The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target—CASP9 encoding caspase-9 in Homo sapiens—matches the canonical literature description of a CARD-containing initiator caspase activated by the Apaf-1/cytochrome c apoptosome in intrinsic (mitochondrial) apoptosis, and responsible for activating downstream executioner caspases (especially caspase-3 and caspase-7). The reviewed sources consistently describe this same protein identity and mechanism and do not indicate symbol ambiguity for the reviewed content. (avrutsky2021caspase9amultimodal pages 1-2, dorstyn2018newinsightsinto pages 1-2)
Caspase-9 is an initiator caspase in the intrinsic (mitochondrial) apoptosis pathway; it is activated on a multiprotein platform (the apoptosome) rather than primarily by upstream proteolytic cleavage in the way some executioner caspases are activated. (avrutsky2021caspase9amultimodal pages 1-2, dorstyn2018newinsightsinto pages 1-2)
Apoptosome (definition): a heptameric complex formed by Apaf-1 in response to mitochondrial outer membrane permeabilization (MOMP) and cytochrome c release; this platform recruits procaspase-9 through CARD–CARD interactions and promotes caspase-9 activation by proximity-driven dimerization. (avrutsky2021caspase9amultimodal pages 1-2, dorstyn2018newinsightsinto pages 1-2)
Caspases are cysteine-aspartyl proteases that cleave peptide bonds almost exclusively C-terminal to aspartate (P1 = Asp) in substrates. (araya2021deorphanizingcaspase3and pages 1-3, araya2021deorphanizingcaspase3and pages 4-6)
For caspase-9, the best-established physiological role is to proteolytically activate procaspase-3 and procaspase-7 by cleaving their intersubunit linker (ISL) between large and small catalytic subunits. (araya2021deorphanizingcaspase3and pages 1-3)
Caspase-9 specificity is frequently assayed using tetrapeptide motifs; LEHD-containing peptide substrates are described as optimal assay substrates for caspase-9. (yin2006caspase9holoenzymeis pages 2-3, yin2006caspase9holoenzymeis pages 1-2)
However, protein substrate cleavage is not determined by motif alone: local structural context and accessibility can dominate whether a motif is productively cleaved. For example, caspase-9 effectively cleaves procaspase-3 ISL at IETD↓S, but does not efficiently activate procaspase-6 despite it having ISL Asp motifs, because the local context prevents productive cleavage. (soni2021caspase9activationof pages 20-22, soni2021caspase9activationof pages 6-8, soni2021caspase9activationof pages 9-11)
In intrinsic apoptosis, mitochondrial stress leads to cytochrome c release, which binds Apaf-1; Apaf-1 assembles a heptameric apoptosome that directly engages multiple procaspase-9 molecules via CARD–CARD interactions, forming an activation assembly that promotes caspase-9 activation and subsequent activation of downstream effector caspases. (avrutsky2021caspase9amultimodal pages 1-2, dorstyn2018newinsightsinto pages 1-2)
Biochemical evidence indicates that dimerization is sufficient to activate caspase-9 catalysis, but apoptosome binding strongly optimizes recognition/processing of physiologic protein substrates (notably procaspase-3). In particular, the apoptosome-bound caspase-9 holoenzyme shows much stronger functional efficiency toward procaspase-3 (lower Km) than engineered dimeric caspase-9, even though peptide-substrate kinetics can differ. (yin2006caspase9holoenzymeis pages 2-3, yin2006caspase9holoenzymeis pages 1-2)
Functionally, caspase-9 activation occurs in the cytosol at/near sites where cytochrome c becomes available and apoptosome assembly occurs (after MOMP). This is implied by the requirement for cytosolic cytochrome c to assemble Apaf-1 apoptosomes and activate caspase-9. (avrutsky2021caspase9amultimodal pages 1-2, dorstyn2018newinsightsinto pages 1-2)
Substrate profiling studies also support that caspase-9 substrates are largely cytoplasmic and nuclear proteins (with relatively few mitochondrial substrates detected), consistent with broad downstream proteolysis after activation. (araya2021identifyingnovelapoptotic pages 64-66)
Deep N-terminomics in native lysates identified a caspase-9 cleavage motif consistent with LESD↓(G/S) at P4–P1↓P1′, described as similar to previously reported LEHD specificity. (araya2021deorphanizingcaspase3and pages 4-6)
In direct biochemical context-dependent studies, caspase-9 showed an active-site preference ranking of IETDS > TEVDA > DVVDN (P4–P1′), with mechanistic explanation based on hydrogen-bonding and hydrophobicity of subsites (e.g., hydrophobic S4 accommodating hydrophobic P4 residues). (soni2021caspase9activationof pages 20-22, soni2021caspase9activationof pages 6-8)
Caspase-9 cleaves and activates downstream effector caspases, especially by cleaving procaspase-3 at an ISL site IETD↓S (cleavage after Asp). (soni2021caspase9activationof pages 20-22, soni2021caspase9activationof pages 6-8, araya2021deorphanizingcaspase3and pages 1-3)
Historically, few caspase-9 substrates outside the procaspase cascade were known; deep substrate profiling substantially expanded this list.
Caspase-9 generally has lower intrinsic catalytic efficiency than executioner caspases in peptide-based comparisons; one analysis reports kcat/Km ~3.3 × 10^3 M−1 s−1 for caspase-9 versus 7.6 × 10^5 M−1 s−1 for caspase-3. (araya2021deorphanizingcaspase3and pages 4-6)
(a) Host kinase c-Abl → inhibitory Tyr phosphorylation
A mechanistic study identified Tyr-397 as a dominant c-Abl phosphorylation site on caspase-9 and concluded that phosphorylation at this site inhibits caspase-9 activity, consistent with the site being adjacent to (and interfering with) substrate binding near the active site. (serrano2017activesite–adjacentphosphorylation pages 2-4)
(b) Bacterial kinase LegK3 → CASP9 Thr102 phosphorylation to suppress apoptosis
A 2024 Nature Communications study showed that Legionella pneumophila effector LegK3 directly phosphorylates multiple caspases, including caspase-9 at Thr102, and that this phosphorylation impairs caspase activation/processing by upstream regulators without abolishing intrinsic proteolytic activity—supporting a pathogen strategy to keep infected host cells alive. (Published Sep 2024; https://doi.org/10.1038/s41467-024-52817-1). (ge2024phosphorylationofcaspases pages 1-2)
In the context of acetaminophen (APAP)-induced hepatocyte death, a 2024 Cell Death & Disease study reported that APAP not only fails to activate caspases but also strongly impedes their activation upon classical apoptosis induction, shifting apoptosis toward necrosis; importantly, the work identifies oxidative stress as a key factor and reports that caspase inhibition and the phenotype switch are reversible by antioxidants. (Published Sep 2024; https://doi.org/10.1038/s41419-024-06998-8). (lambrecht2024druginducedoxidativestress pages 1-2)
This type of mechanism is directly relevant to CASP9 functional annotation because caspase-9 activation depends on successful apoptosome/caspase activation downstream of MOMP, and redox state can act as a “decision layer” controlling whether the caspase cascade proceeds. (lambrecht2024druginducedoxidativestress pages 1-2)
LegK3-mediated phosphorylation of caspase-9 at Thr102 provides a concrete example of pathogen-encoded, residue-specific suppression of host intrinsic apoptosis. This expands the known regulatory landscape from host PTMs to bacterial effector PTMs acting on initiator caspases. (ge2024phosphorylationofcaspases pages 1-2)
The APAP hepatotoxicity study reframes “absence of caspase activation” not merely as ATP depletion or failure of MOMP, but as an oxidative-stress-driven, reversible block of caspase activation. This directly informs how caspase-9-dependent apoptosis may be prevented in clinically important toxic injuries. (lambrecht2024druginducedoxidativestress pages 1-2)
A 2024 review highlights extensive deployment of inducible caspase-9 (iCasp9) as a clinically relevant, pharmacologically controlled safety switch (AP1903/rimiducid or AP20187), with rapid on-demand elimination of modified cells to manage severe toxicities (e.g., GVHD/CRS/ICANS). (Published Dec 2024; https://doi.org/10.1007/s00018-024-05495-7). (abdelghany2024theconcealedside pages 13-15, abdelghany2024theconcealedside pages 15-17)
iCasp9 is a fusion construct that uses chemical dimerizers (e.g., AP1903/rimiducid, AP20187) to force caspase-9 dimerization and trigger apoptosis of engineered cells.
Quantitative examples summarized in the 2024 review include:
* >90% apoptosis of iCasp9-transduced cells within ~2 hours after 10 nM AP1903 in some settings. (abdelghany2024theconcealedside pages 13-15)
* >98% programmed cell death in iPSC systems under reported inducer conditions (e.g., AP20187 0.1 nM in one cited system). (abdelghany2024theconcealedside pages 15-17)
These data indicate that engineered caspase-9 activation can provide fast, high-magnitude control of cell therapies, while also acknowledging limitations such as possible resistance/outgrowth mechanisms and safety concerns (e.g., cytokine release). (abdelghany2024theconcealedside pages 15-17)
CASPALLO (NCT00710892; Baylor College of Medicine; first posted 2008)
A Phase 1 trial of allodepleted donor T cells transduced with iCasp9 after haploidentical transplant; the dimerizer AP1903 is used to eliminate transduced cells if needed, with the primary safety objective defined as Grade III/IV GVHD ≤25%. Enrollment reported as 10 (actual). (NCT00710892 chunk 1)
Administration of Donor T Cells With the Caspase-9 Suicide Gene (NCT01494103; Baylor College of Medicine; first posted 2011)
Phase 1 dose-escalation study of iCasp9-modified donor T cells after haploidentical transplant to improve immune reconstitution while retaining an AP1903-activatable safety switch; enrollment reported as 15 (actual). (NCT01494103 chunk 1)
Anti-CD19 CAR-T Cells With Inducible Caspase 9 Safety Switch for B-cell lymphoma (NCT03696784; UNC; first posted 2019)
Phase 1 iC9-CAR19 study where rimiducid/AP1903 can activate the safety switch to reduce CAR-T burden in severe CRS/ICANS; the record describes long-term follow-up up to 15 years. (NCT03696784 chunk 1)
A consistent mechanistic theme is that caspase-9 is not simply “turned on” by cleavage, but is controlled by assembly on activating platforms (apoptosome) and by factors that determine whether the platform forms and whether caspase-9 engages substrates productively. This explains why peptide activity can be a poor proxy for physiological substrate processing and why cellular context (mitochondrial permeabilization, nucleotide availability, redox state) strongly impacts functional output. (dorstyn2018newinsightsinto pages 1-2, yin2006caspase9holoenzymeis pages 1-2)
Beyond apoptosis initiation, evidence supports broader substrate sets and roles—e.g., numerous substrates identified by N-terminomics and the possibility that caspase-9 can cleave “early substrates” and may participate in non-apoptotic regulation. (araya2021deorphanizingcaspase3and pages 4-6, araya2021identifyingnovelapoptotic pages 64-66)
Open Targets lists CASP9 associations across multiple disease areas including neurodegenerative disease, non-small cell lung carcinoma, acute myeloid leukemia, and hepatocellular carcinoma, supporting CASP9 as a disease-relevant apoptosis regulator and potential therapeutic node. (OpenTargets Search: -CASP9)
In drug-induced liver injury models, cell-death outcomes can shift away from caspase-mediated apoptosis due to oxidative stress–linked caspase inhibition, highlighting a mechanistic connection between redox injury and caspase-9 pathway failure in clinically important contexts. (lambrecht2024druginducedoxidativestress pages 1-2)
The following table consolidates core CASP9 functional annotation—identity, catalytic chemistry, activation mechanism, substrates, regulation, disease and applications—with direct evidence anchors.
| Aspect | Key points | Representative recent evidence (2024) and foundational evidence |
|---|---|---|
| Identity / domains | Human CASP9 encodes caspase-9, the canonical initiator caspase of intrinsic (mitochondrial) apoptosis. Domain architecture matches UniProt P55211: N-terminal CARD plus catalytic caspase large/small subunits (p35/p10 after processing). Activation occurs on the Apaf-1 apoptosome via CARD–CARD interactions. | 2024 review and pathway synthesis support intrinsic-pathway initiator role; foundational apoptosome review details CARD-mediated recruitment to Apaf-1 apoptosome (avrutsky2021caspase9amultimodal pages 1-2, dorstyn2018newinsightsinto pages 1-2) |
| Catalytic reaction | Cysteine-aspartate protease that cleaves peptide bonds C-terminal to Asp (P1 = D) in substrates. Physiologic role is proteolytic activation of downstream effector caspases. | Caspases cleave after Asp; caspase-9 functions upstream of caspase-3/-7 (araya2021deorphanizingcaspase3and pages 1-3, araya2021deorphanizingcaspase3and pages 4-6) |
| Substrate specificity | Canonical peptide preference includes LEHD; deep profiling found a related LESD↓(G/S) motif in native lysates. Specificity depends on both sequence and local structural context. | LEHD-AFC described as optimal peptide substrate; N-terminomics identified LESD-like motif and lower catalytic efficiency than caspase-3 (yin2006caspase9holoenzymeis pages 2-3, yin2006caspase9holoenzymeis pages 1-2, araya2021deorphanizingcaspase3and pages 4-6) |
| Activation mechanism | Mitochondrial stress releases cytochrome c, which binds Apaf-1; with nucleotide loading this forms the heptameric apoptosome that recruits procaspase-9 via CARD–CARD interactions, promoting dimerization/activation. Apoptosome binding strongly enhances productive processing of physiologic substrates. | 2024 intrinsic-apoptosis reviews summarize cytochrome c/Apaf-1/caspase-9 axis; foundational work shows apoptosome is the activating platform and optimizes procaspase-3 processing (avrutsky2021caspase9amultimodal pages 1-2, dorstyn2018newinsightsinto pages 1-2, yin2006caspase9holoenzymeis pages 2-3, yin2006caspase9holoenzymeis pages 1-2) |
| Key substrates | Best-established physiologic substrates are procaspase-3 and procaspase-7. Caspase-9 directly cleaves procaspase-3 at the ISL motif IETD↓S (around D175) but does not directly activate procaspase-6 efficiently because local context blocks productive cleavage. Additional reported substrates include vimentin, semaphorin-7A, MVP, SNX1/2, HDAC7, RING2/RING1B, and many newly identified targets. | Procaspase-3 cleavage motif and inability to directly activate procaspase-6 shown biochemically; broader substrate set expanded by deep substrate profiling (soni2021caspase9activationof pages 20-22, soni2021caspase9activationof pages 6-8, araya2021deorphanizingcaspase3and pages 1-3, araya2021identifyingnovelapoptotic pages 28-31) |
| Regulation / PTMs | Caspase-9 is heavily regulated by phosphorylation and protein inhibitors. c-Abl phosphorylation at Tyr-397 inhibits activity by blocking substrate binding near the active site. A 2024 study showed LegK3 from Legionella pneumophila phosphorylates Thr102 in caspase-9, impairing upstream processing/activation without abolishing intrinsic catalytic competence. XIAP is a direct endogenous inhibitor of caspase-9 and can restrain downstream activation after MOMP. | 2024 bacterial-effector study identifies Thr102; foundational JBC study identifies inhibitory Tyr-397 phosphorylation; 2024 hepatocyte study notes XIAP directly inhibits caspase-9/3 downstream of MOMP (ge2024phosphorylationofcaspases pages 1-2, serrano2017activesite–adjacentphosphorylation pages 2-4, yin2006caspase9holoenzymeis pages 2-3) |
| Non-apoptotic roles | Beyond apoptosis, caspase-9 has reported roles in cell differentiation, mitochondrial/homeostatic regulation, and cell motility. In 2024 proteomics-based work, caspase-9 was identified as a positive regulator of osteoblastic cell migration. | 2024 osteoblast study supports migration role; multimodal review summarizes broader non-apoptotic functions (avrutsky2021caspase9amultimodal pages 1-2, abdelghany2024theconcealedside pages 15-17) |
| Disease links | Dysregulated CASP9 signaling is implicated across cancer and neurodegeneration; Open Targets lists associations including neurodegenerative disease, non-small cell lung carcinoma, acute myeloid leukemia, and hepatocellular carcinoma. CASP9 alternative splicing into pro-apoptotic caspase-9a and pro-survival caspase-9b is a recurrent disease-relevant mechanism. | 2024 disease-focused reviews discuss oncologic and neurodegenerative relevance; Open Targets disease associations support broad translational importance; 2024 splicing review notes caspase-9a vs caspase-9b (OpenTargets Search: -CASP9, avrutsky2021caspase9amultimodal pages 1-2) |
| Applications / real-world implementation | Inducible caspase-9 (iCasp9) is an established suicide/safety switch in engineered cell therapy. A chemical dimerizer (e.g., AP1903/rimiducid) activates iCasp9, rapidly triggering apoptosis of modified cells to control GVHD, CRS, or ICANS. Representative trials: NCT00710892 (CASPALLO allodepleted donor T cells; actual enrollment 10), NCT01494103 (donor T cells with iCasp9 after haploidentical transplant; actual enrollment 15), NCT03696784 (anti-CD19 CAR-T with iC9 safety switch for B-cell lymphoma; active-not-recruiting). | 2024 review summarizes iCasp9 mechanism, rapid kill kinetics, benefits and caveats; trial records document real clinical deployment in transplant and CAR-T settings (abdelghany2024theconcealedside pages 15-17, abdelghany2024theconcealedside pages 13-15, NCT00710892 chunk 1, NCT01494103 chunk 1, NCT03696784 chunk 1) |
Table: This table summarizes the core functional annotation of human CASP9/caspase-9, including mechanism, substrate specificity, regulation, disease relevance, and translational applications. It highlights both recent 2024 findings and foundational mechanistic evidence with citation IDs for direct traceability.
References
(avrutsky2021caspase9amultimodal pages 1-2): Maria I. Avrutsky and Carol M. Troy. Caspase-9: a multimodal therapeutic target with diverse cellular expression in human disease. Frontiers in Pharmacology, Jul 2021. URL: https://doi.org/10.3389/fphar.2021.701301, doi:10.3389/fphar.2021.701301. This article has 164 citations.
(dorstyn2018newinsightsinto pages 1-2): Loretta Dorstyn, Christopher W. Akey, and Sharad Kumar. New insights into apoptosome structure and function. Cell Death & Differentiation, 25:1194-1208, May 2018. URL: https://doi.org/10.1038/s41418-017-0025-z, doi:10.1038/s41418-017-0025-z. This article has 254 citations and is from a domain leading peer-reviewed journal.
(araya2021deorphanizingcaspase3and pages 1-3): Luam E. Araya, Ishankumar V. Soni, Jeanne A. Hardy, and Olivier Julien. Deorphanizing caspase-3 and caspase-9 substrates in and out of apoptosis with deep substrate profiling. ACS chemical biology, 16:2280-2296, Sep 2021. URL: https://doi.org/10.1021/acschembio.1c00456, doi:10.1021/acschembio.1c00456. This article has 155 citations and is from a domain leading peer-reviewed journal.
(araya2021deorphanizingcaspase3and pages 4-6): Luam E. Araya, Ishankumar V. Soni, Jeanne A. Hardy, and Olivier Julien. Deorphanizing caspase-3 and caspase-9 substrates in and out of apoptosis with deep substrate profiling. ACS chemical biology, 16:2280-2296, Sep 2021. URL: https://doi.org/10.1021/acschembio.1c00456, doi:10.1021/acschembio.1c00456. This article has 155 citations and is from a domain leading peer-reviewed journal.
(yin2006caspase9holoenzymeis pages 2-3): Qian Yin, Hyun Ho Park, Jee Y. Chung, Su-Chang Lin, Yu-Chih Lo, Li S. da Graca, Xuejun Jiang, and Hao Wu. Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine. Molecular cell, 22 2:259-68, Apr 2006. URL: https://doi.org/10.1016/j.molcel.2006.03.030, doi:10.1016/j.molcel.2006.03.030. This article has 112 citations and is from a highest quality peer-reviewed journal.
(yin2006caspase9holoenzymeis pages 1-2): Qian Yin, Hyun Ho Park, Jee Y. Chung, Su-Chang Lin, Yu-Chih Lo, Li S. da Graca, Xuejun Jiang, and Hao Wu. Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine. Molecular cell, 22 2:259-68, Apr 2006. URL: https://doi.org/10.1016/j.molcel.2006.03.030, doi:10.1016/j.molcel.2006.03.030. This article has 112 citations and is from a highest quality peer-reviewed journal.
(soni2021caspase9activationof pages 20-22): Ishankumar V. Soni and Jeanne A. Hardy. Caspase-9 activation of procaspase-3 but not procaspase-6 is based on the local context of cleavage site motifs and on sequence. Biochemistry, 60:2824-2835, Sep 2021. URL: https://doi.org/10.1021/acs.biochem.1c00459, doi:10.1021/acs.biochem.1c00459. This article has 19 citations and is from a peer-reviewed journal.
(soni2021caspase9activationof pages 6-8): Ishankumar V. Soni and Jeanne A. Hardy. Caspase-9 activation of procaspase-3 but not procaspase-6 is based on the local context of cleavage site motifs and on sequence. Biochemistry, 60:2824-2835, Sep 2021. URL: https://doi.org/10.1021/acs.biochem.1c00459, doi:10.1021/acs.biochem.1c00459. This article has 19 citations and is from a peer-reviewed journal.
(soni2021caspase9activationof pages 9-11): Ishankumar V. Soni and Jeanne A. Hardy. Caspase-9 activation of procaspase-3 but not procaspase-6 is based on the local context of cleavage site motifs and on sequence. Biochemistry, 60:2824-2835, Sep 2021. URL: https://doi.org/10.1021/acs.biochem.1c00459, doi:10.1021/acs.biochem.1c00459. This article has 19 citations and is from a peer-reviewed journal.
(araya2021identifyingnovelapoptotic pages 64-66): Luam Ellen Araya. Identifying novel apoptotic and non-apoptotic substrates of caspases. Text, Jan 2021. URL: https://doi.org/10.7939/r3-hq7g-3f52, doi:10.7939/r3-hq7g-3f52. This article has 1 citations and is from a peer-reviewed journal.
(araya2021identifyingnovelapoptotic pages 28-31): Luam Ellen Araya. Identifying novel apoptotic and non-apoptotic substrates of caspases. Text, Jan 2021. URL: https://doi.org/10.7939/r3-hq7g-3f52, doi:10.7939/r3-hq7g-3f52. This article has 1 citations and is from a peer-reviewed journal.
(serrano2017activesite–adjacentphosphorylation pages 2-4): Banyuhay P. Serrano, Hannah S. Szydlo, Dominique Alfandari, and Jeanne A. Hardy. Active site–adjacent phosphorylation at tyr-397 by c-abl kinase inactivates caspase-9. Journal of Biological Chemistry, 292:21352-21365, Dec 2017. URL: https://doi.org/10.1074/jbc.m117.811976, doi:10.1074/jbc.m117.811976. This article has 14 citations and is from a domain leading peer-reviewed journal.
(ge2024phosphorylationofcaspases pages 1-2): Jinli Ge, Ying Wang, Xueyu Li, Qian Lu, Hangqian Yu, Hongtao Liu, Kelong Ma, Xuming Deng, Zhao-Qing Luo, Xiaoyun Liu, and Jiazhang Qiu. Phosphorylation of caspases by a bacterial kinase inhibits host programmed cell death. Nature Communications, Sep 2024. URL: https://doi.org/10.1038/s41467-024-52817-1, doi:10.1038/s41467-024-52817-1. This article has 14 citations and is from a highest quality peer-reviewed journal.
(lambrecht2024druginducedoxidativestress pages 1-2): Rebekka Lambrecht, Jasmin Jansen, Franziska Rudolf, Mohamed El-Mesery, Sabrina Caporali, Ivano Amelio, Florian Stengel, and Thomas Brunner. Drug-induced oxidative stress actively prevents caspase activation and hepatocyte apoptosis. Cell Death & Disease, Sep 2024. URL: https://doi.org/10.1038/s41419-024-06998-8, doi:10.1038/s41419-024-06998-8. This article has 15 citations and is from a peer-reviewed journal.
(abdelghany2024theconcealedside pages 13-15): Lina Abdelghany, Chanin Sillapachaiyaporn, and Boris Zhivotovsky. The concealed side of caspases: beyond a killer of cells. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05495-7, doi:10.1007/s00018-024-05495-7. This article has 19 citations.
(abdelghany2024theconcealedside pages 15-17): Lina Abdelghany, Chanin Sillapachaiyaporn, and Boris Zhivotovsky. The concealed side of caspases: beyond a killer of cells. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05495-7, doi:10.1007/s00018-024-05495-7. This article has 19 citations.
(NCT00710892 chunk 1): Malcolm Brenner. CASPALLO: Allodepleted T Cells Transduced With Inducible Caspase 9 Suicide Gene. Baylor College of Medicine. 2008. ClinicalTrials.gov Identifier: NCT00710892
(NCT01494103 chunk 1): Malcolm Brenner. Administration of Donor T Cells With the Caspase-9 Suicide Gene. Baylor College of Medicine. 2011. ClinicalTrials.gov Identifier: NCT01494103
(NCT03696784 chunk 1): Anti-CD19 CAR-T Cells With Inducible Caspase 9 Safety Switch for B-cell Lymphoma. UNC Lineberger Comprehensive Cancer Center. 2019. ClinicalTrials.gov Identifier: NCT03696784
(OpenTargets Search: -CASP9): Open Targets Query (-CASP9, 10 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.