References
1. Amstad, P. A. et al. Detection of caspase activation in situ by fluorochrome-labeled caspase inhibitors. Biotechniques 31, 608- 610, 612, 614, passim (2001). 2. Bedner, E., Smolewski, P., Amstad, P. & Darzynkiewicz, Z. Activation of caspases measured in situ by binding of fluorochromelabeled inhibitors of caspases (FLICA): correlation with DNA fragmentation. Exp Cell Res 259, 308-313, doi:10.1006/excr.2000.4955 (2000). 3. Slee, E. A., Adrain, C. & Martin, S. J. Serial killers: ordering caspase activation events in apoptosis. Cell Death Differ 6, 1067- 1074, doi:10.1038/sj.cdd.4400601 (1999). 4. Shamaa, O. R., Mitra, S., Gavrilin, M. A. & Wewers, M. D. Monocyte Caspase-1 Is Released in a Stable, Active High Molecular Weight Complex Distinct from the Unstable Cell Lysate-Activated Caspase-1. PLoS One 10, e0142203, doi:10.1371/journal. pone.0142203 (2015). 5. Mariathasan, S. et al. Diff erential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218, doi:10.1038/nature02664 (2004). 6. Kumar, S. Mechanisms mediating caspase activation in cell death. Cell Death Differ 6, 1060-1066, doi:10.1038/sj.cdd.4400600 (1999). 7. Rotonda, J. et al. The three-dimensional structure of apopain/ CPP32, a key mediator of apoptosis. Nat Struct Biol 3, 619-625 (1996). 8. Walker, N. P. et al. Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer. Cell 78, 343-352 (1994). 9. Wilson, K. P. et al. Structure and mechanism of interleukin-1 beta converting enzyme. Nature 370, 270-275, doi:10.1038/370270a0 (1994). 10. Thornberry, N. A. et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functionalrelationships established for keyUSBio References
No references available
TDS
NCBI
UniProt
Tech Support
Customer Service
