Gene Ontology annotation through association of InterPro records with GO terms

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

C. elegans MAC-1, an essential member of the AAA family of ATPases, can bind CED-4 and prevent cell death.

The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3 substrate that associates with CED-4 and mediates apoptosis in mammalian cells.

The C. elegans orthologue ceBNIP3 interacts with CED-9 and CED-3 but kills through a BH3- and caspase-independent mechanism.

Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing.

Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans.

Matefin/SUN-1 is a nuclear envelope receptor for CED-4 during Caenorhabditis elegans apoptosis.

DPL-1 DP, LIN-35 Rb and EFL-1 E2F act with the MCD-1 zinc-finger protein to promote programmed cell death in Caenorhabditis elegans.

Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death execution pathways downstream of ced-3 and independent of ced-9.

Inhibition of CED-3 zymogen activation and apoptosis in Caenorhabditis elegans by caspase homolog CSP-3.

Caenorhabditis elegans caspase homolog CSP-2 inhibits CED-3 autoactivation and apoptosis in germ cells.

Caspase-dependent conversion of Dicer ribonuclease into a death-promoting deoxyribonuclease.

Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4.

Meiotic errors activate checkpoints that improve gamete quality without triggering apoptosis in male germ cells.

Shared developmental roles and transcriptional control of autophagy and apoptosis in Caenorhabditis elegans.

Programmed elimination of cells by caspase-independent cell extrusion in C. elegans.

Both the caspase CSP-1 and a caspase-independent pathway promote programmed cell death in parallel to the canonical pathway for apoptosis in Caenorhabditis elegans.

The Nrf2/SKN-1-dependent glutathione S-transferase π homologue GST-1 inhibits dopamine neuron degeneration in a Caenorhabditis elegans model of manganism.

Mechanistic insights into CED-4-mediated activation of CED-3.

Caspase-mediated activation of Caenorhabditis elegans CED-8 promotes apoptosis and phosphatidylserine externalization.

Maintenance of muscle myosin levels in adult C. elegans requires both the double bromodomain protein BET-1 and sumoylation.

Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by inhibiting the AKT pathway.

CED-3 caspase acts with miRNAs to regulate non-apoptotic gene expression dynamics for robust development in C. elegans.

The Cell Death Pathway Regulates Synapse Elimination through Cleavage of Gelsolin in Caenorhabditis elegans Neurons.

Regulation of CED-3 caspase localization and activation by C. elegans nuclear-membrane protein NPP-14.

Genetic control of programmed cell death in the nematode C. elegans.

Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product.

The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease.

Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death.

Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4.

Interaction and regulation of the Caenorhabditis elegans death protease CED-3 by CED-4 and CED-9.

Role of CED-4 in the activation of CED-3.

Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor.

The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9.

The death inhibitory molecules CED-9 and CED-4L use a common mechanism to inhibit the CED-3 death protease.

Regulation of apoptosis by a Caenorhabditis elegans BNIP3 homolog.

Identification of multiple Caenorhabditis elegans caspases and their potential roles in proteolytic cascades.