Receptor-Interacting Protein Serine-Threonine Kinases
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Subject Areas on Research
- A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.
- A RNA interference screen identifies RIP3 as an essential inducer of TNF-induced programmed necrosis.
- A role for c-FLIP(L) in the regulation of apoptosis, autophagy, and necroptosis in T lymphocytes.
- A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses.
- An Islet-Targeted Genome-Wide Association Scan Identifies Novel Genes Implicated in Cytokine-Mediated Islet Stress in Type 2 Diabetes.
- CYLD deubiquitinates RIP1 in the TNFα-induced necrosome to facilitate kinase activation and programmed necrosis.
- Ca2+-dependent demethylation of phosphatase PP2Ac promotes glucose deprivation-induced cell death independently of inhibiting glycolysis.
- Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death.
- Cell biology. RIPK3 takes another deadly turn.
- Cell biology: A guardian angel of cell integrity.
- Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury.
- Cutting edge: RIPK1 Kinase inactive mice are viable and protected from TNF-induced necroptosis in vivo.
- Differential roles of RIPK1 and RIPK3 in TNF-induced necroptosis and chemotherapeutic agent-induced cell death.
- Distinct Kinase-Independent Role of RIPK3 in CD11c+ Mononuclear Phagocytes in Cytokine-Induced Tissue Repair.
- Fueling the flames: Mammalian programmed necrosis in inflammatory diseases.
- Heme induces programmed necrosis on macrophages through autocrine TNF and ROS production.
- Key roles of necroptotic factors in promoting tumor growth.
- MLKL Requires the Inositol Phosphate Code to Execute Necroptosis.
- Mice Lacking RIP3 Kinase are not Protected from Acute Radiation Syndrome.
- Necroptosis-independent signaling by the RIP kinases in inflammation.
- Necroptosis: Mechanisms and Relevance to Disease.
- Necrosis-dependent and independent signaling of the RIP kinases in inflammation.
- Peptidoglycan-Sensing Receptors Trigger the Formation of Functional Amyloids of the Adaptor Protein Imd to Initiate Drosophila NF-κB Signaling.
- Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation.
- Positive and negative phosphorylation regulates RIP1- and RIP3-induced programmed necrosis.
- Programmed necrosis in the cross talk of cell death and inflammation.
- RIP1-dependent and independent effects of necrostatin-1 in necrosis and T cell activation.
- RIP3 induces apoptosis independent of pronecrotic kinase activity.
- RIP3: a molecular switch for necrosis and inflammation.
- RIPK1 and PGAM5 Control Leishmania Replication through Distinct Mechanisms.
- Regulation of RIPK3- and RHIM-dependent Necroptosis by the Proteasome.
- TNF-induced necroptosis and PARP-1-mediated necrosis represent distinct routes to programmed necrotic cell death.
- The Inflammatory Signal Adaptor RIPK3: Functions Beyond Necroptosis.
- The Mitochondrial Phosphatase PGAM5 Is Dispensable for Necroptosis but Promotes Inflammasome Activation in Macrophages.
- The Nucleotide Sensor ZBP1 and Kinase RIPK3 Induce the Enzyme IRG1 to Promote an Antiviral Metabolic State in Neurons.
- The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis.
- The c-FLIPL cleavage product p43FLIP promotes activation of extracellular signal-regulated kinase (ERK), nuclear factor κB (NF-κB), and caspase-8 and T cell survival.
- The molecular regulation of programmed necrotic cell injury.
- The necroptosis adaptor RIPK3 promotes injury-induced cytokine expression and tissue repair.
- The oncogenic microRNA miR-21 promotes regulated necrosis in mice.
- USP20 (Ubiquitin-Specific Protease 20) Inhibits TNF (Tumor Necrosis Factor)-Triggered Smooth Muscle Cell Inflammation and Attenuates Atherosclerosis.