Death caspase-1
Akita, K., et al. (1997). Involvement of caspase-1 and caspase-3 in the production and processing of mature human interleukin 18 in monocytic THP.1 cells. J. Biol. Chem. 272(42): 26595-26603.
Alnemri, E. S., et al. (1996). Human ICD/CED-3 protease nomenclature. Cell 87: 171
Beidler, D. R., et al. (1995). The baculovirus p35 protein inhibits Fas- and tumor necrosis factor-induced apoptosis. J Biol Chem 270: 16526-16528.
Bergeron, L., et al. (1998). Defects in regulation of apoptosis in caspase-2-deficient mice. Genes Dev. 12(9): 1304-1314.
Brancolini, C., et al. (1997). Dismantling cell-cell contacts during apoptosis is coupled to a caspase-dependent proteolytic cleavage of beta-catenin. J. Cell Biol. 139(3): 759-771.
Bruey, J.-M., et al. (2007). Bcl-2 and Bcl-XL regulate proinflammatory Caspase-1 activation by interaction with NALP1. Cell 129: 45-56. Medline abstract: 17418785
Buendia, B., Santa-Maria, A. and Courvalin, J. C. (1999). Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis. J. Cell Sci. 112(Pt 11): 1743-1753.
Campbell, D. S. and Holt, C. E. (2003). Apoptotic pathway and MAPKs differentially regulate chemotropic responses of retinal growth cones. Neuron 37: 939-952. 12670423
Cardone, M. H., et al. (1997). The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell 90(2): 315-323.
Cecconi, F., et al. (1998). Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 94(6): 727-37.
Chai, J., et al. (2000). Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 406(6798): 855-62. 10972280
Cheema, Z. F., et al. (1999). Fas/Apo [Apoptosis]-1 and associated proteins in the differentiating cerebral cortex: induction of caspase-dependent cell death and activation of NF-kappaB. J. Neurosci. 19(5): 1754-70.
Chen, P., et al. (1998). Dredd, a novel effector of the apoptosis activators Reaper, Grim, and Hid in Drosophila. Dev. Biol. 201(2): 202-16
Cheng, E. H., et al. (1997). Conversion of Bcl-2 to a Bax-like death effector by caspases. Science 278(5345): 1966-1968.
Chin, Y. E., et al. (1997). Activation of the STAT signaling pathway can cause expression of caspase 1 and apoptosis. Mol. Cell. Biol. 17(9): 5328-5337.
Chinnaiyan, A. M., et al. (1996). Molecular ordering of the cell death pathway. Bcl-2 and Bcl-xL Function upstream of the CED-3-like apoptotic proteases. J. Biol. Chem. 271: 4573-4576.
Chong, J. A., et al. (1995). REST: a mammalian silencer protein that restricts sodium channel gene expression to neurons. Cell 80: 949-957. PubMed Citation: 7697725
Chu, Z. L., et al. (1997). Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control. Proc. Natl. Acad. Sci. 94(19): 10057-10062
Clarke, C. A., Bennett, L. N. and Clarke, P. R. (2005). Cleavage of claspin by caspase-7 during apoptosis inhibits the Chk1 pathway. J. Biol. Chem. 280(42): 35337-45. 16123041
Clem, R. J., et al. (1998). Modulation of cell death by Bcl-xL through caspase interaction. Proc. Natl. Acad. Sci. 95: 554-559
Devereaux, Q. L., et al (1997). X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388(6639): 300-304.
Dorstyn, L., et al. (1999a). DRONC, an ecdysone-inducible Drosophila caspase. Proc. Natl. Acad. Sci. 96(8): 4307-12.
Dorstyn, L., et al. (1999b). DECAY, a novel Drosophila caspase related to mammalian caspase-3 and caspase-7. J. Biol. Chem. 274: 30778-30783.
Du, Y., et al. (1997). Activation of a caspase 3-related cysteine protease is required for glutamate-mediated apoptosis of cultured cerebellar granule neurons. Proc. Natl. Acad. Sci. 94(21): 11657-11662.
Duckett, C. S., et al. (1996). A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors. EMBO J. 15: 2685-2694
Duckett, C. S., et al. (1998). Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c. Mol. Cell. Biol. 18(1): 608-615.
Ekert, P., et al. (2001). Diablo promotes apoptosis by removing miha/xiap from processed caspase 9. J. Cell Biol. 152(3): 483-90. 11157976
Enari, M., Hug, H. and Nagata, S. (1995). Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 375: 78-81.
Enari, M., et al. (1998). A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391(6662): 43-50.
Erhardt, P., Tomaselli, K. J. and Cooper, G. M. (1997). Identification of the MDM2 oncoprotein as a substrate for CPP32-like apoptotic proteases. J. Biol. Chem. 272 (24): 15049-15052.
Fernandes-Alnemri, T., Litwack, G. and Alnemri, E. S. (1994). CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J Biol Chem 269: 30761-30764.
Fraser, A. G. and Evan, G. I. (1997a). Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE. EMBO J. 16: 2805-13.
Fraser, A.G., McCarthy, N.J. and Evan, G.I. (1997b). drICE is an essential caspase required for apoptotic activity in Drosophila cells. EMBO J. 16(20): 6192-6199.
Goping, I. S., et al. (1998). Regulated targeting of BAX to mitochondria. J. Cell Biol. 143(1): 207-15.
Hakem, R., et al. (1998). Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 94(3): 339-352.
Hasegawa, J., et al. (1996). Involvement of CPP32/Yama(-like) proteases in Fas-mediated apoptosis. Cancer Res. 56: 1713-1718.
Hawkins, C. J., Wang, S. L. and Hay, B. A. (1999). A cloning method to identify caspases and their regulators in yeast: identification of Drosophila IAP1 as an inhibitor of the Drosophila caspase DCP-1. Proc. Natl. Acad. Sci. 96(6): 2885-90.
Hay, B. A., Wassarman, D. A. and Rubin, G. M. (1995). Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death. Cell 83: 1253-1262
Hoeppner, D. J., Hengartner, M. O. and Schnabel, R. (2001). Engulfment genes cooperate with ced-3 to promote cell death in Caenorhabditis elegans Nature 412: 202-206. 11449279
Hu, Y., et al. (1998). Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc. Natl. Acad. Sci. 95(8): 4386-4391. 9539746
Huesmann, G. R. and Clayton, D. F. (2006). Dynamic role of postsynaptic caspase-3 and BIRC4 in zebra finch song-response habituation. Neuron 52(6): 1061-72. Medline abstract: 17178408
Hugunin, M., et al. (1996). Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product. J. Biol. Chem. 271: 3517-3522.
Inohara, N., et al. (1997). CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis. Proc. Natl. Acad. Sci. 94(20): 10717-10722.
James, C. et al. (1997). CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9. Current Biol. 7: 246-252. 9094313
Joshi, P. and Eisenmann, D. M. (2004). The Caenorhabditis elegans pvl-5 gene protects hypodermal cells from ced-3-dependent, ced-4-independent cell death. Genetics 167(2): 673-85. . 15238520
Juo, P., et al. (1997). Fas activation of the p38 mitogen-activated protein kinase signaling pathway requires ICE/CED-3 family proteases. Mol. Cell. Biol 17: 24-35
Kagaya, S., et al. (1997). A functional role for death proteases in s-Myc- and c-Myc-mediated apoptosis. Mol. Cell. Biol. 17(11): 6736-6745.
Kaiser, W. J., Vucic, D. and Miller, L. K. (1998). The Drosophila inhibitor of apoptosis D-IAP1 suppresses cell death induced by the caspase drICE. FEBS Lett. 440(1-2): 243-8.
Kanuka, H., et al. (1999). Proapoptotic activity of Caenorhabditis elegans CED-4 protein in Drosophila: implicated mechanisms for caspase activation. Proc. Natl. Acad. Sci. 96(1): 145-50.
Kiessling, S. and Green, D. R. (2006). Cell survival and proliferation in Drosophila S2 cells following apoptotic stress in the absence of the APAF-1 homolog, ARK, or downstream caspases. Apoptosis 11(4): 497-507. 16532275
Kitanaka, C., et al. (1997). Caspase-dependent apoptosis of COS-7 cells induced by Bax overexpression: differential effects of Bcl-2 and Bcl-xL on Bax-induced caspase activation and apoptosis. Oncogene 15(15): 1763-1772.
Kluck, R. M., et al. (1997). Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. EMBO J. 16(15): 4639-4649.
Kondo, T., Yokokura, T. and Nagata, S. (1997a). Activation of distinct caspase-like proteases by fas and reaper in Drosophila cells. Proc. Natl. Acad. Sci. 94(22): 11951-11956.
Kondo, T., et al. (1997b). ERM (Ezrin/Radixin/Moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. J. Cell Biol. 139: 749-758
Koseki, T., et al. (1998). ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases. Proc. Natl. Acad. Sci. 95(9): 5156-5160.
Kothakota, S. L., et al. (1997). Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis. Science 278(5336): 294-298
Krajewski, S., et al. (1999). Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia. Proc. Natl. Acad. Sci. 96(10): 5752-7.
Kruse, A. A., Stripling, R. and Clayton, D. F. (2000). Minimal experience required for immediate-early gene induction in zebra finch neostriatum. Neurobiol. Learn. Mem. 74(3): 179-84. Medline abstract: 11031126
Kuida, K., et al. (1998). Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 94(3): 325-337.
Kumar, A., et al. (1997). Defective TNF-alpha-induced apoptosis in STAT1-null cells due to low constitutive levels of caspases. Science 278(5343): 1630-1632.
Kumar, S., et al. (1994). Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme. Genes Dev. 8: 1613-26.
Lee, C.-Y., et al. (2000). E93 directs steroid-triggered programmed cell death in Drosophila. Mol. Cell 6: 433-443. 10983989
Lee, N., et al. (1997). Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis. Proc. Natl. Acad. Sci. 94(25): 13642-13647.
Levkau, B., et al. (1999). Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-kappaB loop. Nat. Cell Biol. 1: 227-233
Li, H., et al. (1997). Activation of caspase-2 in apoptosis. J. Biol. Chem. 272(34): 21010-21017.
Li, P., et al. (1997). Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91(4): 479-489.
Los, M., et al. (1995). Requirement of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis. Nature 375: 81-83.
Luo X., et al. (1998). Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94(4): 481-490.
Maurer, C. W., Chiorazzi, M. and Shaham, S. (2007). Timing of the onset of a developmental cell death is controlled by transcriptional induction of the C. elegans ced-3 caspase-encoding gene. Development 134(7): 1357-68. Medline abstract: 17329362
McCall, K. and Steller, H. (1998). Requirement for DCP-1 caspase during Drosophila oogenesis. Science 279(5348): 230-234
Meier, P., et al. (2000). The Drosophila caspase Dronc is regulated by DIAP1. EMBO J. 19: 598-611
Mello, C. V., Vicario, D. S. and Clayton, D. F. (1992). Song presentation induces gene expression in the songbird forebrain. Proc. Natl. Acad. Sci. 89(15): 6818-22. Medline abstract: 1495970
Mochizuki, T., et al. (1997). Pim-1 kinase stimulates c-Myc-mediated death signaling upstream of caspase-3 (CPP32)-like protease activation. Oncogene 15(12): 1471-1480.
Mosser, D. D., et al. (1997). Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17(9): 5317-5327.
Mukae, N., et al. (1998). Molecular cloning and characterization of human caspase-activated DNase. Proc. Natl. Acad. Sci. 95(16): 9123-9128.
Continued: Death caspase-1 Evolutionary homologs part 2/2
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