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, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis.
The apoptotic signaling pathway activated by Toll-like receptor-2.
Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule.
Interaction of Daxx, a Fas binding protein, with sentrin and Ubc9.
Caspase-10 is an initiator caspase in death receptor signaling.
CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis.
Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis.
Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes.
Defects in death-inducing signalling complex formation prevent JNK activation and Fas-mediated apoptosis in DU 145 prostate carcinoma cells.
Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation.
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction.
The role of receptor internalization in CD95 signaling.
Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1.
The structure of FADD and its mode of interaction with procaspase-8.
Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation.
Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling.
No death without life: vital functions of apoptotic effectors.
Yes and PI3K bind CD95 to signal invasion of glioblastoma.
A pathway sensor for genome-wide screens of intracellular proteolytic cleavage.
TNF-alpha induces two distinct caspase-8 activation pathways.
Identification of an antiapoptotic protein complex at death receptors.
ABIN-1 is a ubiquitin sensor that restricts cell death and sustains embryonic development.
The Fas-FADD death domain complex structure unravels signalling by receptor clustering.
The Parkinson disease protein leucine-rich repeat kinase 2 transduces death signals via Fas-associated protein with death domain and caspase-8 in a cellular model of neurodegeneration.
Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha.
Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation.
Expression of the Bcl-2 protein BAD promotes prostate cancer growth.
Multivalent DR5 peptides activate the TRAIL death pathway and exert tumoricidal activity.
Phosphorylation by polo-like kinase 1 induces the tumor-suppressing activity of FADD.
The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations.
Whole-exome-sequencing-based discovery of human FADD deficiency.
Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced apoptosis.
NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-α feedforward signaling.
TWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8.
Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation.
The naturally processed CD95L elicits a c-yes/calcium/PI3K-driven cell migration pathway.
cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms.
DJ-1 inhibits TRAIL-induced apoptosis by blocking pro-caspase-8 recruitment to FADD.
PMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivo.
Toward an understanding of the protein interaction network of the human liver.
RIP1 is required for IAP inhibitor-mediated sensitization of childhood acute leukemia cells to chemotherapy-induced apoptosis.
Pick your poison: the Ripoptosome, a cell death platform regulating apoptosis and necroptosis.
Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation.
Vesicles released by activated T cells induce both Fas-mediated RIP-dependent apoptotic and Fas-independent nonapoptotic cell deaths.
Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains.
A type III effector antagonizes death receptor signalling during bacterial gut infection.
DDX24 negatively regulates cytosolic RNA-mediated innate immune signaling.
Apo2L/TRAIL and the death receptor 5 agonist antibody AMG 655 cooperate to promote receptor clustering and antitumor activity.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
A massively parallel pipeline to clone DNA variants and examine molecular phenotypes of human disease mutations.
TNFα sensitizes neuroblastoma cells to FasL-, cisplatin- and etoposide-induced cell death by NF-κB-mediated expression of Fas.
The seventh zinc finger motif of A20 is required for the suppression of TNF-α-induced apoptosis.
An Evolution-Guided Analysis Reveals a Multi-Signaling Regulation of Fas by Tyrosine Phosphorylation and its Implication in Human Cancers.
A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
A protein interaction landscape of breast cancer.
Deciphering DED assembly mechanisms in FADD-procaspase-8-cFLIP complexes regulating apoptosis.
A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain.
FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.
TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.
Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death.
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
Casper is a FADD- and caspase-related inducer of apoptosis.
Bovine herpesvirus 4 BORFE2 protein inhibits Fas- and tumor necrosis factor receptor 1-induced apoptosis and contains death effector domains shared with other gamma-2 herpesviruses.
Caspase-8 processing in the DISC
TRADD:TRAF2:RIP1 binds FADD
TRAIL-mediated dimerization of procaspase-8
TNF-mediated dimerization of procaspase-8
FASL:FAS Receptor Trimer:FADD complex binds procaspase-10
TRAIL:TRAIL-Receptor2 Trimer:FADD complex binds procaspase-10
MAVS interacts with RIPK1 and FADD
TLR4-induced ripoptosome assembly
Caspase-8 processing within TLR4 complex
FLIP(L) and procaspase-8 form heterodimer in TRAIL signaling
FLIP(L) and procaspase-8 form heterodimer in TNF signaling
FLIP(S) and procaspase-8 form heterodimer
Caspase-8 and FLIP(L) processing at DISC
FLIP(L) and procaspase-8 form heterodimer in FasL/CD95 signaling
RIPK1 is cleaved by CASP8
FLIP(L) and procaspase-8 form heterodimer
FAS-mediated dimerization of procaspase-8
TRAIL:TRAIL Receptor Trimer:FADD complex binds procaspase-8
TRAIL:TRAIL receptor trimers bind FADD
TRADD:TRAF2:RIP1:FADD binds pro-caspase 8
FASL:FAS Receptor Trimer:FADD complex binds pro-Caspase-8
TLR3-induced ripoptosome assembly
Caspase-8 processing within TLR3 complex
Dimerzation of procaspase-8, procaspase-10
Recruitment of caspase-8 and -10 to FADD complex
Recruitment of IKK complex
RIPK1 variant is not cleaved by CASP8
Caspase-8 and FLIP(L) processing at TNFR signaling complex
RIPK1 is cleaved by CASP8:FLIP(L)
MicroRNA-103/107 Regulate Programmed Necrosis and Myocardial Ischemia/Reperfusion Injury Through Targeting FADD.