Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword 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
Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis.
An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9.
Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1.
Livin, a novel inhibitor of apoptosis protein family member.
Regulation of apoptosis at cell division by p34cdc2 phosphorylation of survivin.
ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas.
Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes.
A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis.
Characterization of a novel proapoptotic caspase-2- and caspase-9-binding protein.
SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP).
CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis.
Mechanism of XIAP-mediated inhibition of caspase-9.
Apoptosis triggered redistribution of caspase-9 from cytoplasm to mitochondria.
BRCC2, a novel BH3-like domain-containing protein, induces apoptosis in a caspase-dependent manner.
c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage.
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c-Abl directly binds caspase-9
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Phosphorylates caspase-9 at Tyr-153 in DNA damage response
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Y153F mutant attenuates DNA damage-induced apoptosis
Towards a proteome-scale map of the human protein-protein interaction network.
Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.
Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex.
The dependence receptor DCC requires lipid raft localization for cell death signaling.
Engineered hybrid dimers: tracking the activation pathway of caspase-7.
Protective role of Cop in Rip2/caspase-1/caspase-4-mediated HeLa cell death.
Integrin-linked kinase interacts with caspase-9 and -8 in an adhesion-dependent manner for promoting radiation-induced apoptosis in human leukemia cells.
Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1.
IAP antagonists induce autoubiquitination of c-IAPs, NF-kappaB activation, and TNFalpha-dependent apoptosis.
No death without life: vital functions of apoptotic effectors.
Executioner caspase-3 and caspase-7 are functionally distinct proteases.
The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9.
HIP1R interacts with a member of Bcl-2 family, BCL2L10, and induces BAK-dependent cell death.
The Apaf-1*procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer.
Netrin-1 up-regulation in inflammatory bowel diseases is required for colorectal cancer progression.
A truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 function.
Structure of an apoptosome-procaspase-9 CARD complex.
The holo-apoptosome: activation of procaspase-9 and interactions with caspase-3.
Identification of a conserved anti-apoptotic protein that modulates the mitochondrial apoptosis pathway.
The E. coli effector protein NleF is a caspase inhibitor.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
A proteome-scale map of the human interactome network.
A massively parallel pipeline to clone DNA variants and examine molecular phenotypes of human disease mutations.
The EHEC-host interactome reveals novel targets for the translocated intimin receptor.
Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
Dual Site Phosphorylation of Caspase-7 by PAK2 Blocks Apoptotic Activity by Two Distinct Mechanisms.
Active site–adjacent phosphorylation at Tyr-397 by c-Abl kinase inactivates caspase-9.
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Serrano et al. 2017 observed no evidence for Tyr-153 phosphorylation of caspase-9 in vitro or in cells, suggesting that Tyr-153 is NOT phosphorylated by c-Abl as previously reported (cf. PMID:15657060). Instead, the authors identified active-site adjacent Tyr-397 as a c-Abl phosphorylation site that inhibits catalytic activity by interfering with substrate binding — making the c-Abl/caspase-9 axis inhibitory rather than activating in their hands.
New insights into apoptosome structure and function.
LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.
Maximizing binary interactome mapping with a minimal number of assays.
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.
Caspase-9: a multimodal therapeutic target with diverse cellular expression in human disease.
Caspase-9 activation of procaspase-3 but not procaspase-6 is based on the local context of cleavage site motifs and on sequence.
Deorphanizing caspase-3 and caspase-9 substrates in and out of apoptosis with deep substrate profiling.
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Deep N-terminomics identified 124 putative caspase-9 protein substrates (137 cleavage sites) with a caspase-9 cleavage motif of LESD↓(G/S), broadly consistent with classical LEHD preference. Caspase-9 intrinsic catalytic efficiency (kcat/Km ~3.3 x 10^3 M^-1 s^-1) is markedly lower than caspase-3 (7.6 x 10^5 M^-1 s^-1).
Calmodulin Binding Activates Chromobacterium CopC Effector to ADP-Riboxanate Host Apoptotic Caspases.
Drug-induced oxidative stress actively prevents caspase activation and hepatocyte apoptosis.
Phosphorylation of caspases by a bacterial kinase inhibits host programmed cell death.
The concealed side of caspases: beyond a killer of cells.
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Review summarizing non-apoptotic functions of caspases including a role for caspase-9 as a positive regulator of osteoblastic cell migration, and summarizing clinical use of inducible caspase-9 (iCasp9, AP1903/rimiducid) as a safety switch in adoptive cell therapy.
ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B.
Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.
Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner.
Cleavage of Procaspase-3 by the apoptosome
CYCS:APAF1 binds procaspase-9
Cleavage of Procaspase‑9 to caspase‑9
Cleavage of Procaspase-7 by the apoptosome
AKT phosphorylates caspase-9
AKT1 E17K mutant phosphorylates caspase-9
Caspase-9 binds DCC:DIP13alpha complex
CASP9 is phosphorylated at T412
Deep research report on CASP9
Falcon deep research report on CASP9
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Apoptosome binding optimizes physiologic substrate processing (procaspase-3) beyond simple dimerization, integrating evidence from Yin et al. 2006 (PMID:16630893).
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Caspase-9 cleaves procaspase-3 at IETD↓S but does NOT efficiently activate procaspase-6 because local context blocks productive cleavage (PMID:34472839).
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Deep N-terminomics expanded the caspase-9 substrate landscape to ~124 proteins with a LESD↓(G/S) motif (PMID:34553588).
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c-Abl phosphorylates caspase-9 at Tyr-397 (active-site adjacent) to inhibit catalytic activity (PMID:29066624). Notably, the same study observed no evidence for Tyr-153 phosphorylation of caspase-9 in vitro or in cells, suggesting the previously reported activating Tyr-153 c-Abl phosphorylation (PMID:15657060) may not be a productive in-cell event; the c-Abl/caspase-9 axis is best framed as inhibitory via Tyr-397.
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Bacterial effector LegK3 phosphorylates caspase-9 at Thr-102 to inhibit host intrinsic apoptosis (PMID:39349471).
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Drug-induced oxidative stress reversibly blocks caspase activation downstream of MOMP, switching cell death from apoptosis to necrosis (PMID:39245717).
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Non-apoptotic roles include positive regulation of osteoblastic cell migration (PMID:39625520).