메뉴 건너뛰기




Volumn 367, Issue 2, 2015, Pages 108-112

Cell death decision by p53 via control of the mitochondrial membrane

Author keywords

Apoptosis; Mitochondria; Necroptosis; Necrosis; P53

Indexed keywords

CYCLOPHILIN D; DYNAMIN RELATED PROTEIN 1; MICRORNA; MITOCHONDRIAL PROTEIN; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BID; PROTEIN MCL 1; PROTEIN MDM2; PROTEIN NOXA; PROTEIN P53; PUMA PROTEIN; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN;

EID: 84939266852     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2015.07.019     Document Type: Review
Times cited : (90)

References (61)
  • 1
    • 26444489119 scopus 로고    scopus 로고
    • Connected to death: the (unexpurgated) mitochondrial pathway of apoptosis
    • Spierings D., et al. Connected to death: the (unexpurgated) mitochondrial pathway of apoptosis. Science 2005, 310(5745):66-67.
    • (2005) Science , vol.310 , Issue.5745 , pp. 66-67
    • Spierings, D.1
  • 2
    • 33745149291 scopus 로고    scopus 로고
    • P53 regulates mitochondrial respiration
    • Matoba S., et al. p53 regulates mitochondrial respiration. Science 2006, 312(5780):1650-1653.
    • (2006) Science , vol.312 , Issue.5780 , pp. 1650-1653
    • Matoba, S.1
  • 3
    • 84922935178 scopus 로고    scopus 로고
    • Effect of p53 on mitochondrial morphology, import and assembly in skeletal muscle
    • Saleem A., et al. Effect of p53 on mitochondrial morphology, import and assembly in skeletal muscle. Am. J. Physiol. Cell Physiol 2015, 308(4):C319-C329.
    • (2015) Am. J. Physiol. Cell Physiol , vol.308 , Issue.4 , pp. C319-C329
    • Saleem, A.1
  • 4
    • 84906514892 scopus 로고    scopus 로고
    • Necroptosis: is there a role for mitochondria?
    • Marshall K.D., Baines C.P. Necroptosis: is there a role for mitochondria?. Front. Physiol 2014, 5:323.
    • (2014) Front. Physiol , vol.5 , pp. 323
    • Marshall, K.D.1    Baines, C.P.2
  • 5
    • 79952702745 scopus 로고    scopus 로고
    • Is mPTP the gatekeeper for necrosis, apoptosis, or both?
    • Kinnally K.W., et al. Is mPTP the gatekeeper for necrosis, apoptosis, or both?. Biochim. Biophys. Acta 2011, 1813(4):616-622.
    • (2011) Biochim. Biophys. Acta , vol.1813 , Issue.4 , pp. 616-622
    • Kinnally, K.W.1
  • 6
    • 84926387317 scopus 로고    scopus 로고
    • Ferroptosis as a p53-mediated activity during tumour suppression
    • Jiang L., et al. Ferroptosis as a p53-mediated activity during tumour suppression. Nature 2015, 520(7545):57-62.
    • (2015) Nature , vol.520 , Issue.7545 , pp. 57-62
    • Jiang, L.1
  • 7
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano K., Vousden K.H. PUMA, a novel proapoptotic gene, is induced by p53. Mol. Cell 2001, 7(3):683-694.
    • (2001) Mol. Cell , vol.7 , Issue.3 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 8
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death
    • Wei M.C., et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001, 292(5517):727-730.
    • (2001) Science , vol.292 , Issue.5517 , pp. 727-730
    • Wei, M.C.1
  • 9
    • 0037093091 scopus 로고    scopus 로고
    • P53AIP1 regulates the mitochondrial apoptotic pathway
    • Matsuda K., et al. p53AIP1 regulates the mitochondrial apoptotic pathway. Cancer Res 2002, 62(10):2883-2889.
    • (2002) Cancer Res , vol.62 , Issue.10 , pp. 2883-2889
    • Matsuda, K.1
  • 10
    • 0037349289 scopus 로고    scopus 로고
    • P53 has a direct apoptogenic role at the mitochondria
    • Mihara M., et al. p53 has a direct apoptogenic role at the mitochondria. Mol. Cell 2003, 11(3):577-590.
    • (2003) Mol. Cell , vol.11 , Issue.3 , pp. 577-590
    • Mihara, M.1
  • 11
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk J.E., et al. Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 2004, 303(5660):1010-1014.
    • (2004) Science , vol.303 , Issue.5660 , pp. 1010-1014
    • Chipuk, J.E.1
  • 12
    • 2342553892 scopus 로고    scopus 로고
    • Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex
    • Leu J.I., et al. Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex. Nat. Cell Biol 2004, 6(5):443-450.
    • (2004) Nat. Cell Biol , vol.6 , Issue.5 , pp. 443-450
    • Leu, J.I.1
  • 13
    • 24644436766 scopus 로고    scopus 로고
    • PUMA couples the nuclear and cytoplasmic proapoptotic function of p53
    • Chipuk J.E., et al. PUMA couples the nuclear and cytoplasmic proapoptotic function of p53. Science 2005, 309(5741):1732-1735.
    • (2005) Science , vol.309 , Issue.5741 , pp. 1732-1735
    • Chipuk, J.E.1
  • 14
    • 33847276654 scopus 로고    scopus 로고
    • Monoubiquitylation promotes mitochondrial p53 translocation
    • Marchenko N.D., et al. Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J. 2007, 26(4):923-934.
    • (2007) EMBO J. , vol.26 , Issue.4 , pp. 923-934
    • Marchenko, N.D.1
  • 15
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk J.E., Green D.R. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?. Trends Cell Biol 2008, 18(4):157-164.
    • (2008) Trends Cell Biol , vol.18 , Issue.4 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 16
    • 69749112731 scopus 로고    scopus 로고
    • PUMA cooperates with direct activator proteins to promote mitochondrial outer membrane permeabilization and apoptosis
    • Chipuk J.E., Green D.R. PUMA cooperates with direct activator proteins to promote mitochondrial outer membrane permeabilization and apoptosis. Cell Cycle 2009, 8(17):2692-2696.
    • (2009) Cell Cycle , vol.8 , Issue.17 , pp. 2692-2696
    • Chipuk, J.E.1    Green, D.R.2
  • 17
    • 77449091505 scopus 로고    scopus 로고
    • BclxL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain
    • Hagn F., et al. BclxL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain. J. Biol. Chem 2010, 285(5):3439-3450.
    • (2010) J. Biol. Chem , vol.285 , Issue.5 , pp. 3439-3450
    • Hagn, F.1
  • 18
    • 84902009201 scopus 로고    scopus 로고
    • The DNA-binding domain mediates both nuclear and cytosolic functions of p53
    • Follis A.V., et al. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nat. Struct. Mol. Biol 2014, 21(6):535-543.
    • (2014) Nat. Struct. Mol. Biol , vol.21 , Issue.6 , pp. 535-543
    • Follis, A.V.1
  • 19
    • 77957105977 scopus 로고    scopus 로고
    • Molecular mechanisms of necroptosis: an ordered cellular explosion
    • Vandenabeele P., et al. Molecular mechanisms of necroptosis: an ordered cellular explosion. Nat. Rev. Mol. Cell Biol 2010, 11(10):700-714.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , Issue.10 , pp. 700-714
    • Vandenabeele, P.1
  • 20
    • 77951251430 scopus 로고    scopus 로고
    • Necroptosis as an alternative form of programmed cell death
    • Christofferson D.E., Yuan J. Necroptosis as an alternative form of programmed cell death. Curr. Opin. Cell Biol 2010, 22(2):263-268.
    • (2010) Curr. Opin. Cell Biol , vol.22 , Issue.2 , pp. 263-268
    • Christofferson, D.E.1    Yuan, J.2
  • 21
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang Z., et al. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 2012, 148(1-2):228-243.
    • (2012) Cell , vol.148 , Issue.1-2 , pp. 228-243
    • Wang, Z.1
  • 22
    • 84862675016 scopus 로고    scopus 로고
    • P53 opens the mitochondrial permeability transition pore to trigger necrosis
    • Vaseva A.V., et al. p53 opens the mitochondrial permeability transition pore to trigger necrosis. Cell 2012, 149(7):1536-1548.
    • (2012) Cell , vol.149 , Issue.7 , pp. 1536-1548
    • Vaseva, A.V.1
  • 23
    • 84899830906 scopus 로고    scopus 로고
    • DAPK1-p53 interaction converges necrotic and apoptotic pathways of ischemic neuronal death
    • Pei L., et al. DAPK1-p53 interaction converges necrotic and apoptotic pathways of ischemic neuronal death. J. Neurosci 2014, 34(19):6546-6556.
    • (2014) J. Neurosci , vol.34 , Issue.19 , pp. 6546-6556
    • Pei, L.1
  • 24
    • 78651232227 scopus 로고    scopus 로고
    • MiR-499 regulates mitochondrial dynamics by targeting calcineurin and dynamin-related protein-1
    • Wang J.X., et al. miR-499 regulates mitochondrial dynamics by targeting calcineurin and dynamin-related protein-1. Nat. Med 2010, 17(1):71-78.
    • (2010) Nat. Med , vol.17 , Issue.1 , pp. 71-78
    • Wang, J.X.1
  • 25
    • 76749157966 scopus 로고    scopus 로고
    • MiR-30 regulates mitochondrial fission through targeting p53 and the dynamin-related protein-1 pathway
    • Li J., et al. miR-30 regulates mitochondrial fission through targeting p53 and the dynamin-related protein-1 pathway. PLoS Genet 2010, 6(1):e1000795.
    • (2010) PLoS Genet , vol.6 , Issue.1 , pp. e1000795
    • Li, J.1
  • 26
    • 84902329877 scopus 로고    scopus 로고
    • Drp1 stabilizes p53 on the mitochondria to trigger necrosis under oxidative stress conditions in vitro and in vivo
    • Guo X., Sesaki H., Qi X. Drp1 stabilizes p53 on the mitochondria to trigger necrosis under oxidative stress conditions in vitro and in vivo. Biochem. J. 2014, 461(1):137-146.
    • (2014) Biochem. J. , vol.461 , Issue.1 , pp. 137-146
    • Guo, X.1    Sesaki, H.2    Qi, X.3
  • 27
    • 34250372956 scopus 로고    scopus 로고
    • RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels
    • Yagoda N., et al. RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels. Nature 2007, 447(7146):864-868.
    • (2007) Nature , vol.447 , Issue.7146 , pp. 864-868
    • Yagoda, N.1
  • 28
    • 84861541814 scopus 로고    scopus 로고
    • Ferroptosis: an iron-dependent form of nonapoptotic cell death
    • Dixon S.J., et al. Ferroptosis: an iron-dependent form of nonapoptotic cell death. Cell 2012, 149(5):1060-1072.
    • (2012) Cell , vol.149 , Issue.5 , pp. 1060-1072
    • Dixon, S.J.1
  • 29
    • 0033229866 scopus 로고    scopus 로고
    • P53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2
    • Li P.F., Dietz R., von Harsdorf R. p53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2. EMBO J. 1999, 18(21):6027-6036.
    • (1999) EMBO J. , vol.18 , Issue.21 , pp. 6027-6036
    • Li, P.F.1    Dietz, R.2    von Harsdorf, R.3
  • 30
    • 33746883125 scopus 로고    scopus 로고
    • P53 and Nur77/TR3 - transcription factors that directly target mitochondria for cell death induction
    • Moll U.M., Marchenko N., Zhang X.K. p53 and Nur77/TR3 - transcription factors that directly target mitochondria for cell death induction. Oncogene 2006, 25(34):4725-4743.
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4725-4743
    • Moll, U.M.1    Marchenko, N.2    Zhang, X.K.3
  • 31
    • 75949105922 scopus 로고    scopus 로고
    • The BCL-2 family reunion
    • Chipuk J.E., et al. The BCL-2 family reunion. Mol. Cell 2010, 37(3):299-310.
    • (2010) Mol. Cell , vol.37 , Issue.3 , pp. 299-310
    • Chipuk, J.E.1
  • 32
    • 79958834471 scopus 로고    scopus 로고
    • Differential regulation of the proapoptotic multidomain protein Bak by p53 and p73 at the promoter level
    • Graupner V., et al. Differential regulation of the proapoptotic multidomain protein Bak by p53 and p73 at the promoter level. Cell Death Differ 2011, 18(7):1130-1139.
    • (2011) Cell Death Differ , vol.18 , Issue.7 , pp. 1130-1139
    • Graupner, V.1
  • 33
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T., Reed J.C. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 1995, 80(2):293-299.
    • (1995) Cell , vol.80 , Issue.2 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 34
    • 0034640281 scopus 로고    scopus 로고
    • Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis
    • Oda E., et al. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. Science 2000, 288(5468):1053-1058.
    • (2000) Science , vol.288 , Issue.5468 , pp. 1053-1058
    • Oda, E.1
  • 35
    • 0141818136 scopus 로고    scopus 로고
    • Integral role of Noxa in p53-mediated apoptotic response
    • Shibue T., et al. Integral role of Noxa in p53-mediated apoptotic response. Genes Dev 2003, 17(18):2233-2238.
    • (2003) Genes Dev , vol.17 , Issue.18 , pp. 2233-2238
    • Shibue, T.1
  • 36
    • 33646826684 scopus 로고    scopus 로고
    • WT p53, but not tumor-derived mutants, bind to Bcl2 via the DNA binding domain and induce mitochondrial permeabilization
    • Tomita Y., et al. WT p53, but not tumor-derived mutants, bind to Bcl2 via the DNA binding domain and induce mitochondrial permeabilization. J. Biol. Chem 2006, 281(13):8600-8606.
    • (2006) J. Biol. Chem , vol.281 , Issue.13 , pp. 8600-8606
    • Tomita, Y.1
  • 37
    • 33749846225 scopus 로고    scopus 로고
    • Role of Bax and Bak in mitochondrial morphogenesis
    • Karbowski M., et al. Role of Bax and Bak in mitochondrial morphogenesis. Nature 2006, 443(7112):658-662.
    • (2006) Nature , vol.443 , Issue.7112 , pp. 658-662
    • Karbowski, M.1
  • 38
    • 84896737071 scopus 로고    scopus 로고
    • Structural insights into the transcription-independent apoptotic pathway of p53
    • Chi S.W. Structural insights into the transcription-independent apoptotic pathway of p53. BMB Rep 2014, 47(3):167-172.
    • (2014) BMB Rep , vol.47 , Issue.3 , pp. 167-172
    • Chi, S.W.1
  • 39
    • 0028335717 scopus 로고
    • Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo
    • Miyashita T., et al. Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo. Oncogene 1994, 9(6):1799-1805.
    • (1994) Oncogene , vol.9 , Issue.6 , pp. 1799-1805
    • Miyashita, T.1
  • 40
    • 25444520537 scopus 로고    scopus 로고
    • MiR-15 and miR-16 induce apoptosis by targeting BCL2
    • Cimmino A., et al. miR-15 and miR-16 induce apoptosis by targeting BCL2. Proc. Natl. Acad. Sci. U.S.A. 2005, 102(39):13944-13949.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.39 , pp. 13944-13949
    • Cimmino, A.1
  • 41
    • 44949249814 scopus 로고    scopus 로고
    • MiR-15b and miR-16 modulate multidrug resistance by targeting BCL2 in human gastric cancer cells
    • Xia L., et al. miR-15b and miR-16 modulate multidrug resistance by targeting BCL2 in human gastric cancer cells. Int. J. Cancer 2008, 123(2):372-379.
    • (2008) Int. J. Cancer , vol.123 , Issue.2 , pp. 372-379
    • Xia, L.1
  • 42
    • 77955619456 scopus 로고    scopus 로고
    • MiR-181b modulates multidrug resistance by targeting BCL2 in human cancer cell lines
    • Zhu W., et al. miR-181b modulates multidrug resistance by targeting BCL2 in human cancer cell lines. Int. J. Cancer 2010, 127(11):2520-2529.
    • (2010) Int. J. Cancer , vol.127 , Issue.11 , pp. 2520-2529
    • Zhu, W.1
  • 43
    • 84871276136 scopus 로고    scopus 로고
    • MiR-1915 inhibits Bcl-2 to modulate multidrug resistance by increasing drug-sensitivity in human colorectal carcinoma cells
    • Xu K., et al. miR-1915 inhibits Bcl-2 to modulate multidrug resistance by increasing drug-sensitivity in human colorectal carcinoma cells. Mol. Carcinog 2011, 52(1):70-78.
    • (2011) Mol. Carcinog , vol.52 , Issue.1 , pp. 70-78
    • Xu, K.1
  • 44
    • 84859779031 scopus 로고    scopus 로고
    • MiR-200bc/429 cluster modulates multidrug resistance of human cancer cell lines by targeting BCL2 and XIAP
    • Zhu W., et al. miR-200bc/429 cluster modulates multidrug resistance of human cancer cell lines by targeting BCL2 and XIAP. Cancer Chemother. Pharmacol 2011, 69(3):723-731.
    • (2011) Cancer Chemother. Pharmacol , vol.69 , Issue.3 , pp. 723-731
    • Zhu, W.1
  • 45
    • 84903776044 scopus 로고    scopus 로고
    • Tumor suppressor p53 induces miR-1915 processing to inhibit Bcl-2 in the apoptotic response to DNA damage
    • Nakazawa K., Dashzeveg N., Yoshida K. Tumor suppressor p53 induces miR-1915 processing to inhibit Bcl-2 in the apoptotic response to DNA damage. FEBS J. 2014, 281(13):2937-2944.
    • (2014) FEBS J. , vol.281 , Issue.13 , pp. 2937-2944
    • Nakazawa, K.1    Dashzeveg, N.2    Yoshida, K.3
  • 46
    • 84892599654 scopus 로고    scopus 로고
    • Induction of amphiregulin by p53 promotes apoptosis via control of microRNA biogenesis in response to DNA damage
    • Taira N., et al. Induction of amphiregulin by p53 promotes apoptosis via control of microRNA biogenesis in response to DNA damage. Proc. Natl. Acad. Sci. U.S.A. 2014, 111(2):717-722.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , Issue.2 , pp. 717-722
    • Taira, N.1
  • 47
    • 70349558133 scopus 로고    scopus 로고
    • MiR-34a, a microRNA up-regulated in a double transgenic mouse model of Alzheimer's disease, inhibits bcl2 translation
    • Wang X., et al. miR-34a, a microRNA up-regulated in a double transgenic mouse model of Alzheimer's disease, inhibits bcl2 translation. Brain Res. Bull 2009, 80(4-5):268-273.
    • (2009) Brain Res. Bull , vol.80 , Issue.4-5 , pp. 268-273
    • Wang, X.1
  • 48
    • 34547458550 scopus 로고    scopus 로고
    • P53-mediated activation of miRNA34 candidate tumor-suppressor genes
    • Bommer G.T., et al. p53-mediated activation of miRNA34 candidate tumor-suppressor genes. Curr. Biol 2007, 17(15):1298-1307.
    • (2007) Curr. Biol , vol.17 , Issue.15 , pp. 1298-1307
    • Bommer, G.T.1
  • 49
    • 84900037375 scopus 로고    scopus 로고
    • Downregulation of Bcl-2 expression by miR-34a mediates palmitate-induced Min6 cells apoptosis
    • 258695
    • Lin X., et al. Downregulation of Bcl-2 expression by miR-34a mediates palmitate-induced Min6 cells apoptosis. J. Diabetes Res 2014, 2014. 258695.
    • (2014) J. Diabetes Res , vol.2014
    • Lin, X.1
  • 50
    • 67749143728 scopus 로고    scopus 로고
    • Modulation of microRNA processing by p53
    • Suzuki H.I., et al. Modulation of microRNA processing by p53. Nature 2009, 460(7254):529-533.
    • (2009) Nature , vol.460 , Issue.7254 , pp. 529-533
    • Suzuki, H.I.1
  • 51
    • 84874044758 scopus 로고    scopus 로고
    • PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis
    • Follis A.V., et al. PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis. Nat. Chem. Biol 2013, 9(3):163-168.
    • (2013) Nat. Chem. Biol , vol.9 , Issue.3 , pp. 163-168
    • Follis, A.V.1
  • 52
    • 3242690522 scopus 로고    scopus 로고
    • In vivo mitochondrial p53 translocation triggers a rapid first wave of cell death in response to DNA damage that can precede p53 target gene activation
    • Erster S., et al. In vivo mitochondrial p53 translocation triggers a rapid first wave of cell death in response to DNA damage that can precede p53 target gene activation. Mol. Cell. Biol 2004, 24(15):6728-6741.
    • (2004) Mol. Cell. Biol , vol.24 , Issue.15 , pp. 6728-6741
    • Erster, S.1
  • 53
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl-2 family proteins induces regression of solid tumours
    • Oltersdorf T., et al. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature 2005, 435(7042):677-681.
    • (2005) Nature , vol.435 , Issue.7042 , pp. 677-681
    • Oltersdorf, T.1
  • 54
    • 42449114966 scopus 로고    scopus 로고
    • Transcriptional control of human p53-regulated genes
    • Riley T., et al. Transcriptional control of human p53-regulated genes. Nat. Rev. Mol. Cell Biol 2008, 9(5):402-412.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , Issue.5 , pp. 402-412
    • Riley, T.1
  • 55
    • 85006263913 scopus 로고    scopus 로고
    • BID regulation by p53 contributes to chemosensitivity
    • Sax J.K., et al. BID regulation by p53 contributes to chemosensitivity. Nat. Cell Biol 2002, 4(11):842-849.
    • (2002) Nat. Cell Biol , vol.4 , Issue.11 , pp. 842-849
    • Sax, J.K.1
  • 56
    • 84901070084 scopus 로고    scopus 로고
    • Palmdelphin, a novel target of p53 with Ser46 phosphorylation, controls cell death in response to DNA damage
    • Dashzeveg N., et al. Palmdelphin, a novel target of p53 with Ser46 phosphorylation, controls cell death in response to DNA damage. Cell Death Dis 2014, 5:e1221.
    • (2014) Cell Death Dis , vol.5 , pp. e1221
    • Dashzeveg, N.1
  • 57
    • 79952623655 scopus 로고    scopus 로고
    • CIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production
    • Vanlangenakker N., et al. cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production. Cell Death Differ 2011, 18(4):656-665.
    • (2011) Cell Death Differ , vol.18 , Issue.4 , pp. 656-665
    • Vanlangenakker, N.1
  • 58
    • 84886732111 scopus 로고    scopus 로고
    • Membrane TNF-alpha-activated programmed necrosis is mediated by Ceramide-induced reactive oxygen species
    • Ardestani S., Deskins D.L., Young P.P. Membrane TNF-alpha-activated programmed necrosis is mediated by Ceramide-induced reactive oxygen species. J. Mol. Signal 2013, 8(1):12.
    • (2013) J. Mol. Signal , vol.8 , Issue.1 , pp. 12
    • Ardestani, S.1    Deskins, D.L.2    Young, P.P.3
  • 59
    • 84907212907 scopus 로고    scopus 로고
    • Cell biology. Metabolic control of cell death
    • 1250256
    • Green D.R., Galluzzi L., Kroemer G. Cell biology. Metabolic control of cell death. Science 2014, 345(6203). 1250256.
    • (2014) Science , vol.345 , Issue.6203
    • Green, D.R.1    Galluzzi, L.2    Kroemer, G.3
  • 60
    • 3042665524 scopus 로고    scopus 로고
    • Hypoxia inhibits tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by blocking Bax translocation
    • Kim M., et al. Hypoxia inhibits tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by blocking Bax translocation. Cancer Res 2004, 64(12):4078-4081.
    • (2004) Cancer Res , vol.64 , Issue.12 , pp. 4078-4081
    • Kim, M.1
  • 61
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - a key regulatory factor in tumour growth
    • Harris A.L. Hypoxia - a key regulatory factor in tumour growth. Nat. Rev. Cancer 2002, 2(1):38-47.
    • (2002) Nat. Rev. Cancer , vol.2 , Issue.1 , pp. 38-47
    • Harris, A.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.