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Volumn 80, Issue 11, 2015, Pages 1393-1405

Mechanisms of apoptosis

Author keywords

apoptosis; caspase pathways; membrane organelles; necrosis

Indexed keywords

APOPTOSIS REGULATORY PROTEIN; CASPASE 3;

EID: 84947437649     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297915110012     Document Type: Review
Times cited : (185)

References (90)
  • 1
    • 84988811185 scopus 로고    scopus 로고
    • How cell death shapes cancer
    • 4385913 1:CAS:528:DC%2BC2MXjvFOhurs%3D 25741600
    • Labi, V., and Erlacher, M. (2015) How cell death shapes cancer, Cell Death Dis., 6, e1675.
    • (2015) Cell Death Dis. , vol.6 , pp. e1675
    • Labi, V.1    Erlacher, M.2
  • 4
    • 84925337178 scopus 로고    scopus 로고
    • Triggers, inhibitors, mechanisms, and significance of eryptosis: The suicidal erythrocyte death
    • Lang, E., and Lang, F. (2015) Triggers, inhibitors, mechanisms, and significance of eryptosis: the suicidal erythrocyte death, Biomed. Res. Int., doi: 10.1155/2015/513518.
    • (2015) Biomed. Res. Int.
    • Lang, E.1    Lang, F.2
  • 5
    • 84898606305 scopus 로고    scopus 로고
    • Driving glioblastoma to drink
    • 1:CAS:528:DC%2BC2cXmslals74%3D 24725398
    • Gilbertson, R. J. (2014) Driving glioblastoma to drink, Cell, 157, 289-290.
    • (2014) Cell , vol.157 , pp. 289-290
    • Gilbertson, R.J.1
  • 7
    • 0035736138 scopus 로고    scopus 로고
    • If not apoptosis, then what? Treatment-induced senescence and mitotic catastrophe in tumor cells
    • 1:CAS:528:DC%2BD38Xkt1SjsL4%3D 11991684
    • Roninson, I. B., Broude, E. V., and Chang, B. D. (2001) If not apoptosis, then what? Treatment-induced senescence and mitotic catastrophe in tumor cells, Drug Resist. Updat., 4, 303-313.
    • (2001) Drug Resist. Updat. , vol.4 , pp. 303-313
    • Roninson, I.B.1    Broude, E.V.2    Chang, B.D.3
  • 8
    • 0036831681 scopus 로고    scopus 로고
    • Centrosome aberrations: Cause or consequence of cancer progression?
    • Nigg, E. A. (2002) Centrosome aberrations: cause or consequence of cancer progression? Nat. Rev. Cancer, 2, 815825.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 815825
    • Nigg, E.A.1
  • 9
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: Apoptosis, necrosis and autophagy
    • 1:CAS:528:DC%2BD2cXpsVOrtbk%3D 15530778
    • Edinger, A. L., and Thompson, C. B. (2004) Death by design: apoptosis, necrosis and autophagy, Curr. Opin. Cell Biol., 16, 663-669.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 10
    • 17144403458 scopus 로고    scopus 로고
    • Programmed cell death via mitochondria: Different modes of dying
    • 1:CAS:528:DC%2BD2MXislamsb4%3D
    • Bras, M., Queenan, B., and Susin, S. A. (2005) Programmed cell death via mitochondria: different modes of dying, Biochemistry (Moscow), 70, 231-239.
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 231-239
    • Bras, M.1    Queenan, B.2    Susin, S.A.3
  • 11
    • 45449107013 scopus 로고    scopus 로고
    • Elan vital, elan letal: One life but multiple deaths
    • 1:STN:280:DC%2BD1czosFyqsA%3D%3D 18552859
    • Kroemer, G., Tolkovsky, A. M., and Zakeri, Z. (2008) Elan vital, elan letal: one life but multiple deaths, Cell Death Differ., 15, 1089-1090.
    • (2008) Cell Death Differ. , vol.15 , pp. 1089-1090
    • Kroemer, G.1    Tolkovsky, A.M.2    Zakeri, Z.3
  • 12
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • 2175271 1:CAS:528:DC%2BD3cXmtVelsrs%3D 10953012
    • Nakagawa, T., and Yuan, J. (2000) Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis, J. Cell Biol., 150, 887-894.
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 14
    • 79952348567 scopus 로고    scopus 로고
    • Caspase-4 directly activates caspase-9 in endoplasmic reticulum stress-induced apoptosis in SH-SY5Y cells
    • 1:CAS:528:DC%2BC3MXivVKrtbo%3D 21282934
    • Yamamuro, A., Kishino, T., Ohshima, Y., Yoshioka, Y., Kimura, T., Kasai, A., and Maeda, S. (2011) Caspase-4 directly activates caspase-9 in endoplasmic reticulum stress-induced apoptosis in SH-SY5Y cells, J. Pharmacol. Sci., 115, 239-243.
    • (2011) J. Pharmacol. Sci. , vol.115 , pp. 239-243
    • Yamamuro, A.1    Kishino, T.2    Ohshima, Y.3    Yoshioka, Y.4    Kimura, T.5    Kasai, A.6    Maeda, S.7
  • 16
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri, K. F., and Kroemer, G. (2001) Organelle-specific initiation of cell death pathways, Nat. Cell Biol., 3, 255-263.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 255-263
    • Ferri, K.F.1    Kroemer, G.2
  • 18
    • 84884282500 scopus 로고    scopus 로고
    • Switching on p53: An essential role for protein phosphorylation?
    • Loughery, J., and Meek, D. (2013) Switching on p53: an essential role for protein phosphorylation? BioDiscovery, 8, 1.
    • (2013) BioDiscovery , vol.8 , pp. 1
    • Loughery, J.1    Meek, D.2
  • 19
    • 84938198407 scopus 로고    scopus 로고
    • Distinct target genes and effector processes appear to be critical for p53-activated responses to acute DNA damage versus p53-mediated tumor suppression
    • Valente, L., and Strasser, A. (2013) Distinct target genes and effector processes appear to be critical for p53-activated responses to acute DNA damage versus p53-mediated tumor suppression, BioDiscovery, 8, 3.
    • (2013) BioDiscovery , vol.8 , pp. 3
    • Valente, L.1    Strasser, A.2
  • 20
    • 62349098335 scopus 로고    scopus 로고
    • Caspases: Evolutionary aspects of their functions in vertebrates
    • 2779465 1:CAS:528:DC%2BD1MXkvVGlurc%3D 20735596
    • Sakamaki, K., and Satou, Y. (2009) Caspases: evolutionary aspects of their functions in vertebrates, J. Fish Biol., 74, 727-753.
    • (2009) J. Fish Biol. , vol.74 , pp. 727-753
    • Sakamaki, K.1    Satou, Y.2
  • 21
    • 84923233758 scopus 로고    scopus 로고
    • Comparative structural analysis of the caspase family with other clan CD cysteine peptidases
    • 4357240 1:CAS:528:DC%2BC2MXjtFCqur4%3D 25697094
    • McLuskey, K., and Mottram, J. C. (2015) Comparative structural analysis of the caspase family with other clan CD cysteine peptidases, Biochem. J., 466, 219-232.
    • (2015) Biochem. J. , vol.466 , pp. 219-232
    • McLuskey, K.1    Mottram, J.C.2
  • 22
    • 84877049921 scopus 로고    scopus 로고
    • Caspase-3 is involved in the signaling in erythroid differentiation by targeting late progenitors
    • 3642196 1:CAS:528:DC%2BC3sXnsFWqsbo%3D 23658722
    • Boehm, D., Mazurier, C., Giarratana, M. C., Darghouth, D., Faussat, A. M., Harmand, L., and Douay, L. (2013) Caspase-3 is involved in the signaling in erythroid differentiation by targeting late progenitors, PLoS One, 8, e62303.
    • (2013) PLoS One , vol.8 , pp. e62303
    • Boehm, D.1    Mazurier, C.2    Giarratana, M.C.3    Darghouth, D.4    Faussat, A.M.5    Harmand, L.6    Douay, L.7
  • 23
    • 84923119242 scopus 로고    scopus 로고
    • Old, new and emerging functions of caspases
    • 1:CAS:528:DC%2BC2cXitFKlt7nI 25526085
    • Shalini, S., Dorstyn, L., Dawar, S., and Kumar, S. (2015) Old, new and emerging functions of caspases, Cell Death Differ., 22, 526-539.
    • (2015) Cell Death Differ. , vol.22 , pp. 526-539
    • Shalini, S.1    Dorstyn, L.2    Dawar, S.3    Kumar, S.4
  • 24
    • 84915805120 scopus 로고    scopus 로고
    • Caspase crosstalk: Integration of apoptotic and innate immune signaling pathways
    • 1:CAS:528:DC%2BC2cXhvVamtrrF 25457353
    • Creagh, E. M. (2014) Caspase crosstalk: integration of apoptotic and innate immune signaling pathways, Trends Immunol., 35, 631-640.
    • (2014) Trends Immunol. , vol.35 , pp. 631-640
    • Creagh, E.M.1
  • 26
    • 84896690342 scopus 로고    scopus 로고
    • Apoptotic cell clearance: Basic biology and therapeutic potential
    • 4040260 1:CAS:528:DC%2BC2cXhs1ShsLc%3D 24481336
    • Poon, I. K., Lucas, C. D., Rossi, A. G., and Ravichandran, K. S. (2014) Apoptotic cell clearance: basic biology and therapeutic potential, Nat. Rev. Immunol., 14, 166-180.
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 166-180
    • Poon, I.K.1    Lucas, C.D.2    Rossi, A.G.3    Ravichandran, K.S.4
  • 27
    • 0038320321 scopus 로고    scopus 로고
    • The TNF superfamily
    • 1:CAS:528:DC%2BD3sXkt1Ghsrw%3D 12787557
    • Ware, C. F. (2003) The TNF superfamily, Cytokine Growth Factor Rev., 14, 181-184.
    • (2003) Cytokine Growth Factor Rev. , vol.14 , pp. 181-184
    • Ware, C.F.1
  • 28
    • 0041330433 scopus 로고    scopus 로고
    • Receptor-mediated choreography of life and death
    • Bhardway, A., and Aggarwal, B. B. (2003) Receptor-mediated choreography of life and death, J. Clin. Immunol., 23, 317-332.
    • (2003) J. Clin. Immunol. , vol.23 , pp. 317-332
    • Bhardway, A.1    Aggarwal, B.B.2
  • 30
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumor-necrosis factor superfamily
    • 1:CAS:528:DC%2BD38Xksl2ltr4%3D
    • Ashkenazi, A. (2002) Targeting death and decoy receptors of the tumor-necrosis factor superfamily, Nat. Cancer Rev., 2, 420-430.
    • (2002) Nat. Cancer Rev. , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 31
    • 67650741483 scopus 로고    scopus 로고
    • Mitochondrial targeting of tBid/Bax: A role for the TOM complex?
    • 1:CAS:528:DC%2BD1MXoslOitLs%3D 19521421
    • Ott, M., Norberg, E., Zhivotovsky, B., and Orrenius, S. (2009) Mitochondrial targeting of tBid/Bax: a role for the TOM complex? Cell Death Differ., 16, 1075-1082.
    • (2009) Cell Death Differ. , vol.16 , pp. 1075-1082
    • Ott, M.1    Norberg, E.2    Zhivotovsky, B.3    Orrenius, S.4
  • 32
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • 1:CAS:528:DC%2BD3sXlvFCgu7Y%3D 12887920
    • Micheau, O., and Tschopp, J. (2003) Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes, Cell, 114, 181-190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 33
    • 80053602333 scopus 로고    scopus 로고
    • The regulation of TNF signaling: What a tangled web we weave
    • Silke, J. (2011) The regulation of TNF signaling: what a tangled web we weave, Curr. Opin. Immunol., 23, 620626.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 620626
    • Silke, J.1
  • 34
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins forma death-inducing signaling complex (DISC) with the receptor
    • 394672 1:CAS:528:DyaK2MXpslamtr4%3D 8521815
    • Kischkel, F. C., Hellbardt, S., Behrmann, I., Germer M., Pawlita, M., Krammer, P. H., and Peter, M. E. (1995) Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins forma death-inducing signaling complex (DISC) with the receptor, EMBO J., 14, 5579-5588.
    • (1995) EMBO J. , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.G.M.3    Pawlita, M.4    Krammer, P.H.5    Peter, M.E.6
  • 37
    • 84863338304 scopus 로고    scopus 로고
    • Ubiquitination in signaling to and activation of IKK
    • 3549672 22435549
    • Chen, Z. J. (2012) Ubiquitination in signaling to and activation of IKK, Immunol. Rev., 246, 95-106.
    • (2012) Immunol. Rev. , vol.246 , pp. 95-106
    • Chen, Z.J.1
  • 40
    • 33750443289 scopus 로고    scopus 로고
    • IκB kinase complexes: Gateways to NF-κB activation and transcription
    • Scheidereit, C. (2006) IκB kinase complexes: gateways to NF-κB activation and transcription, Oncogene, 25, 66856705.
    • (2006) Oncogene , vol.25 , pp. 66856705
    • Scheidereit, C.1
  • 42
    • 77449147556 scopus 로고    scopus 로고
    • Regulation of TNFRSF and innate immune signaling complexes by TRAFs and cIAPs
    • 1:CAS:528:DC%2BD1MXhsFGnurnM 19680262
    • Silke, J., and Brink, R. (2010) Regulation of TNFRSF and innate immune signaling complexes by TRAFs and cIAPs, Cell Death Differ., 17, 35-45.
    • (2010) Cell Death Differ. , vol.17 , pp. 35-45
    • Silke, J.1    Brink, R.2
  • 43
    • 43049152912 scopus 로고    scopus 로고
    • TNF-A induces two distinct caspase-8 activation pathways
    • 1:CAS:528:DC%2BD1cXmsVOru78%3D 18485876
    • Wang, L., Du, F., and Wang, X. (2008) TNF-a induces two distinct caspase-8 activation pathways, Cell, 133, 693-703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 44
    • 0038320263 scopus 로고    scopus 로고
    • The signaling adaptors and pathways activated by TNF superfamily
    • Dempsey, P. W., Doyle, S. E., He, J. Q., and Cheng, G. (2003) The signaling adaptors and pathways activated by TNF superfamily, Cytokine Growth Factor Rev., 14, 193209.
    • (2003) Cytokine Growth Factor Rev. , vol.14 , pp. 193209
    • Dempsey, P.W.1    Doyle, S.E.2    He, J.Q.3    Cheng, G.4
  • 45
    • 3142683813 scopus 로고    scopus 로고
    • Apoptotic mechanisms in the control of erythropoiesis
    • 1:CAS:528:DC%2BD2cXkvF2kurY%3D 15208642
    • Testa, U. (2004) Apoptotic mechanisms in the control of erythropoiesis, Leukemia, 18, 1176-1199.
    • (2004) Leukemia , vol.18 , pp. 1176-1199
    • Testa, U.1
  • 46
    • 84928205948 scopus 로고    scopus 로고
    • The molecular relationships between apoptosis, autophagy, and necroptosis
    • Lalaoui, N., Lindqvist, L. M., Sandow, J. J., and Ekert, P. G. (2015) The molecular relationships between apoptosis, autophagy, and necroptosis, Semin. Cell Dev. Biol., 39, 6369.
    • (2015) Semin. Cell Dev. Biol. , vol.39 , pp. 6369
    • Lalaoui, N.1    Lindqvist, L.M.2    Sandow, J.J.3    Ekert, P.G.4
  • 48
    • 84928214039 scopus 로고    scopus 로고
    • Necroptosis: Pathway diversity and characteristics
    • 1:CAS:528:DC%2BC2MXivFaiu7s%3D 25683283
    • De Almagro, M. C., and Vucic, D. (2015) Necroptosis: pathway diversity and characteristics, Semin. Cell Dev. Biol., 39, 56-62.
    • (2015) Semin. Cell Dev. Biol. , vol.39 , pp. 56-62
    • De Almagro, M.C.1    Vucic, D.2
  • 49
    • 0036194529 scopus 로고    scopus 로고
    • Mitochondria as a pharmacological target
    • 1:CAS:528:DC%2BD38XislOgtb8%3D 11870261
    • Szewczyk, A., and Wojtcak, L. (2002) Mitochondria as a pharmacological target, Pharm Rev., 54, 101-127.
    • (2002) Pharm Rev. , vol.54 , pp. 101-127
    • Szewczyk, A.1    Wojtcak, L.2
  • 50
    • 84921938707 scopus 로고    scopus 로고
    • Curcumin induces apoptosis through mitochondrial pathway and caspases activation in human melanoma cells
    • 25262359
    • Jiang, A. J., Jiang, G., Li, L. T., and Zheng, J. N. (2014) Curcumin induces apoptosis through mitochondrial pathway and caspases activation in human melanoma cells, Mol. Biol. Rep., 42, 267-275.
    • (2014) Mol. Biol. Rep. , vol.42 , pp. 267-275
    • Jiang, A.J.1    Jiang, G.2    Li, L.T.3    Zheng, J.N.4
  • 51
    • 84907581445 scopus 로고    scopus 로고
    • Ruthenium(II) polypyridyl complexes induce BEL-7402 cell apoptosis by ROS-mediated mitochondrial pathway
    • 1:CAS:528:DC%2BC2cXhsFOqsL3N 25268891
    • Jiang, G. B., Zheng, X., Yao, J. H., Han, B. J., Li, W., Wang, J., Huang, H. L., and Liu, Y. J. (2014) Ruthenium(II) polypyridyl complexes induce BEL-7402 cell apoptosis by ROS-mediated mitochondrial pathway, J. Inorg. Biochem., 141, 170-179.
    • (2014) J. Inorg. Biochem. , vol.141 , pp. 170-179
    • Jiang, G.B.1    Zheng, X.2    Yao, J.H.3    Han, B.J.4    Li, W.5    Wang, J.6    Huang, H.L.7    Liu, Y.J.8
  • 52
    • 84907484374 scopus 로고    scopus 로고
    • Anthraquinone G503 induces apoptosis in gastric cancer cells through the mitochondrial pathway
    • 4182468 25268882
    • Huang, L., Zhang, T., Li, S., Duan, J., Ye, F., Li, H., She, Z., Gao, G., and Yang, X. (2014) Anthraquinone G503 induces apoptosis in gastric cancer cells through the mitochondrial pathway, PLoS One, 9, e108286.
    • (2014) PLoS One , vol.9 , pp. e108286
    • Huang, L.1    Zhang, T.2    Li, S.3    Duan, J.4    Ye, F.5    Li, H.6    She, Z.7    Gao, G.8    Yang, X.9
  • 53
    • 84911370231 scopus 로고    scopus 로고
    • Mitochondria-A bullseye in cancer therapy
    • 1:CAS:528:DC%2BC2cXhslGnsLjL 25315654
    • Gogvadze, V., and Zhivotovsky, B. (2014) Mitochondria-a bullseye in cancer therapy, Mitochondrion, 19, Pt. A, 1-2.
    • (2014) Mitochondrion , vol.19 , pp. 1-2
    • Gogvadze, V.1    Zhivotovsky, B.2
  • 54
    • 0033596980 scopus 로고    scopus 로고
    • An APAF1-cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • 1:CAS:528:DyaK1MXislGmur8%3D 10206961
    • Zou, H., Li, Y., Liu, X., and Wang, X. (1999) An APAF1-cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9, J. Biol. Chem., 274, 11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 55
    • 68949141833 scopus 로고    scopus 로고
    • Opening the doors to cytochrome c: Changes in mitochondrial shape and apoptosis
    • 1:CAS:528:DC%2BD1MXhtVentbvE 19393761
    • Scorrano, L. (2009) Opening the doors to cytochrome c: changes in mitochondrial shape and apoptosis, Int. J. Biochem. Cell Biol., 41, 1875-1883.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1875-1883
    • Scorrano, L.1
  • 56
    • 84877814906 scopus 로고    scopus 로고
    • The oxido-reductase activity of the apoptosis inducing factor: A promising pharmacological tool?
    • 1:CAS:528:DC%2BC3sXmt1ygtbY%3D 23116400
    • Ferreira, P., Villanueva, R., Cabon, L., Susin, S. A., and Medina, M. (2013) The oxido-reductase activity of the apoptosis inducing factor: a promising pharmacological tool? Curr. Pharm. Des., 19, 2628-2636.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 2628-2636
    • Ferreira, P.1    Villanueva, R.2    Cabon, L.3    Susin, S.A.4    Medina, M.5
  • 57
    • 84875738463 scopus 로고    scopus 로고
    • AIF, reactive oxygen species, and neurodegeneration: A "complex" problem
    • 3610861 1:CAS:528:DC%2BC3sXltVSltg%3D%3D 23246553
    • Polster, B. M. (2013) AIF, reactive oxygen species, and neurodegeneration: a "complex" problem, Neurochem. Int., 62, 695-702.
    • (2013) Neurochem. Int. , vol.62 , pp. 695-702
    • Polster, B.M.1
  • 58
    • 84900562472 scopus 로고    scopus 로고
    • Mitochondrial and postmitochondrial survival signaling in cancer
    • 1:CAS:528:DC%2BC2cXhtFWgsbg%3D 24333692
    • Yadav, N., and Chandra, D. (2014) Mitochondrial and postmitochondrial survival signaling in cancer, Mitochondrion, 16, 18-25.
    • (2014) Mitochondrion , vol.16 , pp. 18-25
    • Yadav, N.1    Chandra, D.2
  • 59
    • 79960845529 scopus 로고    scopus 로고
    • Bax: Addressed to kill
    • 1:CAS:528:DC%2BC3MXpt1Ogtr0%3D 21641962
    • Renault, T. T., and Manon, S. (2011) Bax: addressed to kill, Biochimie, 93, 1379-1391.
    • (2011) Biochimie , vol.93 , pp. 1379-1391
    • Renault, T.T.1    Manon, S.2
  • 60
    • 0027977928 scopus 로고
    • The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane
    • 1:CAS:528:DyaK2cXktVGlurc%3D 8043515
    • Lithgow, T., Van Driel, R., Bertram, J. F., and Strasser, A. (1994) The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane, Cell Growth Differ., 5, 411-417.
    • (1994) Cell Growth Differ. , vol.5 , pp. 411-417
    • Lithgow, T.V.1    Driel, R.2    Bertram, J.F.3    Strasser, A.4
  • 62
    • 84916618668 scopus 로고    scopus 로고
    • Molecular identity of the mitochondrial permeability transition pore and its role in ischemia-reperfusion injury
    • 1:CAS:528:DC%2BC2cXhsVOmsLfJ 25172387
    • Morciano, G., Giorgi, C., Bonora, M., Punzetti, S., Pavasini, R., Wieckowski, M. R., Campo, G., and Pinton, P. (2015) Molecular identity of the mitochondrial permeability transition pore and its role in ischemia-reperfusion injury, J. Mol. Cell. Cardiol., 78, 142-153.
    • (2015) J. Mol. Cell. Cardiol. , vol.78 , pp. 142-153
    • Morciano, G.1    Giorgi, C.2    Bonora, M.3    Punzetti, S.4    Pavasini, R.5    Wieckowski, M.R.6    Campo, G.7    Pinton, P.8
  • 63
    • 84946018343 scopus 로고    scopus 로고
    • Putting the pieces together: How is the mitochondrial pathway of apoptosis regulated in cancer and chemotherapy?
    • 4304082 25621172
    • Elkholi, R., Renault, T. T., Serasinghe, M. N., and Chipuk, J. E. (2014) Putting the pieces together: how is the mitochondrial pathway of apoptosis regulated in cancer and chemotherapy? Cancer Metab., 2, 16.
    • (2014) Cancer Metab. , vol.2 , pp. 16
    • Elkholi, R.1    Renault, T.T.2    Serasinghe, M.N.3    Chipuk, J.E.4
  • 64
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • 3049806 1:CAS:528:DC%2BD2cXntFWitQ%3D%3D 14749836
    • Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., and Wallace, D. C. (2004) The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore, Nature, 427, 461-465.
    • (2004) Nature , vol.427 , pp. 461-465
    • Kokoszka, J.E.1    Waymire, K.G.2    Levy, S.E.3    Sligh, J.E.4    Cai, J.5    Jones, D.P.6    MacGregor, G.R.7    Wallace, D.C.8
  • 65
    • 33746912767 scopus 로고    scopus 로고
    • The permeability transition pore complex in cancer cell death
    • 1:CAS:528:DC%2BD28Xnsl2hsb4%3D 16892087
    • Brenner, C., and Grimm, S. (2006) The permeability transition pore complex in cancer cell death, Oncogene, 25, 4744-4756.
    • (2006) Oncogene , vol.25 , pp. 4744-4756
    • Brenner, C.1    Grimm, S.2
  • 66
    • 84906254466 scopus 로고    scopus 로고
    • What makes you can also break you. Part III: Mitochondrial permeability transition pore formation by an uncoupling channel within the C-subunit ring of the F1FO ATP synthase?
    • 4153043 25232534
    • Chinopoulos, C., and Szabadkai, G. (2014) What makes you can also break you. Part III: mitochondrial permeability transition pore formation by an uncoupling channel within the C-subunit ring of the F1FO ATP synthase? Front. Oncol., 4, 235.
    • (2014) Front. Oncol. , vol.4 , pp. 235
    • Chinopoulos, C.1    Szabadkai, G.2
  • 67
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • 1:CAS:528:DC%2BD2MXislCnu7c%3D 15800626
    • Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., and Tsujimoto, Y. (2005) Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death, Nature, 434, 652-658.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 68
    • 4444253303 scopus 로고    scopus 로고
    • Survival and apoptosis signals in ER stress: The role of protein kinases
    • 1:CAS:528:DC%2BD2cXnsFSqsbw%3D 15363494
    • Kadowaki, H., Nishitoh, H., and Ichijo, H. (2004) Survival and apoptosis signals in ER stress: the role of protein kinases, J. Chem. Neuroanat., 28, 93-100.
    • (2004) J. Chem. Neuroanat. , vol.28 , pp. 93-100
    • Kadowaki, H.1    Nishitoh, H.2    Ichijo, H.3
  • 69
    • 84926024405 scopus 로고    scopus 로고
    • ER stress and ER stressmediated apoptosis are involved in manganese-induced neurotoxicity in the rat striatum in vivo
    • 1:CAS:528:DC%2BC2MXjvVOqsLo%3D 25732873
    • Wang, T., Yang, D., Li, X., Zhang, H., Zhao, P., Fu, J., Yao, B., and Zhou, Z. (2015) ER stress and ER stressmediated apoptosis are involved in manganese-induced neurotoxicity in the rat striatum in vivo, Neurotoxicology, 48, 109-119.
    • (2015) Neurotoxicology , vol.48 , pp. 109-119
    • Wang, T.1    Yang, D.2    Li, X.3    Zhang, H.4    Zhao, P.5    Fu, J.6    Yao, B.7    Zhou, Z.8
  • 70
    • 84929300310 scopus 로고    scopus 로고
    • The antioxidant machinery of the endoplasmic reticulum: Protection and signaling
    • Delaunay-Moisan, A., and Appenzeller-Herzog, C. (2015) The antioxidant machinery of the endoplasmic reticulum: protection and signaling, Free Radic. Biol. Med., 83, 341351.
    • (2015) Free Radic. Biol. Med. , vol.83 , pp. 341351
    • Delaunay-Moisan, A.1    Appenzeller-Herzog, C.2
  • 71
    • 0037810844 scopus 로고    scopus 로고
    • Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis
    • 2172724 1:CAS:528:DC%2BD3sXltleksLw%3D 12847083
    • Zong, W. X., Li, C., Hatzivassiliou, G., Lindsten, T., Yu, Q. C., Yuan, J., and Thompson, C. B. (2003) Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis, J. Cell Biol., 162, 59-69.
    • (2003) J. Cell Biol. , vol.162 , pp. 59-69
    • Zong, W.X.1    Li, C.2    Hatzivassiliou, G.3    Lindsten, T.4    Yu, Q.C.5    Yuan, J.6    Thompson, C.B.7
  • 72
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • 1:CAS:528:DC%2BD2cXit12nur4%3D 14765132
    • Rao, R. V., Ellerby, H. M., and Bredesen, D. E. (2004) Coupling endoplasmic reticulum stress to the cell death program, Cell Death Differ., 11, 372-380.
    • (2004) Cell Death Differ. , vol.11 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 73
    • 84887023145 scopus 로고    scopus 로고
    • CDIP1-BAP31 complex transduces apoptotic signals from endoplasmic reticulum to mitochondria under endoplasmic reticulum stress
    • 1:CAS:528:DC%2BC3sXhs1CrtrfI 24139803
    • Namba, T., Tian, F., Chu, K., Hwang, S. Y., Yoon, K. W., Byun, S., Hiraki, M., Mandinova, A., and Lee, S. W. (2013) CDIP1-BAP31 complex transduces apoptotic signals from endoplasmic reticulum to mitochondria under endoplasmic reticulum stress, Cell Rep., 5, 331-339.
    • (2013) Cell Rep. , vol.5 , pp. 331-339
    • Namba, T.1    Tian, F.2    Chu, K.3    Hwang, S.Y.4    Yoon, K.W.5    Byun, S.6    Hiraki, M.7    Mandinova, A.8    Lee, S.W.9
  • 74
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2dependent mechanism in response to the ER stress
    • 1:CAS:528:DC%2BD3MXjt12rsr0%3D 11278723
    • Yoneda, T., Imaizumi, K., Oono, K., Yui, D., Gomi, F., Katayama, T., and Tohyama, M. (2001) Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2dependent mechanism in response to the ER stress, J. Biol. Chem., 276, 13935-13940.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 75
    • 4444338911 scopus 로고    scopus 로고
    • Caspases involved in ER stress-mediated cell death
    • 1:CAS:528:DC%2BD2cXnsFSqsb0%3D 15363495
    • Momoi, T. (2004) Caspases involved in ER stress-mediated cell death, J. Chem. Neuroanat., 28, 101-105.
    • (2004) J. Chem. Neuroanat. , vol.28 , pp. 101-105
    • Momoi, T.1
  • 76
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • 1:CAS:528:DC%2BC38XnvVeltQ%3D%3D 22251901
    • Hetz, C. (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond, Nat. Rev. Mol. Cell Biol., 13, 89-102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 77
    • 84907539353 scopus 로고    scopus 로고
    • Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 1. An overview
    • Dufey, E., Sepulveda, D., Rojas-Rivera, D., and Hetz, C. (2014) Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 1. An overview, Am. J. Physiol. Cell Physiol., 307, 582-594.
    • (2014) Am. J. Physiol. Cell Physiol. , vol.307 , pp. 582-594
    • Dufey, E.1    Sepulveda, D.2    Rojas-Rivera, D.3    Hetz, C.4
  • 78
    • 9644295726 scopus 로고    scopus 로고
    • Translocation of Bim to the endoplasmic reticulum (ER) mediates ER stress signaling for activation of caspase-12 during ER stress-induced apoptosis
    • 1:CAS:528:DC%2BD2cXhtVWjs7bF 15452118
    • Morishima, N., Nakanishi, K., Tsuchiya, K., Shibata, T., and Seiwa, E. (2004) Translocation of Bim to the endoplasmic reticulum (ER) mediates ER stress signaling for activation of caspase-12 during ER stress-induced apoptosis, J. Biol. Chem., 279, 50375-50381.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50375-50381
    • Morishima, N.1    Nakanishi, K.2    Tsuchiya, K.3    Shibata, T.4    Seiwa, E.5
  • 79
    • 35848969791 scopus 로고    scopus 로고
    • ER stress signaling and the BCL-2 family of proteins: From adaptation to irreversible cellular damage
    • 1:CAS:528:DC%2BD2sXht1GrsLrI 17854276
    • Hetz, C. A. (2007) ER stress signaling and the BCL-2 family of proteins: from adaptation to irreversible cellular damage, Antioxid. Redox Signal., 9, 2345-2355.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2345-2355
    • Hetz, C.A.1
  • 80
    • 84879033457 scopus 로고    scopus 로고
    • Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis
    • 3682588 1:CAS:528:DC%2BC3sXpsFamtL4%3D 23661706
    • Li, C., Wei, J., Li, Y., He, X., Zhou, Q., Yan, J., Zhang, J., Liu, Y., Liu, Y., and Shu, H. B. (2013) Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis, J. Biol. Chem., 288, 17908-17917.
    • (2013) J. Biol. Chem. , vol.288 , pp. 17908-17917
    • Li, C.1    Wei, J.2    Li, Y.3    He, X.4    Zhou, Q.5    Yan, J.6    Zhang, J.7    Liu, Y.8    Liu, Y.9    Shu, H.B.10
  • 82
    • 0042266400 scopus 로고    scopus 로고
    • Death from within: Apoptosis and the secretory pathway
    • 1:CAS:528:DC%2BD3sXlvVGjtro%3D 12892786
    • Maag, R. S., Hicks, S. W., and Machamer, C. E. (2003) Death from within: apoptosis and the secretory pathway, Curr. Opin. Cell Biol., 15, 456-461.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 456-461
    • Maag, R.S.1    Hicks, S.W.2    MacHamer, C.E.3
  • 83
    • 84856853692 scopus 로고    scopus 로고
    • Inactivation of ceramide transfer protein during pro-apoptotic stress by Golgi disassembly and caspase cleavage
    • 3354954 1:CAS:528:DC%2BC38Xit1Oksbk%3D 22129459
    • Chandran, S., and Machamer, C. E. (2012) Inactivation of ceramide transfer protein during pro-apoptotic stress by Golgi disassembly and caspase cleavage, Biochem. J., 442, 391-401.
    • (2012) Biochem. J. , vol.442 , pp. 391-401
    • Chandran, S.1    MacHamer, C.E.2
  • 84
    • 0013865801 scopus 로고
    • Functions of lysosomes
    • 1:CAS:528:DyaF28Xkt1entrc%3D 5322983
    • De Duve, C., and Wattiaux, R. (1966) Functions of lysosomes, Annu. Rev. Physiol., 28, 435-492.
    • (1966) Annu. Rev. Physiol. , vol.28 , pp. 435-492
    • De Duve, C.1    Wattiaux, R.2
  • 85
    • 84878643872 scopus 로고    scopus 로고
    • Lysosomal cell death at a glance
    • 1:CAS:528:DC%2BC3sXhtFWjtL3O 23720375
    • Aits, S., and Jaattela, M. (2013) Lysosomal cell death at a glance, J. Cell Sci., 126 (Pt. 9), 1905-1912.
    • (2013) J. Cell Sci. , vol.126 , pp. 1905-1912
    • Aits, S.1    Jaattela, M.2
  • 86
    • 84861671713 scopus 로고    scopus 로고
    • Lysosomal pathways to cell death and their therapeutic applications
    • 22465226
    • Cesen, M. H., Pegan, K., Spes, A., and Turk, B. (2012) Lysosomal pathways to cell death and their therapeutic applications, Exp. Cell Res., 318, 1245-1251.
    • (2012) Exp. Cell Res. , vol.318 , pp. 1245-1251
    • Cesen, M.H.1    Pegan, K.2    Spes, A.3    Turk, B.4
  • 87
    • 44449145862 scopus 로고    scopus 로고
    • Redox signaling and cancer: The role of "labile" iron
    • 1:CAS:528:DC%2BD1cXmsFKlu7k%3D 18374479
    • Galaris, D., Skiada, V., and Barbouti, A. (2008) Redox signaling and cancer: the role of "labile" iron, Cancer Lett., 266, 21-29.
    • (2008) Cancer Lett. , vol.266 , pp. 21-29
    • Galaris, D.1    Skiada, V.2    Barbouti, A.3
  • 89
    • 84921342043 scopus 로고    scopus 로고
    • Cell death controlling complexes and their potential therapeutic role
    • 1:CAS:528:DC%2BC2cXhsl2gtrfO 25323133
    • Zamaraev, A. V., Kopeina, G. S., Zhivotovsky, B., and Lavrik, I. N. (2015) Cell death controlling complexes and their potential therapeutic role, Cell Mol. Life Sci., 72, 505-517.
    • (2015) Cell Mol. Life Sci. , vol.72 , pp. 505-517
    • Zamaraev, A.V.1    Kopeina, G.S.2    Zhivotovsky, B.3    Lavrik, I.N.4


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