カスパーゼ-3 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "カスパーゼ-3" in Japanese language version.

refsWebsite

Global rank Japanese rank

64nih.gov

4^th place

24^th place

44doi.org

2^nd place

6^th place

1ensembl.org

1,626^th place

2,625^th place

1wikipedia.org

low place

1univ-montp2.fr

low place

doi.org (Global: 2^nd place; Japanese: 6^th place)

“Human ICE/CED-3 protease nomenclature”. Cell 87 (2): 171. (October 1996). doi:10.1016/S0092-8674(00)81334-3. PMID 8861900.
“Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation”. Cell 97 (3): 395–406. (April 1999). doi:10.1016/s0092-8674(00)80748-5. PMID 10319819.
“Construction and analysis of a modular model of caspase activation in apoptosis”. Theoretical Biology & Medical Modelling 5 (1): 26. (2008). doi:10.1186/1742-4682-5-26. PMC 2672941. PMID 19077196.
“Apoptosis: an overview”. British Medical Bulletin 53 (3): 451–65. (1997). doi:10.1093/oxfordjournals.bmb.a011623. PMID 9374030.
“Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis”. The Journal of Biological Chemistry 272 (30): 18530–3. (July 1997). doi:10.1074/jbc.272.30.18530. PMID 9228015.
“Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8”. The Biochemical Journal 350 (2): 563–8. (September 2000). doi:10.1042/0264-6021:3500563. PMC 1221285. PMID 10947972.
“Caspases: opening the boxes and interpreting the arrows”. Cell Death and Differentiation 9 (1): 3–5. (January 2002). doi:10.1038/sj.cdd.4400963. PMID 11803369.
“Plasticity of S2-S4 specificity pockets of executioner caspase-7 revealed by structural and kinetic analysis”. The FEBS Journal 274 (18): 4752–65. (September 2007). doi:10.1111/j.1742-4658.2007.05994.x. PMID 17697120.
“Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition”. Journal of Molecular Biology 360 (3): 654–66. (July 2006). doi:10.1016/j.jmb.2006.05.041. PMID 16781734.
“Caspases: structure-guided design of drugs to control cell death”. Mini Reviews in Medicinal Chemistry 8 (11): 1154–62. (October 2008). doi:10.2174/138955708785909899. PMID 18855730.
“Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase”. Cell 81 (5): 801–9. (June 1995). doi:10.1016/0092-8674(95)90541-3. PMID 7774019.
“Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis”. Nature 376 (6535): 37–43. (July 1995). doi:10.1038/376037a0. PMID 7596430.
“Caspases: pharmacological manipulation of cell death”. The Journal of Clinical Investigation 115 (10): 2665–72. (October 2005). doi:10.1172/JCI26252. PMC 1236692. PMID 16200200.
“Emerging roles of caspase-3 in apoptosis”. Cell Death and Differentiation 6 (2): 99–104. (February 1999). doi:10.1038/sj.cdd.4400476. PMID 10200555.
“Biochemical characteristics of caspases-3, -6, -7, and -8”. The Journal of Biological Chemistry 272 (41): 25719–23. (October 1997). doi:10.1074/jbc.272.41.25719. PMID 9325297.
“Apoptosis and cancer: mutations within caspase genes”. Journal of Medical Genetics 46 (8): 497–510. (August 2009). doi:10.1136/jmg.2009.066944. PMID 19505876.
“Mechanisms of caspase activation”. Current Opinion in Cell Biology 15 (6): 725–31. (December 2003). doi:10.1016/j.ceb.2003.10.009. PMID 14644197.
“A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis”. The Biochemical Journal 424 (3): 335–45. (December 2009). doi:10.1042/BJ20090825. PMC 2805924. PMID 19788411.
“Apoptosis: live or die--hard work either way!”. Hormone and Metabolic Research 33 (9): 511–9. (September 2001). doi:10.1055/s-2001-17213. PMID 11561209.
“Novel procaspase-3 activating cascade mediated by lysoapoptases and its biological significances in apoptosis”. Advances in Enzyme Regulation 41 (1): 237–50. (2001). doi:10.1016/S0065-2571(00)00018-2. PMID 11384748.
“Mitochondrial activation of apoptosis”. Cell 116 (2 Suppl): S57–9, 2 p following S59. (January 2004). doi:10.1016/S0092-8674(04)00031-5. PMID 15055583.
“Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9”. The Biochemical Journal 405 (1): 11–9. (July 2007). doi:10.1042/BJ20070288. PMC 1925235. PMID 17437405.
“Protective effect of mangosteen extract against beta-amyloid-induced cytotoxicity, oxidative stress and altered proteome in SK-N-SH cells”. Journal of Proteome Research 9 (5): 2076–86. (May 2010). doi:10.1021/pr100049v. PMID 20232907.
“Serum caspase-3 p17 fragment is elevated in patients with ST-segment elevation myocardial infarction: a novel observation”. Journal of the American College of Cardiology 57 (2): 220–1. (January 2011). doi:10.1016/j.jacc.2010.08.628. PMID 21211695.
“Rehabilitation of a contract killer: caspase-3 directs stem cell differentiation”. Cell Stem Cell 2 (6): 515–6. (June 2008). doi:10.1016/j.stem.2008.05.013. PMID 18522841.
“Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. The Journal of Biological Chemistry 277 (16): 13430–7. (April 2002). doi:10.1074/jbc.M108029200. PMID 11832478.
“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”. Proceedings of the National Academy of Sciences of the United States of America 93 (25): 14486–91. (December 1996). doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078.
Selvakumar, P.; Sharma, RK. (May 2007). “Role of calpain and caspase system in the regulation of N-myristoyltransferase in human colon cancer (Review).”. Int J Mol Med 19 (5): 823–7. doi:10.3892/ijmm.19.5.823. PMID 17390089.
“Casper is a FADD- and caspase-related inducer of apoptosis”. Immunity 6 (6): 751–63. (June 1997). doi:10.1016/S1074-7613(00)80450-1. PMID 9208847.
“MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death”. Proceedings of the National Academy of Sciences of the United States of America 94 (21): 11333–8. (October 1997). doi:10.1073/pnas.94.21.11333. PMC 23459. PMID 9326610.
“The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation”. Proceedings of the National Academy of Sciences of the United States of America 98 (6): 3416–21. (March 2001). doi:10.1073/pnas.051378298. PMC 30668. PMID 11248093.
“Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells”. The EMBO Journal 18 (8): 2040–8. (April 1999). doi:10.1093/emboj/18.8.2040. PMC 1171288. PMID 10205158.
“Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis”. The EMBO Journal 18 (8): 2049–56. (April 1999). doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159.
“Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells”. The Biochemical Journal 364 (Pt 1): 41–7. (May 2002). doi:10.1042/bj3640041. PMC 1222543. PMID 11988074.
“Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis”. Biochemical and Biophysical Research Communications 288 (4): 981–9. (November 2001). doi:10.1006/bbrc.2001.5862. PMID 11689006.
“An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7”. Biochemistry 40 (4): 1117–23. (January 2001). doi:10.1021/bi001603q. PMID 11170436.
“TRAF1 is a substrate of caspases activated during tumor necrosis factor receptor-alpha-induced apoptosis”. The Journal of Biological Chemistry 276 (11): 8087–93. (March 2001). doi:10.1074/jbc.M009450200. PMID 11098060.
“Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death”. Proceedings of the National Academy of Sciences of the United States of America 98 (15): 8662–7. (July 2001). doi:10.1073/pnas.161506698. PMC 37492. PMID 11447297.
“The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites”. The Journal of Cell Biology 157 (1): 115–24. (April 2002). doi:10.1083/jcb.200108085. PMC 2173256. PMID 11927604.
“Structural basis for the inhibition of caspase-3 by XIAP”. Cell 104 (5): 791–800. (March 2001). doi:10.1016/S0092-8674(01)00274-4. PMID 11257232.
“The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases”. The EMBO Journal 16 (23): 6914–25. (December 1997). doi:10.1093/emboj/16.23.6914. PMC 1170295. PMID 9384571.
“X-linked IAP is a direct inhibitor of cell-death proteases”. Nature 388 (6639): 300–4. (July 1997). doi:10.1038/40901. PMID 9230442.
“X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes”. The Journal of Biological Chemistry 276 (29): 27058–63. (July 2001). doi:10.1074/jbc.M102415200. PMID 11359776.
“Identification of NRF2, a member of the NF-E2 family of transcription factors, as a substrate for caspase-3(-like) proteases”. Cell Death and Differentiation 6 (9): 865–72. (September 1999). doi:10.1038/sj.cdd.4400566. PMID 10510468.

ensembl.org (Global: 1,626^th place; Japanese: 2,625^th place)

May2017.archive.ensembl.org

GRCm38: Ensembl release 89: ENSMUSG00000031628 - Ensembl, May 2017

nih.gov (Global: 4^th place; Japanese: 24^th place)

pubmed.ncbi.nlm.nih.gov

“Human ICE/CED-3 protease nomenclature”. Cell 87 (2): 171. (October 1996). doi:10.1016/S0092-8674(00)81334-3. PMID 8861900.
“Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation”. Cell 97 (3): 395–406. (April 1999). doi:10.1016/s0092-8674(00)80748-5. PMID 10319819.
“Construction and analysis of a modular model of caspase activation in apoptosis”. Theoretical Biology & Medical Modelling 5 (1): 26. (2008). doi:10.1186/1742-4682-5-26. PMC 2672941. PMID 19077196.
“Apoptosis: an overview”. British Medical Bulletin 53 (3): 451–65. (1997). doi:10.1093/oxfordjournals.bmb.a011623. PMID 9374030.
“Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis”. The Journal of Biological Chemistry 272 (30): 18530–3. (July 1997). doi:10.1074/jbc.272.30.18530. PMID 9228015.
“Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8”. The Biochemical Journal 350 (2): 563–8. (September 2000). doi:10.1042/0264-6021:3500563. PMC 1221285. PMID 10947972.
“Caspases: opening the boxes and interpreting the arrows”. Cell Death and Differentiation 9 (1): 3–5. (January 2002). doi:10.1038/sj.cdd.4400963. PMID 11803369.
“Plasticity of S2-S4 specificity pockets of executioner caspase-7 revealed by structural and kinetic analysis”. The FEBS Journal 274 (18): 4752–65. (September 2007). doi:10.1111/j.1742-4658.2007.05994.x. PMID 17697120.
“Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition”. Journal of Molecular Biology 360 (3): 654–66. (July 2006). doi:10.1016/j.jmb.2006.05.041. PMID 16781734.
“Caspases: structure-guided design of drugs to control cell death”. Mini Reviews in Medicinal Chemistry 8 (11): 1154–62. (October 2008). doi:10.2174/138955708785909899. PMID 18855730.
“CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme”. The Journal of Biological Chemistry 269 (49): 30761–4. (December 1994). PMID 7983002.
“Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase”. Cell 81 (5): 801–9. (June 1995). doi:10.1016/0092-8674(95)90541-3. PMID 7774019.
“Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis”. Nature 376 (6535): 37–43. (July 1995). doi:10.1038/376037a0. PMID 7596430.
“Caspases: pharmacological manipulation of cell death”. The Journal of Clinical Investigation 115 (10): 2665–72. (October 2005). doi:10.1172/JCI26252. PMC 1236692. PMID 16200200.
“Emerging roles of caspase-3 in apoptosis”. Cell Death and Differentiation 6 (2): 99–104. (February 1999). doi:10.1038/sj.cdd.4400476. PMID 10200555.
“Biochemical characteristics of caspases-3, -6, -7, and -8”. The Journal of Biological Chemistry 272 (41): 25719–23. (October 1997). doi:10.1074/jbc.272.41.25719. PMID 9325297.
“Apoptosis and cancer: mutations within caspase genes”. Journal of Medical Genetics 46 (8): 497–510. (August 2009). doi:10.1136/jmg.2009.066944. PMID 19505876.
“Mechanisms of caspase activation”. Current Opinion in Cell Biology 15 (6): 725–31. (December 2003). doi:10.1016/j.ceb.2003.10.009. PMID 14644197.
“A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis”. The Biochemical Journal 424 (3): 335–45. (December 2009). doi:10.1042/BJ20090825. PMC 2805924. PMID 19788411.
“Apoptosis: live or die--hard work either way!”. Hormone and Metabolic Research 33 (9): 511–9. (September 2001). doi:10.1055/s-2001-17213. PMID 11561209.
“Novel procaspase-3 activating cascade mediated by lysoapoptases and its biological significances in apoptosis”. Advances in Enzyme Regulation 41 (1): 237–50. (2001). doi:10.1016/S0065-2571(00)00018-2. PMID 11384748.
“Mitochondrial activation of apoptosis”. Cell 116 (2 Suppl): S57–9, 2 p following S59. (January 2004). doi:10.1016/S0092-8674(04)00031-5. PMID 15055583.
“Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9”. The Biochemical Journal 405 (1): 11–9. (July 2007). doi:10.1042/BJ20070288. PMC 1925235. PMID 17437405.
“Protective effect of mangosteen extract against beta-amyloid-induced cytotoxicity, oxidative stress and altered proteome in SK-N-SH cells”. Journal of Proteome Research 9 (5): 2076–86. (May 2010). doi:10.1021/pr100049v. PMID 20232907.
“Serum caspase-3 p17 fragment is elevated in patients with ST-segment elevation myocardial infarction: a novel observation”. Journal of the American College of Cardiology 57 (2): 220–1. (January 2011). doi:10.1016/j.jacc.2010.08.628. PMID 21211695.
“Rehabilitation of a contract killer: caspase-3 directs stem cell differentiation”. Cell Stem Cell 2 (6): 515–6. (June 2008). doi:10.1016/j.stem.2008.05.013. PMID 18522841.
“Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. The Journal of Biological Chemistry 277 (16): 13430–7. (April 2002). doi:10.1074/jbc.M108029200. PMID 11832478.
“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”. Proceedings of the National Academy of Sciences of the United States of America 93 (25): 14486–91. (December 1996). doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078.
Selvakumar, P.; Sharma, RK. (May 2007). “Role of calpain and caspase system in the regulation of N-myristoyltransferase in human colon cancer (Review).”. Int J Mol Med 19 (5): 823–7. doi:10.3892/ijmm.19.5.823. PMID 17390089.
“Casper is a FADD- and caspase-related inducer of apoptosis”. Immunity 6 (6): 751–63. (June 1997). doi:10.1016/S1074-7613(00)80450-1. PMID 9208847.
“MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death”. Proceedings of the National Academy of Sciences of the United States of America 94 (21): 11333–8. (October 1997). doi:10.1073/pnas.94.21.11333. PMC 23459. PMID 9326610.
“The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation”. Proceedings of the National Academy of Sciences of the United States of America 98 (6): 3416–21. (March 2001). doi:10.1073/pnas.051378298. PMC 30668. PMID 11248093.
“Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells”. The EMBO Journal 18 (8): 2040–8. (April 1999). doi:10.1093/emboj/18.8.2040. PMC 1171288. PMID 10205158.
“Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis”. The EMBO Journal 18 (8): 2049–56. (April 1999). doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159.
“Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells”. The Biochemical Journal 364 (Pt 1): 41–7. (May 2002). doi:10.1042/bj3640041. PMC 1222543. PMID 11988074.
“Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis”. Biochemical and Biophysical Research Communications 288 (4): 981–9. (November 2001). doi:10.1006/bbrc.2001.5862. PMID 11689006.
“IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs”. Cancer Research 58 (23): 5315–20. (December 1998). PMID 9850056.
“An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7”. Biochemistry 40 (4): 1117–23. (January 2001). doi:10.1021/bi001603q. PMID 11170436.
“Caspase-mediated cleavage of TRAF3 in FasL-stimulated Jurkat-T cells”. Journal of Leukocyte Biology 69 (3): 490–6. (March 2001). PMID 11261798.
“TRAF1 is a substrate of caspases activated during tumor necrosis factor receptor-alpha-induced apoptosis”. The Journal of Biological Chemistry 276 (11): 8087–93. (March 2001). doi:10.1074/jbc.M009450200. PMID 11098060.
“Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death”. Proceedings of the National Academy of Sciences of the United States of America 98 (15): 8662–7. (July 2001). doi:10.1073/pnas.161506698. PMC 37492. PMID 11447297.
“The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites”. The Journal of Cell Biology 157 (1): 115–24. (April 2002). doi:10.1083/jcb.200108085. PMC 2173256. PMID 11927604.
“Structural basis for the inhibition of caspase-3 by XIAP”. Cell 104 (5): 791–800. (March 2001). doi:10.1016/S0092-8674(01)00274-4. PMID 11257232.
“The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases”. The EMBO Journal 16 (23): 6914–25. (December 1997). doi:10.1093/emboj/16.23.6914. PMC 1170295. PMID 9384571.
“X-linked IAP is a direct inhibitor of cell-death proteases”. Nature 388 (6639): 300–4. (July 1997). doi:10.1038/40901. PMID 9230442.
“X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes”. The Journal of Biological Chemistry 276 (29): 27058–63. (July 2001). doi:10.1074/jbc.M102415200. PMID 11359776.
“Identification of NRF2, a member of the NF-E2 family of transcription factors, as a substrate for caspase-3(-like) proteases”. Cell Death and Differentiation 6 (9): 865–72. (September 1999). doi:10.1038/sj.cdd.4400566. PMID 10510468.

pmc.ncbi.nlm.nih.gov

“Construction and analysis of a modular model of caspase activation in apoptosis”. Theoretical Biology & Medical Modelling 5 (1): 26. (2008). doi:10.1186/1742-4682-5-26. PMC 2672941. PMID 19077196.
“Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8”. The Biochemical Journal 350 (2): 563–8. (September 2000). doi:10.1042/0264-6021:3500563. PMC 1221285. PMID 10947972.
“Caspases: pharmacological manipulation of cell death”. The Journal of Clinical Investigation 115 (10): 2665–72. (October 2005). doi:10.1172/JCI26252. PMC 1236692. PMID 16200200.
“A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis”. The Biochemical Journal 424 (3): 335–45. (December 2009). doi:10.1042/BJ20090825. PMC 2805924. PMID 19788411.
“Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9”. The Biochemical Journal 405 (1): 11–9. (July 2007). doi:10.1042/BJ20070288. PMC 1925235. PMID 17437405.
“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”. Proceedings of the National Academy of Sciences of the United States of America 93 (25): 14486–91. (December 1996). doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078.
“MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death”. Proceedings of the National Academy of Sciences of the United States of America 94 (21): 11333–8. (October 1997). doi:10.1073/pnas.94.21.11333. PMC 23459. PMID 9326610.
“The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation”. Proceedings of the National Academy of Sciences of the United States of America 98 (6): 3416–21. (March 2001). doi:10.1073/pnas.051378298. PMC 30668. PMID 11248093.
“Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells”. The EMBO Journal 18 (8): 2040–8. (April 1999). doi:10.1093/emboj/18.8.2040. PMC 1171288. PMID 10205158.
“Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis”. The EMBO Journal 18 (8): 2049–56. (April 1999). doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159.
“Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells”. The Biochemical Journal 364 (Pt 1): 41–7. (May 2002). doi:10.1042/bj3640041. PMC 1222543. PMID 11988074.
“Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death”. Proceedings of the National Academy of Sciences of the United States of America 98 (15): 8662–7. (July 2001). doi:10.1073/pnas.161506698. PMC 37492. PMID 11447297.
“The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites”. The Journal of Cell Biology 157 (1): 115–24. (April 2002). doi:10.1083/jcb.200108085. PMC 2173256. PMID 11927604.
“The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases”. The EMBO Journal 16 (23): 6914–25. (December 1997). doi:10.1093/emboj/16.23.6914. PMC 1170295. PMID 9384571.

ncbi.nlm.nih.gov

Human PubMed Reference:
Mouse PubMed Reference:
“Entrez Gene: CASP3 caspase 3, apoptosis-related cysteine peptidase”. 2020年5月14日閲覧。

univ-montp2.fr (Global: low place; Japanese: low place)

orthomam.univ-montp2.fr

“ENSG00000164305_CASP3”. www.orthomam.univ-montp2.fr. 2020年5月14日閲覧。

wikipedia.org (Global: low place; Japanese: low place)

en.wikipedia.org

GRCm38: Ensembl release 89: ENSMUSG00000031628 - Ensembl, May 2017