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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
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.
Necroptosis signaling is modulated by the kinase RIPK1 and requires the kinase RIPK3 and the pseudokinase MLKL. (Review)
Data identify RIPK3 and the inflammasome as key tumor suppressors in acute myeloid leukemia (show BCL11A Proteins) (AML (show RUNX1 Proteins)).
Results suggest that impaired hepatic proteasome function by alcohol exposure may contribute to hepatic accumulation of RIP3 resulting in necroptosis and steatosis while RIP1 (show UQCRFS1 Proteins) kinase activity is important for alcohol-induced inflammation.
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.
robust caspase (show CASP3 Proteins) activation in NEMO (show IKBKG Proteins)-deficient cells is concomitant with RIPK3 recruitment to the apoptosis-mediating complex.
study identifies a novel role for RIPK1 (show RIPK1 Proteins) and RIPK3, a pair of homologous serine/threonine kinases previously implicated in the regulation of necroptosis and pathologic tissue injury, in directing IFN-beta (show IFNB1 Proteins) production in macrophages
this study shows that RIPK1 (show RIPK1 Proteins) and RIPK3 account for acute inflammatory responses induced by lipopolysaccharide in vivo; notably, this regulation does not require exogenous manipulation of caspases
RIPK3 and/or MLKL may exert functions independently of necroptosis.
These results identify DAI (show ZBP1 Proteins) as a link between influenza A virus replication and RIPK3 activation and implicate DAI (show ZBP1 Proteins) as a sensor of RNA viruses.
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