“Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade”. Cell91 (4): 479–89. (November 1997). doi:10.1016/s0092-8674(00)80434-1. PMID9390557.
“The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32”. The Journal of Biological Chemistry271 (43): 27099–106. (October 1996). doi:10.1074/jbc.271.43.27099. PMID8900201.
“ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B”. The Journal of Biological Chemistry271 (28): 16720–4. (July 1996). doi:10.1074/jbc.271.28.16720. PMID8663294.
“A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis”. The Journal of Biological Chemistry272 (29): 17907–11. (July 1997). doi:10.1074/jbc.272.29.17907. PMID9218414.
“Caspases: their intracellular localization and translocation during apoptosis”. Cell Death and Differentiation6 (7): 644–51. (July 1999). doi:10.1038/sj.cdd.4400536. PMID10453075.
“Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition”. Circulation Research99 (4): 415–23. (August 2006). doi:10.1161/01.RES.0000237387.05259.a5. PMID16857965.
“Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation”. Molecular Cell9 (2): 423–32. (2002). doi:10.1016/s1097-2765(02)00442-2. PMID11864614.
“Cell death in brain development and degeneration: control of caspase expression may be key!”. Molecular Neurobiology37 (1): 1–6. (February 2008). doi:10.1007/s12035-008-8021-4. PMID18449809.
“Engineering T Cells to Treat Cancer: The Convergence of Immuno-Oncology and Synthetic Biology”. Annual Review of Cancer Biology4: 121–139. (2020). doi:10.1146/annurev-cancerbio-030419-033657.
“A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis”. The Journal of Biological Chemistry276 (12): 9239–45. (March 2001). doi:10.1074/jbc.M006309200. PMID11113115.
“Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-interacting protein”. The Journal of Biological Chemistry279 (38): 39942–50. (September 2004). doi:10.1074/jbc.M405747200. PMID15262985.
“Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex”. The Journal of Biological Chemistry273 (10): 5841–5. (March 1998). doi:10.1074/jbc.273.10.5841. PMID9488720.
“Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. The Journal of Biological Chemistry277 (16): 13430–7. (April 2002). doi:10.1074/jbc.M108029200. PMID11832478.
“Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins”. The Journal of Biological Chemistry276 (12): 9230–8. (March 2001). doi:10.1074/jbc.M009853200. PMID11076957.
“Neuronal apoptosis-inhibitory protein does not interact with Smac and requires ATP to bind caspase-9”. The Journal of Biological Chemistry279 (39): 40622–8. (September 2004). doi:10.1074/jbc.M405963200. PMID15280366.
“Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade”. Cell91 (4): 479–89. (November 1997). doi:10.1016/s0092-8674(00)80434-1. PMID9390557.
“The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32”. The Journal of Biological Chemistry271 (43): 27099–106. (October 1996). doi:10.1074/jbc.271.43.27099. PMID8900201.
“ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B”. The Journal of Biological Chemistry271 (28): 16720–4. (July 1996). doi:10.1074/jbc.271.28.16720. PMID8663294.
“A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis”. The Journal of Biological Chemistry272 (29): 17907–11. (July 1997). doi:10.1074/jbc.272.29.17907. PMID9218414.
“Caspases: their intracellular localization and translocation during apoptosis”. Cell Death and Differentiation6 (7): 644–51. (July 1999). doi:10.1038/sj.cdd.4400536. PMID10453075.
“Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition”. Circulation Research99 (4): 415–23. (August 2006). doi:10.1161/01.RES.0000237387.05259.a5. PMID16857965.
“Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation”. Molecular Cell9 (2): 423–32. (2002). doi:10.1016/s1097-2765(02)00442-2. PMID11864614.
“Cell death in brain development and degeneration: control of caspase expression may be key!”. Molecular Neurobiology37 (1): 1–6. (February 2008). doi:10.1007/s12035-008-8021-4. PMID18449809.
“A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis”. The Journal of Biological Chemistry276 (12): 9239–45. (March 2001). doi:10.1074/jbc.M006309200. PMID11113115.
“Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-interacting protein”. The Journal of Biological Chemistry279 (38): 39942–50. (September 2004). doi:10.1074/jbc.M405747200. PMID15262985.
“Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex”. The Journal of Biological Chemistry273 (10): 5841–5. (March 1998). doi:10.1074/jbc.273.10.5841. PMID9488720.
“Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. The Journal of Biological Chemistry277 (16): 13430–7. (April 2002). doi:10.1074/jbc.M108029200. PMID11832478.
“Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins”. The Journal of Biological Chemistry276 (12): 9230–8. (March 2001). doi:10.1074/jbc.M009853200. PMID11076957.
“Neuronal apoptosis-inhibitory protein does not interact with Smac and requires ATP to bind caspase-9”. The Journal of Biological Chemistry279 (39): 40622–8. (September 2004). doi:10.1074/jbc.M405963200. PMID15280366.