カスパーゼ-6
関連文献

“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 (49):  30761–4. (1995). doi:10.1016/S0021-9258(18)47344-9. PMID 7983002.
“Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis”. Proc. Natl. Acad. Sci. U.S.A. 93 (16):  8395–400. (1996). Bibcode: 1996PNAS...93.8395T. doi:10.1073/pnas.93.16.8395. PMC 38682. PMID 8710882. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC38682/.
“Chromosomal mapping of cell death proteases CPP32, MCH2, and MCH3”. Genomics 36 (2):  362–5. (1997). doi:10.1006/geno.1996.0476. PMID 8812467.
“The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32”. J. Biol. Chem. 271 (43):  27099–106. (1996). doi:10.1074/jbc.271.43.27099. PMID 8900201.
“Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases”. Proc. Natl. Acad. Sci. U.S.A. 93 (25):  14486–91. (1997). Bibcode: 1996PNAS...9314486S. doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC26159/.
“Lamin proteolysis facilitates nuclear events during apoptosis”. J. Cell Biol. 135 (6 Pt 1):  1441–55. (1997). doi:10.1083/jcb.135.6.1441. PMC 2133948. PMID 8978814. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133948/.
“Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease”. Science 277 (5324):  373–6. (1998). doi:10.1126/science.277.5324.373. PMID 9219695.
“FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis”. J. Biol. Chem. 272 (30):  18542–5. (1997). doi:10.1074/jbc.272.30.18542. PMID 9228018.
“Caspase Cleavage of Keratin 18 and Reorganization of Intermediate Filaments during Epithelial Cell Apoptosis”. J. Cell Biol. 138 (6):  1379–94. (1997). doi:10.1083/jcb.138.6.1379. PMC 2132555. PMID 9298992. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132555/.
“Caspases Are Activated in a Branched Protease Cascade and Control Distinct Downstream Processes in Fas-induced Apoptosis”. J. Exp. Med. 187 (4):  587–600. (1998). doi:10.1084/jem.187.4.587. PMC 2212161. PMID 9463409. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2212161/.
“Caspase-mediated cleavage of the ubiquitin-protein ligase Nedd4 during apoptosis”. J. Biol. Chem. 273 (22):  13524–30. (1998). doi:10.1074/jbc.273.22.13524. PMID 9593687.
“The 72-kDa component of signal recognition particle is cleaved during apoptosis”. J. Biol. Chem. 273 (52):  35362–70. (1999). doi:10.1074/jbc.273.52.35362. PMID 9857079.
“Caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis”. J. Biol. Chem. 274 (7):  4335–40. (1999). doi:10.1074/jbc.274.7.4335. PMID 9933635.
“Phosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosis”. Proc. Natl. Acad. Sci. U.S.A. 96 (4):  1391–6. (1999). Bibcode: 1999PNAS...96.1391W. doi:10.1073/pnas.96.4.1391. PMC 15473. PMID 9990034. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC15473/.
“Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases”. FEBS Lett. 445 (1):  149–54. (1999). doi:10.1016/S0014-5793(99)00108-8. hdl:10067/238040151162165141. PMID 10069390. https://repository.uantwerpen.be/docman/irua/8538a1/5202.pdf.
“Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis”. EMBO J. 18 (8):  2049–56. (1999). doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171289/.