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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB.
RIP3, a novel apoptosis-inducing kinase.
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.
DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB.
cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms.
Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1.
cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).
Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase.
The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways.
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis.
Herpes Simplex Virus 1 (HSV-1) and HSV-2 Mediate Species-Specific Modulations of Programmed Necrosis through the Viral Ribonucleotide Reductase Large Subunit R1.
The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex.
PELI1 Selectively Targets Kinase-Active RIP3 for Ubiquitylation-Dependent Proteasomal Degradation.
SARS-Coronavirus Open Reading Frame-3a drives multimodal necrotic cell death.
Nuclear RIPK3 and MLKL contribute to cytosolic necrosome formation and necroptosis.
Herpes simplex virus encoded ICP6 protein forms functional amyloid assemblies with necroptosis-associated host proteins.
The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3.
NMR characterization of an assembling RHIM (RIP homotypic interaction motif) amyloid reveals a cryptic region for self-recognition.
Curcumin alleviates experimental colitis in mice by suppressing necroptosis of intestinal epithelial cells.
ZBP1(DAI) recruits RIP1 and RIP3
RIP3 binds TRIF to mediate necroptosis
RIPK1-mediated regulated necrosis
RIPK1:RIPK3 oligomer binds MLKL
RIPK1:RIPK3 oligomerizes to form amyloid-like fibrils
RIPK3 phosphorylates MLKL
RIP3 binds TICAM1 within TLR3 complex to mediate necroptosis
SARS-CoV-1 3a oligomerizes
SARS-CoV-1 3a binds the lysosomal membrane
SARS-CoV-1 3a binds RIPK1:RIPK3 oligomer
PELI1 ubiquitinates RIPK3 at K363
PELI1 binds activated RIPK1:RIPK3
RIPK3 is cleaved by CASP8
MLKL binds IP4, IP5 and IP6
O-GlcNAcylation of RIPK3 (TLR4 signaling)
STUB1 ubiquitinates RIPK3 at K55, K363
MLKL binds PDCD6IP and SDCBP
Small molecule inhibitor binds RIPK1, RIPK3
ITCH polyubiquitinates MLKL at K50
PRKN polyubiquitinates RIPK3