“Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain”. Cell104 (5): 781–90. (March 2001). doi:10.1016/S0092-8674(01)00273-2. PMID11257231.
“Targeting apoptosis in prostate cancer: focus on caspases and inhibitors of apoptosis proteins”. BJU International96 Suppl 2: 30–4. (December 2005). doi:10.1111/j.1464-410X.2005.05944.x. PMID16359436.
“Making a definitive diagnosis: successful clinical application of whole exome sequencing in a child with intractable inflammatory bowel disease”. Genetics in Medicine13 (3): 255–62. (March 2011). doi:10.1097/GIM.0b013e3182088158. PMID21173700.
“ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis”. The Journal of Biological Chemistry277 (34): 30454–62. (August 2002). doi:10.1074/jbc.M203312200. PMID12048196.
“X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes”. The Journal of Biological Chemistry276 (29): 27058–63. (July 2001). doi:10.1074/jbc.M102415200. PMID11359776.
“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.
“HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins”. The Journal of Biological Chemistry277 (1): 445–54. (January 2002). doi:10.1074/jbc.M109891200. PMID11604410.
“A novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLO”. The Journal of Biological Chemistry278 (9): 7494–9. (February 2003). doi:10.1074/jbc.C200695200. PMID12511567.
“Direct interaction between survivin and Smac/DIABLO is essential for the anti-apoptotic activity of survivin during taxol-induced apoptosis”. The Journal of Biological Chemistry278 (25): 23130–40. (June 2003). doi:10.1074/jbc.M300957200. PMID12660240.
“Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins”. Cell102 (1): 43–53. (July 2000). doi:10.1016/S0092-8674(00)00009-X. PMID10929712.
“The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein”. The Journal of Biological Chemistry278 (40): 38699–706. (October 2003). doi:10.1074/jbc.M303179200. PMID12865429.
“Neurotrophin receptor-interacting mage homologue is an inducible inhibitor of apoptosis protein-interacting protein that augments cell death”. The Journal of Biological Chemistry276 (43): 39985–9. (October 2001). doi:10.1074/jbc.C100171200. PMID11546791.
“XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2”. Cellular Signalling20 (11): 2107–12. (November 2008). doi:10.1016/j.cellsig.2008.08.004. PMID18761086.
“Identification of XAF1 as an antagonist of XIAP anti-Caspase activity”. Nature Cell Biology3 (2): 128–33. (February 2001). doi:10.1038/35055027. PMID11175744.
“Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain”. Cell104 (5): 781–90. (March 2001). doi:10.1016/S0092-8674(01)00273-2. PMID11257231.
“Targeting apoptosis in prostate cancer: focus on caspases and inhibitors of apoptosis proteins”. BJU International96 Suppl 2: 30–4. (December 2005). doi:10.1111/j.1464-410X.2005.05944.x. PMID16359436.
“Making a definitive diagnosis: successful clinical application of whole exome sequencing in a child with intractable inflammatory bowel disease”. Genetics in Medicine13 (3): 255–62. (March 2011). doi:10.1097/GIM.0b013e3182088158. PMID21173700.
“ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis”. The Journal of Biological Chemistry277 (34): 30454–62. (August 2002). doi:10.1074/jbc.M203312200. PMID12048196.
“X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes”. The Journal of Biological Chemistry276 (29): 27058–63. (July 2001). doi:10.1074/jbc.M102415200. PMID11359776.
“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.
“HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins”. The Journal of Biological Chemistry277 (1): 445–54. (January 2002). doi:10.1074/jbc.M109891200. PMID11604410.
“A novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLO”. The Journal of Biological Chemistry278 (9): 7494–9. (February 2003). doi:10.1074/jbc.C200695200. PMID12511567.
“Direct interaction between survivin and Smac/DIABLO is essential for the anti-apoptotic activity of survivin during taxol-induced apoptosis”. The Journal of Biological Chemistry278 (25): 23130–40. (June 2003). doi:10.1074/jbc.M300957200. PMID12660240.
“Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins”. Cell102 (1): 43–53. (July 2000). doi:10.1016/S0092-8674(00)00009-X. PMID10929712.
“The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein”. The Journal of Biological Chemistry278 (40): 38699–706. (October 2003). doi:10.1074/jbc.M303179200. PMID12865429.
“Neurotrophin receptor-interacting mage homologue is an inducible inhibitor of apoptosis protein-interacting protein that augments cell death”. The Journal of Biological Chemistry276 (43): 39985–9. (October 2001). doi:10.1074/jbc.C100171200. PMID11546791.
“XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2”. Cellular Signalling20 (11): 2107–12. (November 2008). doi:10.1016/j.cellsig.2008.08.004. PMID18761086.
“Identification of XAF1 as an antagonist of XIAP anti-Caspase activity”. Nature Cell Biology3 (2): 128–33. (February 2001). doi:10.1038/35055027. PMID11175744.