregulated miRNA in OS
p38MAPK (show MAPK14 ELISA Kits)/MK2 (show KCNA2 ELISA Kits) phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.
MK2 (show KCNA2 ELISA Kits)-mediated RIPK1 phosphorylation is an important molecular mechanism limiting the sensitivity of the cells to the cytotoxic effects of TNF (show TNF ELISA Kits).
An alternative function for RIPK1/RIPK3 (show RIPK3 ELISA Kits) in vascular permeability.
these results revealed a novel, kinase-independent function of RIP1, which is essential for not only promoting TCR-induced proliferative responses but also in blocking apoptosis in mature T cells.
Data show that the kinase domain of RIPK1 is a disease driver of intracerebral hemorrhage, mediating both acute cell death and functional outcome.
MK2 (show KCNA2 ELISA Kits)-mediated phosphorylation of RIPK1 serves as a checkpoint within the TNF (show TNF ELISA Kits) signaling pathway that integrates cell survival and cytokine production.
study identifies a novel role for RIPK1 and RIPK3 (show RIPK3 ELISA Kits), a pair of homologous serine/threonine kinases previously implicated in the regulation of necroptosis and pathologic tissue injury, in directing IFN-beta (show IFNB1 ELISA Kits) production in macrophagesges.
this study shows that RIPK1 and RIPK3 (show RIPK3 ELISA Kits) account for acute inflammatory responses induced by lipopolysaccharide in vivo; notably, this regulation does not require exogenous manipulation of caspases
these findings indicate that RIPK1 cooperates with NF-kappaB (show NFKB1 ELISA Kits) signaling to prevent TNFR1 (show TNFRSF1A ELISA Kits)-independent hepatocyte apoptosis and the development of chronic liver disease and cancer, but acts downstream of TNFR1 (show TNFRSF1A ELISA Kits) signaling to promote diethylnitrosamine-induced liver tumorigenesis.
this study reveals a critical kinase-independent platform role for RIPK1 in protecting against TNF (show TNF ELISA Kits)/caspase (show CASP3 ELISA Kits)-dependent apoptosis of hepatocytes in immune-mediated liver injury
Serine-threonine kinase which transduces inflammatory and cell-death signals (necroptosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necroptosis-inducing complex.
receptor (TNFRSF)-interacting serine-threonine kinase 1
, 1,3,4,5,6-pentakisphosphate 2-kinase
, inositol polyphosphate kinase 1
, inositol-1,3,4,5,6-pentakisphosphate 2-kinase
, inositol-pentakisphosphate 2-kinase
, ins(1,3,4,5,6)P5 2-kinase
, insP5 2-kinase
, cell death protein RIP
, receptor interacting protein
, receptor-interacting protein 1
, receptor-interacting serine/threonine-protein kinase 1
, serine/threonine-protein kinase RIP
, RPA interacting protein delta 2
, RPA interacting protein epsilon
, RPA-interacting protein