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our data demonstrate the protective role of RIPK1 downstream of Fas and highlight the general protective function of RIPK1 in hepatocytes exposed to inflammatory conditions, where TNF-alpha, FasL and/or TRAIL are present.
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This study showed that RIP1 was highly expressed in DRG, SC and HIP of the sciatic nerve in CCI mice and may be involved in chronic neuroinflammation and neuronecrosis.
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It has been proposed that ABIN-1 provides a critical link between methionine1 ubiquitylation mediated by the LUBAC complex and lysine63 deubiquitylation by phospho-A20 to modulate the activation of RIPK1.
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Receptor-Interacting Protein Kinases 1 and 3, and Mixed Lineage Kinase Domain-Like Protein Are Activated by Sublytic Complement and Participate in Complement-Dependent Cytotoxicity.
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Differentiation of macrophages increased the expression of pro-inflammatory cytokines but reduced RipK1-dependent cell death and the RipK3-caspase-8 interaction. The expression of the anti-apoptotic mediators, X-linked inhibitor of apoptosis protein (XIAP) and caspase-like apoptosis regulatory protein (cFLIPL), also increased in differentiated macrophages, which inhibited caspase activation.
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necroptosis contributes to ischemic brain injury induced by oxygen-glucose deprivation and middle cerebral artery occlusion and implicate HIF-1alpha, RIP1, RIP3, and MLKL in necroptosis.
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miR-155 up-regulation in macrophages by Salmonella infection causes macrophage death and it may be mediated by both RIP1/3-related necroptosis and PARP-1-mediated necrosis.
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Ischemia induces an up-regulation of RIP1K and an enhancement of RIP1K-RIP3K complex formation in neurons and astrocytes. Inhibition of RIP1K increases ischemia-induced reduction in MAP2 or GFAP and decreases ischemia-induced neuronal or astrocytic cell necrosis in the ischemic cortex, and directly protects OGD-induced neuronal or astrocytic cell death. Nec-1 blocks RIP1K-RIP3K complex formation.
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Aldehyde dehydrogenase 2 deficiency negates chronic low-to-moderate alcohol consumption-induced cardioprotecion possibly via ROS-dependent apoptosis and RIP1/RIP3/MLKL-mediated necroptosis.
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The major function of RIP1 kinase activity in TNF-induced necroptosis is to autophosphorylate serine 161. This specific phosphorylation then enables RIP1 to recruit RIP3 and form a functional necrosome, a central controller of necroptosis.
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Elevated A20 promotes TNF-induced and RIPK1-dependent intestinal epithelial cell death
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two different modes of necroptosis induction by TNFalpha exist which are differentially regulated by iuRIPK1 formation. Overall, this work reveals a distinct mechanism of RIPK1 activation that mediates the signaling mechanism of RDA as well as a type of necroptosis.
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We show that inflammation and autoimmunity are prevented upon expression of kinase inactive RIPK1 or deletion of RIPK3 or MLKL. We provide evidence that the inflammation is not driven by microbial ligands, but depends on the release of danger-associated molecular patterns and MyD88-dependent signaling.
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RIPK1 kinase activity mediates TWEAK-induced apoptosis.
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RIPK1-DD has a role in mediating RIPK1 dimerization and activation of its kinase activity during necroptosis and RIPK1-dependent apoptosis
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High RIPK1 expression is associated with Alzheimer's disease.
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The authors report here that male reproductive organs of both Ripk3- and Mlkl-knockout mice retain 'youthful' morphology and function into advanced age, while those of age-matched wild-type mice deteriorate. Feeding of wild-type mice with an RIPK1 inhibitor prior to the normal onset of age-related changes in their reproductive organs blocked the appearance of signs of aging.
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Pull down experiments with biotinylated Sorafenib show that it binds independently RIPK1, RIPK3 and MLKL. Moreover, it inhibits RIPK1 and RIPK3 kinase activity. In vivo Sorafenib protects against TNF-induced systemic inflammatory response syndrome (SIRS) and renal ischemia-reperfusion injury (IRI).
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The study provides genetic evidence that different RIP1 kinase inactive mutations have distinct impacts on the embryogenesis of Fadd-deficient mice.
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Excessive death of hepatocytes is a characteristic of liver injury. A new programmed cell death pathway has been described involving upstream death ligands such as TNF and downstream kinases such as RIPK1.
