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RIPK1 inhibits the transcriptional activity of VDR.
Results show that downregulation of RIP1 (zeige UQCRFS1 Proteine) results in increased resistance to SN38, implying a requirement for RIP1 (zeige UQCRFS1 Proteine) in mediating cytotoxicity through the TNF (zeige TNF Proteine)/TNFR (zeige TNFRSF1A Proteine) signaling pathway.
Renal clear cell carcinoma cells cells express increased amounts of RIPK1 and RIPK3 (zeige RIPK3 Proteine) and are poised to undergo necroptosis in response to TNFR1 (zeige TNFRSF1A Proteine) signaling.
Data suggest that pro-death signals through TIR-domain-containing adapter-inducing interferon-beta (zeige IFNB1 Proteine) (TRIF (zeige TRIM69 Proteine)) are regulated by autophagy and propose that pro-apoptotic signalling through TRIF (zeige TRIM69 Proteine)/RIPK1/caspase-8 (zeige CASP8 Proteine) occurs in fibrillary platforms.
UL45 promoted the UL48-RIP1 (zeige UQCRFS1 Proteine) interaction and re-localization of RIP1 (zeige UQCRFS1 Proteine) to the UL48-containing virion assembly complex.
we provide evidence that p62 (zeige GTF2H1 Proteine) is implicated in the activation of NF-kappaB (zeige NFKB1 Proteine) signaling that is partly dependent on RIP1 (zeige UQCRFS1 Proteine)
inactivation of RIP1 (zeige UQCRFS1 Proteine)/RIP3 (zeige RIPK3 Proteine) resulted in reduction of SOCS1 (zeige SOCS1 Proteine) protein levels and partial differentiation of AML (zeige RUNX1 Proteine) cells. AML (zeige RUNX1 Proteine) cells with inactivated RIP1 (zeige UQCRFS1 Proteine)/RIP3 (zeige RIPK3 Proteine) signaling show increased sensitivity to IFN-gamma-induced (zeige SAMHD1 Proteine) differentiation.
Data show that pan-caspase (zeige CASP3 Proteine) inhibitors facilitated 5-fluorouracil (5-FU)-induced necroptosis mediated by secretion of tumor necrosis factor alpha (TNF-alpha (zeige TNF Proteine)) driven by nuclear factor kappaB (NF-kappaB (zeige NFKB1 Proteine)) and required RIP1 (zeige UQCRFS1 Proteine) 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 (zeige MLXIP Proteine)-155-5p. Collectively, we show that miR (zeige MLXIP Proteine)-148a-3p and miR (zeige MLXIP Proteine)-155-5p are species-conserved deregulated miRNA in OS
K45 mediated kinase activity of RIPK1 is not only important for necroptosis but it also has a key role in promoting cytokine signaling and host response to inflammatory stimuli.
Data show that the kinase activity of receptor-interacting protein kinase (zeige CDK7 Proteine) 1 (RIPK1) is required for Yersinia-induced apoptosis.
p38MAPK (zeige MAPK14 Proteine)/MK2 (zeige KCNA2 Proteine) phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.
MK2 (zeige KCNA2 Proteine)-mediated RIPK1 phosphorylation is an important molecular mechanism limiting the sensitivity of the cells to the cytotoxic effects of TNF (zeige TNF Proteine).
An alternative function for RIPK1/RIPK3 (zeige RIPK3 Proteine) 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 (zeige KCNA2 Proteine)-mediated phosphorylation of RIPK1 serves as a checkpoint within the TNF (zeige TNF Proteine) signaling pathway that integrates cell survival and cytokine production.
study identifies a novel role for RIPK1 and RIPK3 (zeige RIPK3 Proteine), a pair of homologous serine/threonine kinases previously implicated in the regulation of necroptosis and pathologic tissue injury, in directing IFN-beta (zeige IFNB1 Proteine) production in macrophagesges.
this study shows that RIPK1 and RIPK3 (zeige RIPK3 Proteine) account for acute inflammatory responses induced by lipopolysaccharide in vivo; notably, this regulation does not require exogenous manipulation of caspases
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