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Human RIPK3 Protein expressed in Wheat germ - ABIN1318116
Northington, Chavez-Valdez, Graham, Razdan, Gauda, Martin: Necrostatin decreases oxidative damage, inflammation, and injury after neonatal HI. in Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2011
2-hydroxyglutarate bound to DNMT1 (show DNMT1 Proteins) and stimulated its association with the RIP3 promoter, inducing hypermethylation that reduces RIP3 protein and consequently impaired RIP3-dependent necroptosis.
the in vivo effects were diametrically reversed with RIP3 deletion or RIP1 (show UQCRFS1 Proteins) blockade, resulting in marked tumor protection. The dichotomy between the in vivo and in vitro results suggests that the microenvironmental milieu resulting from RIP1 (show UQCRFS1 Proteins)/RIP3 signaling is likely responsible for its protumorigenic effects
Shikonin induces glioma cell necroptosis in vitro by reactive oxygen species overproduction and promoting RIP1 (show UQCRFS1 Proteins)/RIP3 necrosome formation.
In critically ill trauma patients, plasma levels of the necroptosis mediator RIP3 at 48 h were associated with AKI stage and RBC (show CACNA1C Proteins) transfusions.
our results reveal that the necroptosis adaptor RIPK3 has key anti-inflammatory and anti-tumoral functions in the intestine, and define RIPK3 as a novel colon tumor suppressor
adhesion-induced eosinophil cytolysis takes place through RIPK3-MLKL-dependent necroptosis, which can be counterregulated by autophagy
Renal clear cell carcinoma cells cells express increased amounts of RIPK1 (show RIPK1 Proteins) and RIPK3 and are poised to undergo necroptosis in response to TNFR1 (show TNFRSF1A Proteins) signaling.
The results highlight a new role of TSC2 in protecting glioblastoma against photodynamic therapy-induced cell death, and TSC2 and YWHAZ (show YWHAZ Proteins) as new RIP3 partners.
inactivation of RIP1 (show UQCRFS1 Proteins)/RIP3 resulted in reduction of SOCS1 (show SOCS1 Proteins) protein levels and partial differentiation of AML (show RUNX1 Proteins) cells. AML (show RUNX1 Proteins) cells with inactivated RIP1 (show UQCRFS1 Proteins)/RIP3 signaling show increased sensitivity to IFN-gamma-induced (show SAMHD1 Proteins) differentiation.
results reveal a pathway for MLKL-dependent programmed necrosis that is executed in the absence of RIPK3 and potentially drives the pathogenesis of severe liver diseases.
Pull down experiments with biotinylated Sorafenib show that it binds independently RIPK1 (show RIPK1 Proteins), RIPK3 and MLKL. Moreover, it inhibits RIPK1 (show RIPK1 Proteins) and RIPK3 kinase activity. In vivo Sorafenib protects against TNF (show TNF Proteins)-induced systemic inflammatory response syndrome (SIRS) and renal ischemia-reperfusion injury (IRI).
RIP3-mediated activation of caspase-1 (show CASP1 Proteins) rather than necroptosis-dependent inflammation was responsible for aggressive inflammation in influenza A (H7N9) virus-infected mice.
we assessed the role of RIP3 in synergy with Caspase-1 (show CASP1 Proteins) in the induction of IL-1beta (show IL1B Proteins) production in BMDM after either LPS (show TLR4 Proteins)/ATP or Chlamydia muridarum stimulation. The possibility of pyroptosis and necroptosis interplays and the role of RIP3 in IL-1beta (show IL1B Proteins) production during Chlamydia muridarum infection in BMDM was investigated as well.
Knock-out mice deficient in MLKL or RIP3 had increased survival and reduced pulmonary injury during Serratia marcescens pneumonia.
Ablation of Ripk3 rescues Fadd (show FADD Proteins)-deficient mice through two processes: inhibiting necroptosis during embryonic development and restricting massive inflammation during postnatal development, which were segregated by the RIPK3 mutation.
Impaired Nrf2 (show NFE2L2 Proteins)-dependent redox homeostasis is an important mechanism that promotes cell death downstream of IFN-I and RIP3 signaling in S. Typhimurium-infected macrophages.
a key physiological function of RIPK3 is to promote reparative cytokine expression through intestinal CD11c (show ITGAX Proteins)(+) mononuclear phagocytes in a kinase- and necroptosis-independent manner.
An alternative function for RIPK1 (show RIPK1 Proteins)/RIPK3 in vascular permeability.
The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor.
receptor-interacting serine-threonine kinase 3
, receptor-interacting serine/threonine-protein kinase 3-like
, RIP-like protein kinase 3
, receptor interacting protein 3
, receptor-interacting protein 3
, receptor-interacting serine/threonine-protein kinase 3
, homocysteine respondent protein HCYP2