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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
We showed that RIP3 spontaneously drives a necroptosis-induced inflammation in established intestinal cell lines and in ileal/colonic samples from IBD patients.
These data demonstrate that caspase-8 (show CASP8 Proteins) functions in synovial antigen-presenting cells to regulate the response to inflammatory stimuli by controlling RIPK3 action, and this delicate balance maintains homeostasis within the joint.
The induced expression of RIP3 by UHRF1 (show UHRF1 Proteins) RNAi depends on the presence of Sp1 (show PSG1 Proteins). Remarkably, the ectopic expression of RIP3 in RIP3-null cancer cells results in a decrease in tumor growth in mice. Therefore, our findings offer insights into RIP3 expression control in cancer cells and suggest an inhibitory effect of RIP3 on tumorigenesis.
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.
RIP3-mediated signaling is not a critical driver of acute radiation syndrome
RIPK3 promotes adenovirus type 5 oncolytic activity.
p55TNFR-IKK2 (show IKBKB Proteins)-Ripk3 signalling orchestrates arthritogenic and death responses in synovial fibroblasts
in Mycobacterium tuberculosis-infected macrophages, mitochondria are an essential platform for induction of necrosis by activating RIPK3 function and preventing caspase 8 (show CASP8 Proteins)-activation.
Ripk3 promotes mitochondrial apoptosis via inhibition of FUNDC1 (show FUNDC1 Proteins) mitophagy in cardiac ischemia reperfusion injury.
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 (show RIPK1 Proteins) inhibitor prior to the normal onset of age-related changes in their reproductive organs blocked the appearance of signs of aging.
These data demonstrate a role for RIP3 in promoting in vivo thrombosis and hemostasis by amplifying platelet activation. RIP3 may represent a novel promising therapeutic target for thrombotic diseases.
these results demonstrated that RIPK3-mediated signaling in Tie-2 expressing cells was responsible for the embryonic lethality of Fadd-/- with cardiac failure.
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.
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