Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Molecular cloning and expression of a receptor for human tumor necrosis factor.
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Original cloning of TNFR1 (p55) demonstrating TNF receptor activity
"Synthetic DNA probes based on amino acid sequence information were used to isolate cDNA clones encoding a receptor for TNF. The TNF receptor (TNF-R) is a 415 amino acid polypeptide with a single membrane-spanning region."
The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation.
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Identified TRADD as the primary adaptor for TNFR1 death domain that signals both apoptosis and NF-kappaB activation
"Many diverse activities of tumor necrosis factor (TNF) are signaled through TNF receptor 1 (TNFR1). We have identified a novel 34 kDa protein, designated TRADD, that specifically interacts with an intracellular domain of TNFR1 known to be essential for mediating programmed cell death. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa B."
TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.
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Demonstrated that TRADD-TRAF2 activates NF-kappaB while TRADD-FADD induces apoptosis, defining the bifurcation of TNFR1 signaling at TRADD
"Tumor necrosis factor (TNF) can induce apoptosis and activate NF-kappa B through signaling cascades emanating from TNF receptor 1 (TNFR1). TRADD is a TNFR1-associated signal transducer that is involved in activating both pathways. Here we show that TRADD directly interacts with TRAF2 and FADD, signal transducers that activate NF-kappa B and induce apoptosis, respectively."
TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex.
MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase.
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Identified MADD as a death domain protein interacting with TNFR1, linking the receptor to MAP kinase activation and arachidonic acid release
"We have used the yeast interaction trap to isolate a protein, MADD, that associates with the death domain of TNFR1 through its own C-terminal death domain. MADD interacts with TNFR1 residues that are critical for signal generation and coimmunoprecipitates with TNFR1, implicating MADD as a component of the TNFR1 signaling complex."
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes.
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Defined the two-complex model: Complex I (TNFR1/TRADD/RIP1/TRAF2) at the membrane for NF-kappaB activation, and cytosolic Complex II (TRADD/RIP1/FADD/caspase-8) for apoptosis
"The initial plasma membrane bound complex (complex I) consists of TNFR1, the adaptor TRADD, the kinase RIP1, and TRAF2 and rapidly signals activation of NF-kappa B. In a second step, TRADD and RIP1 associate with FADD and caspase-8, forming a cytoplasmic complex (complex II)."
TNF receptor 1 genetic risk mirrors outcome of anti-TNF therapy in multiple sclerosis.
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Identified MS-associated TNFRSF1A variant causing exon 6 skipping, producing soluble Delta6-TNFR1 isoform. Showed Golgi membrane localization of TNFR1
"While FL-TNFR1 localizes to the Golgi apparatus, Δ6-TNFR1 demonstrated a more diffuse intracellular distribution (Fig. 2), consistent with the absence of the Golgi-retention motif."
The type 1 receptor (CD120a) is the high-affinity receptor for soluble tumor necrosis factor.
Tumor necrosis factor alpha - a link between neuroinflammation and excitotoxicity.
Tumor necrosis factor disrupts claudin-5 endothelial tight junction barriers in two distinct NF-κB-dependent phases.
Heterogeneity among patients with tumor necrosis factor receptor-associated periodic syndrome phenotypes.
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Characterized TRAPS-associated TNFRSF1A variants and showed soluble TNFR1 in extracellular space
"Plasma concentrations of soluble tumor necrosis factor receptor superfamily 1A (sTNFRSF1A) were measured, and fluorescence-activated cell sorter analysis was used to measure TNFRSF1A shedding from monocytes."
The shedding activity of ADAM17 is sequestered in lipid rafts.
A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway.
SH3RF2 functions as an oncogene by mediating PAK4 protein stability.
Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation.
Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R, cloned using amino acid sequence data of its soluble form, encodes both the cell surface and a soluble form of the receptor.
Signal pathways in astrocytes activated by cross-talk between of astrocytes and mast cells through CD40-CD40L.
Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins.
Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
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Identified BAG4/SODD as a silencer that binds the TNFR1 death domain to prevent spontaneous signaling
"Tumor necrosis factor receptor type 1 (TNF-R1) contains a cytoplasmic death domain that is required for the signaling of TNF activities such as apoptosis and nuclear factor kappa B (NF-kappaB) activation. Normally, these signals are generated only after TNF-induced receptor aggregation."
Deep research synthesis of TNFRSF1A literature
Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD.
A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.
Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1.
IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis.
Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation.
Riboflavin kinase couples TNF receptor 1 to NADPH oxidase.
Proteinase-activated receptor-2 mediated inhibition of TNFalpha-stimulated JNK activation - A novel paradigm for G(q/11) linked GPCRs.
The Polycomb group protein EED couples TNF receptor 1 to neutral sphingomyelinase.
Multivalent DR5 peptides activate the TRAIL death pathway and exert tumoricidal activity.
Smac mimetic bypasses apoptosis resistance in FADD- or caspase-8-deficient cells by priming for tumor necrosis factor α-induced necroptosis.
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis.
Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains.
Progranulin directly binds to the CRD2 and CRD3 of TNFR extracellular domains.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
The seventh zinc finger motif of A20 is required for the suppression of TNF-α-induced apoptosis.
Human tumor necrosis factor-alpha receptor. Purification by immunoaffinity chromatography and initial characterization.
A Human IgSF Cell-Surface Interactome Reveals a Complex Network of Protein-Protein Interactions.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
A physical wiring diagram for the human immune system.
Novel biochemical, structural, and systems insights into inflammatory signaling revealed by contextual interaction proteomics.
Systematic mutational analysis of the death domain of the tumor necrosis factor receptor 1-associated protein TRADD.
The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex.
Toward an understanding of the protein interaction network of the human liver.
Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation.
Membrane lymphotoxin-α(2)β is a novel tumor necrosis factor (TNF) receptor 2 (TNFR2) agonist.
RAIDD is a new 'death' adaptor molecule.
A novel role for the apoptosis inhibitor ARC in suppressing TNFα-induced regulated necrosis.
Expression of the Bcl-2 protein BAD promotes prostate cancer growth.
Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.
Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding.
Reactome pathway - TNFR1-induced signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling
Reactome pathway - TNFR1 signaling