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Volumn 66, Issue 2, 2004, Pages 500-506

Apoptotic pathways in ischemic acute renal failure

Author keywords

Acute renal failure; Cell death; Endonucleases; Mitochondria caspases; Renal tubular epithelial cells

Indexed keywords

CASPASE; DNA FRAGMENT; ENDONUCLEASE;

EID: 3242744482     PISSN: 00852538     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1523-1755.2004.761_6.x     Document Type: Conference Paper
Times cited : (140)

References (63)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • KERR JFR, WYLLIE AH, CURRIE AR: Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239-257, 1972
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0031616983 scopus 로고    scopus 로고
    • Special topic: Apoptosis
    • THOMPSON EB: Special topic: Apoptosis. Ann Rev Physiol 60:525-532, 1998
    • (1998) Ann Rev Physiol , vol.60 , pp. 525-532
    • Thompson, E.B.1
  • 3
    • 0029821680 scopus 로고    scopus 로고
    • Mechanisms of apoptosis and its potential role in renal tubular epithelial cell injury
    • Renal Fluid Electrolyte Physiol 40
    • LIEBERTHAL W, LEVINE JS: Mechanisms of apoptosis and its potential role in renal tubular epithelial cell injury. Am J Physiol 271 (Renal Fluid Electrolyte Physiol 40):F477-F488, 1996
    • (1996) Am J Physiol , vol.271
    • Lieberthal, W.1    Levine, J.S.2
  • 4
    • 0031989121 scopus 로고    scopus 로고
    • Graded ATP depletion can cause necrosis or apoptosis of cultured mouse proximal tubular cells
    • Renal Physiol 43
    • LIEBERTHAL W, MENZA SA, LEVINE JS: Graded ATP depletion can cause necrosis or apoptosis of cultured mouse proximal tubular cells. Am J Physiol 274 (Renal Physiol 43):F315-F327, 1998
    • (1998) Am J Physiol , vol.274
    • Lieberthal, W.1    Menza, S.A.2    Levine, J.S.3
  • 5
    • 0026551591 scopus 로고
    • Morphologic, biochemical, and molecular evidence of apoptosis during the reperfusion phase after brief periods of renal ischemia
    • SCHUMER M, COLOMBEL MC, SAWCZUK IS, et al. Morphologic, biochemical, and molecular evidence of apoptosis during the reperfusion phase after brief periods of renal ischemia. Am J Physiol 140:831-838, 1992
    • (1992) Am J Physiol , vol.140 , pp. 831-838
    • Schumer, M.1    Colombel, M.C.2    Sawczuk, I.S.3
  • 6
    • 0012358348 scopus 로고
    • Induction of apoptosis in ischemia-reperfusion kidney model: Appearance of DNA strand breaks and expression of FAS mRNA
    • NOGAE S, KOJI T, NAKANISHI Y, et al: Induction of apoptosis in ischemia-reperfusion kidney model: Appearance of DNA strand breaks and expression of FAS mRNA. J Am Soc Nephrol 5:905, 1994
    • (1994) J Am Soc Nephrol , vol.5 , pp. 905
    • Nogae, S.1    Koji, T.2    Nakanishi, Y.3
  • 7
    • 0028706978 scopus 로고
    • An evaluation of renal tubular DNA laddering in response to oxygen deprivation and oxidant injury
    • IWATA M, MYERSON D, TOROK-STORB B, ZAGER RA: An evaluation of renal tubular DNA laddering in response to oxygen deprivation and oxidant injury. J Am Soc Nephrol 5:1307-1313, 1994
    • (1994) J Am Soc Nephrol , vol.5 , pp. 1307-1313
    • Iwata, M.1    Myerson, D.2    Torok-Storb, B.3    Zager, R.A.4
  • 8
    • 0029019607 scopus 로고
    • Rapid DNA fragmentation from hypoxia along the thick ascending limb of rat kidneys
    • BEERI R, SYMON Z, BREZIS M, et al: Rapid DNA fragmentation from hypoxia along the thick ascending limb of rat kidneys. Kidney Int 47:1806-1810, 1995
    • (1995) Kidney Int , vol.47 , pp. 1806-1810
    • Beeri, R.1    Symon, Z.2    Brezis, M.3
  • 9
    • 0037218760 scopus 로고    scopus 로고
    • P53 mediates the apoptotic response to GTP depletion after renal ischemia-reperfusion: Protective role of a p53 inhibitor
    • KELLY KJ, PLOTKIN Z, VULGAMOTT SL, DAGHER PC: P53 mediates the apoptotic response to GTP depletion after renal ischemia-reperfusion: Protective role of a p53 inhibitor. J Am Soc Nephrol 14(1):128-138, 2003
    • (2003) J Am Soc Nephrol , vol.14 , Issue.1 , pp. 128-138
    • Kelly, K.J.1    Plotkin, Z.2    Vulgamott, S.L.3    Dagher, P.C.4
  • 10
    • 0035180186 scopus 로고    scopus 로고
    • Guanosine supplementation reduces apoptosis and protects renal function in the setting of ischemic injury
    • KELLY KJ, PLOTKIN Z, DAGHER PC: Guanosine supplementation reduces apoptosis and protects renal function in the setting of ischemic injury. J Clin Invest 108(9):1291-1298, 2001
    • (2001) J Clin Invest , vol.108 , Issue.9 , pp. 1291-1298
    • Kelly, K.J.1    Plotkin, Z.2    Dagher, P.C.3
  • 11
    • 0021888013 scopus 로고
    • The level of induced DNA double-strand breakage correlates with cell killing after x-irradiation
    • RADFORD IR: The level of induced DNA double-strand breakage correlates with cell killing after x-irradiation. Int J Radiat Biol Relat Stud Phys Chem Med 48:45-54, 1985
    • (1985) Int J Radiat Biol Relat Stud Phys Chem Med , vol.48 , pp. 45-54
    • Radford, I.R.1
  • 12
    • 0027093953 scopus 로고
    • Endonuclease-induced DNA damage and cell death in oxidant injury to renal tubular epithelial cells
    • UEDA N, SHAH SV: Endonuclease-induced DNA damage and cell death in oxidant injury to renal tubular epithelial cells. J Clin Invest 90:2593-2597, 1992
    • (1992) J Clin Invest , vol.90 , pp. 2593-2597
    • Ueda, N.1    Shah, S.V.2
  • 14
    • 0029126059 scopus 로고
    • Activation of a 15-kDa endonuclease in hypoxia/reoxygenation injury without morphologic features of apoptosis
    • UEDA N, WALKER PD, HSU S-M, SHAH SV: Activation of a 15-kDa endonuclease in hypoxia/reoxygenation injury without morphologic features of apoptosis. Proc Natl Acad Sci USA 92:7202-7206, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7202-7206
    • Ueda, N.1    Walker, P.D.2    Hsu, S.-M.3    Shah, S.V.4
  • 15
    • 0030034283 scopus 로고    scopus 로고
    • Endonuclease induced DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells
    • HAGAR H, UEDA N, SHAH SV: Endonuclease induced DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells. Kidney Int 49:355-361, 1996
    • (1996) Kidney Int , vol.49 , pp. 355-361
    • Hagar, H.1    Ueda, N.2    Shah, S.V.3
  • 16
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • ENARI M, SAKAHIRA H, YOKOYAMA H, et al: A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391:43-50, 1998
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3
  • 17
    • 0032553416 scopus 로고    scopus 로고
    • The cloning and expression of human deoxyribonuclease II. A possible role in apoptosis
    • KRIESER RJ, EASTMAN A: The cloning and expression of human deoxyribonuclease II. A possible role in apoptosis. J Biol Chem 273:30909-30914, 1998
    • (1998) J Biol Chem , vol.273 , pp. 30909-30914
    • Krieser, R.J.1    Eastman, A.2
  • 18
    • 0034630317 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation
    • NAGATA S: Apoptotic DNA fragmentation. Exp Cell Res 256:12-18, 2000
    • (2000) Exp Cell Res , vol.256 , pp. 12-18
    • Nagata, S.1
  • 19
    • 0027745784 scopus 로고
    • Overexpression of deoxyribonuclease I (DNase I) transfected into COS-cells: Its distribution during apoptotic cell death
    • POLZAR B, PEITSCH MC, LOOS R, et al: Overexpression of deoxyribonuclease I (DNase I) transfected into COS-cells: Its distribution during apoptotic cell death. Eur J Cell Biol 62:397-405, 1993
    • (1993) Eur J Cell Biol , vol.62 , pp. 397-405
    • Polzar, B.1    Peitsch, M.C.2    Loos, R.3
  • 20
    • 0033601251 scopus 로고    scopus 로고
    • DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells
    • ZHANG S, DEMIRS JT, KOCHEVAR IE: DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells. J Biol Chem 274:37450-37454, 1999
    • (1999) J Biol Chem , vol.274 , pp. 37450-37454
    • Zhang, S.1    Demirs, J.T.2    Kochevar, I.E.3
  • 21
    • 0036205657 scopus 로고    scopus 로고
    • DNase I-like endonuclease in rat kidney cortex and activation during ischemia/reperfusion injury
    • BASNAKIAN AG, UEDA N, KAUSHAL GP, et al: DNase I-like endonuclease in rat kidney cortex and activation during ischemia/reperfusion injury. J Am Soc Nephrol 13:1000-1007, 2002
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1000-1007
    • Basnakian, A.G.1    Ueda, N.2    Kaushal, G.P.3
  • 22
    • 0034673555 scopus 로고    scopus 로고
    • Mammalian deoxyribonucleases I are classified into three types: Pancreas, parotid, and pancreas-parotid (mixed), based on differences in their tissue concentrations
    • TAKESHITA H, MOGI K, YASUDA T, et al: Mammalian deoxyribonucleases I are classified into three types: pancreas, parotid, and pancreas-parotid (mixed), based on differences in their tissue concentrations. Biochem Biophys Res Commun 269:481-484, 2000
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 481-484
    • Takeshita, H.1    Mogi, K.2    Yasuda, T.3
  • 23
    • 0019887828 scopus 로고
    • Deoxyribonuclease I in mammalian tissues. Specificity of inhibition by actin
    • LACKS SA: Deoxyribonuclease I in mammalian tissues. Specificity of inhibition by actin. J Biol Chem 256:2644-2648, 1981
    • (1981) J Biol Chem , vol.256 , pp. 2644-2648
    • Lacks, S.A.1
  • 24
    • 14444274100 scopus 로고    scopus 로고
    • Porcine spleen deoxyribonuclease II. Covalent structure, cDNA sequence, molecular cloning, and gene expression
    • WANG CC, LU SC, HL. C, LIAO TH: Porcine spleen deoxyribonuclease II. Covalent structure, cDNA sequence, molecular cloning, and gene expression. J Biol Chem 273:17192-17198, 1998
    • (1998) J Biol Chem , vol.273 , pp. 17192-17198
    • Wang, C.C.1    Lu, S.C.2    Hl, C.3    Liao, T.H.4
  • 25
    • 0032482949 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human caspase-activated DNase
    • MUKAE N, ENARI M, SAKAHIRA H, et al: Molecular cloning and characterization of human caspase-activated DNase. Proc Natl Acad Sci USA 95:9123-9128, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9123-9128
    • Mukae, N.1    Enari, M.2    Sakahira, H.3
  • 26
    • 0036308059 scopus 로고    scopus 로고
    • Mitochondria, the killer organelles and their weapons
    • RAVAGNAN L, ROUMIER T, KROEMER G: Mitochondria, the killer organelles and their weapons. J Cell Physiol 192:131-137, 2002
    • (2002) J Cell Physiol , vol.192 , pp. 131-137
    • Ravagnan, L.1    Roumier, T.2    Kroemer, G.3
  • 28
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • HENGARTNER MO: The biochemistry of apoptosis. Nature 407:770-776, 2000
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 29
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • WANG X: The expanding role of mitochondria in apoptosis. Genes Dev 15:2922-2933, 2001
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 30
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • THORNBERRY NA, LAZEBNIK Y: Caspases: enemies within. Science 281:1312-1316, 1998
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 31
    • 0033575255 scopus 로고    scopus 로고
    • Suicidal tendencies: Apoptotic cell death by caspase family proteinases
    • WOLF BB, GREEN DR: Suicidal tendencies: apoptotic cell death by caspase family proteinases. J Biol Chem 274:20049-20052, 1999
    • (1999) J Biol Chem , vol.274 , pp. 20049-20052
    • Wolf, B.B.1    Green, D.R.2
  • 32
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • EARNSHAW WC, MARTINS LM, KAUFMANN SH: Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Ann Rev Biochem 68:383-424, 1999
    • (1999) Ann Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 33
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • CRYNS V, YUAN J: Proteases to die for. Genes Dev 12:1551-1570, 1998
    • (1998) Genes Dev , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 35
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • LIU X, KIM CN, YANG J, et al: Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 86(1):147-157, 1996
    • (1996) Cell , vol.86 , Issue.1 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3
  • 36
    • 0037188903 scopus 로고    scopus 로고
    • Destabilizing influences in apoptosis: Sowing the seeds of IAP destruction
    • MARTIN SJ: Destabilizing influences in apoptosis: Sowing the seeds of IAP destruction. Cell 109:793-796, 2002
    • (2002) Cell , vol.109 , pp. 793-796
    • Martin, S.J.1
  • 37
    • 0037318902 scopus 로고    scopus 로고
    • Mitochondria, AIF and caspases - Rivaling for cell death execution
    • PENNINGER JM, KROEMER G: Mitochondria, AIF and caspases - Rivaling for cell death execution. Nat Cell Biol 5:97-99, 2003
    • (2003) Nat Cell Biol , vol.5 , pp. 97-99
    • Penninger, J.M.1    Kroemer, G.2
  • 38
    • 0030798072 scopus 로고    scopus 로고
    • Role of caspases (ICE/CED 3 proteases) in DNA damage and cell death in response to a mitochondrial inhibitor, antimycin A
    • KAUSHAL GP, UEDA N, SHAH SV: Role of caspases (ICE/CED 3 proteases) in DNA damage and cell death in response to a mitochondrial inhibitor, antimycin A. Kidney Int 52:438-445, 1997
    • (1997) Kidney Int , vol.52 , pp. 438-445
    • Kaushal, G.P.1    Ueda, N.2    Shah, S.V.3
  • 39
    • 0032780169 scopus 로고    scopus 로고
    • Role of caspases in hypoxia-induced necrosis of rat renal proximal tubules
    • EDELSTEIN CL, SHI Y, SCHRIER RW: Role of caspases in hypoxia-induced necrosis of rat renal proximal tubules. J Am Soc Nephrol 10:1940-1949, 1999
    • (1999) J Am Soc Nephrol , vol.10 , pp. 1940-1949
    • Edelstein, C.L.1    Shi, Y.2    Schrier, R.W.3
  • 41
    • 0031919843 scopus 로고    scopus 로고
    • Identification of caspase (ICE-like proteases) gene family in rat kidney and altered expression in ischemia/reperfusion injury
    • KAUSHAL GP, SINGH AB, SHAH SV: Identification of caspase (ICE-like proteases) gene family in rat kidney and altered expression in ischemia/reperfusion injury. Am J Physiol 274:F587-F595, 1998
    • (1998) Am J Physiol , vol.274
    • Kaushal, G.P.1    Singh, A.B.2    Shah, S.V.3
  • 42
    • 0033826589 scopus 로고    scopus 로고
    • Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion
    • SHI Y, MELNIKOV VY, SCHRIER RW, EDELSTEIN CL: Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion. Am J Physiol Renal Physiol 279:F509-F517, 2000
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Shi, Y.1    Melnikov, V.Y.2    Schrier, R.W.3    Edelstein, C.L.4
  • 43
    • 0032743421 scopus 로고    scopus 로고
    • Inhibition of apoptosis induced by ischemia-reperfusion prevents inflammation
    • DAEMEN MA, VAN VEER C, DENECKER G, et al: Inhibition of apoptosis induced by ischemia-reperfusion prevents inflammation. J Clin Invest 104:541-549, 1999
    • (1999) J Clin Invest , vol.104 , pp. 541-549
    • Daemen, M.A.1    Van Veer, C.2    Denecker, G.3
  • 44
    • 0031944498 scopus 로고    scopus 로고
    • Role of IL-1 in renal ischemic reperfusion injury
    • HAQ M, NORMAN J, SABA SR, et al: Role of IL-1 in renal ischemic reperfusion injury. J Am Soc Nephrol 9:614-619, 1998
    • (1998) J Am Soc Nephrol , vol.9 , pp. 614-619
    • Haq, M.1    Norman, J.2    Saba, S.R.3
  • 45
    • 0033136706 scopus 로고    scopus 로고
    • Ischemia/reperfusion-induced IFN-gamma up-regulation: Involvement of IL-12 and IL-18
    • DAEMEN MA, VAN'T VEER C, WOLFS TG, MUURMAN WA: Ischemia/reperfusion- induced IFN-gamma up-regulation: involvement of IL-12 and IL-18. J Immunol 162:5506-5510, 1999
    • (1999) J Immunol , vol.162 , pp. 5506-5510
    • Daemen, M.A.1    Van't Veer, C.2    Wolfs, T.G.3    Muurman, W.A.4
  • 46
    • 0035015397 scopus 로고    scopus 로고
    • Impaired IL-18 processing protects caspase-1-deficient mice from ischemic acute renal failure
    • MELNIKOV VY, ECDER T, FANTUZZI G, et al: Impaired IL-18 processing protects caspase-1-deficient mice from ischemic acute renal failure. J Clin Invest 107:1145-1152, 2001
    • (2001) J Clin Invest , vol.107 , pp. 1145-1152
    • Melnikov, V.Y.1    Ecder, T.2    Fantuzzi, G.3
  • 47
    • 0035957196 scopus 로고    scopus 로고
    • Activated caspase-1 is not a central mediator of inflammation in the course of ischemia-reperfusion
    • DAEMEN MA, DENECKER G, VAN'T VEER C, et al: Activated caspase-1 is not a central mediator of inflammation in the course of ischemia-reperfusion. Transplantation 71:778-784, 2001
    • (2001) Transplantation , vol.71 , pp. 778-784
    • Daemen, M.A.1    Denecker, G.2    Van't Veer, C.3
  • 48
    • 0035028773 scopus 로고    scopus 로고
    • De novo demonstration and co-localization of free-radical production and apoptosis formation in rat kidney subjected to ischemia/reperfusion
    • CHIEN CT, LEE PH, CHEN CF, et al: De novo demonstration and co-localization of free-radical production and apoptosis formation in rat kidney subjected to ischemia/reperfusion. J Am Soc Nephrol 12:973-982, 2001
    • (2001) J Am Soc Nephrol , vol.12 , pp. 973-982
    • Chien, C.T.1    Lee, P.H.2    Chen, C.F.3
  • 49
    • 0032585644 scopus 로고    scopus 로고
    • Role of hypoxia-induced Bax translocation and cytochrome C release in reoxygenation injury
    • SAIKUMAR P, DONG Z, PATEL Y, et al: Role of hypoxia-induced Bax translocation and cytochrome C release in reoxygenation injury. Oncogene 17:3401-3415, 1998
    • (1998) Oncogene , vol.17 , pp. 3401-3415
    • Saikumar, P.1    Dong, Z.2    Patel, Y.3
  • 50
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three akts
    • DATTA SR, BRUNET A, GREENBERG ME: Cellular survival: A play in three akts. Genes Dev 13:2905-2927, 1999
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 51
    • 0030907987 scopus 로고    scopus 로고
    • PI3K downstream AKTion blocks apoptosis
    • FRANKE TF, KAPLAN DR, CANTLEY LC: PI3K downstream AKTion blocks apoptosis. Cell 88:435-437, 1997
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 52
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • DATTA SR, DUDEK H, TAO X, et al: Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91:231-241, 1997
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3
  • 53
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • YANG E, ZHA J, JOCKEL J, et al: Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80:285-291, 1995
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3
  • 54
    • 0001582482 scopus 로고
    • Molecular cloning of the akt oncogene and its human homologs Akt1 and Akt2: Amplification of Akt1 in a primary human gastric adenocarcinoma
    • STAAL SP: Molecular cloning of the akt oncogene and its human homologs Akt1 and Akt2: Amplification of Akt1 in a primary human gastric adenocarcinoma. Proc Natl Acad Sci USA 84:5034-5037, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5034-5037
    • Staal, S.P.1
  • 55
    • 0027470177 scopus 로고
    • Structure, expression and chromosomal mapping of c-akt: Relationship to v-akt and its implications
    • BELLACOSA A, FRANKE TF, GONZALEZ-PORTAL ME, et al: Structure, expression and chromosomal mapping of c-akt: relationship to v-akt and its implications. Oncogene 8:745-754, 1993
    • (1993) Oncogene , vol.8 , pp. 745-754
    • Bellacosa, A.1    Franke, T.F.2    Gonzalez-Portal, M.E.3
  • 56
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X
    • ZHA J, HARADA H, YANG E, et al: Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X. Cell 87:619-628, 1996
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3
  • 57
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • VAUX DL, KORSMEYER SJ: Cell death in development. Cell 96:245-254, 1999
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 58
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • GROSS A, MCDONNELL JM, KORSMEYER S: BCL-2 family members and the mitochondria in apoptosis. Genes Dev 13:1899-1911, 1999
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.3
  • 59
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • DEL PESO L, GONZALEZ-GARCIA M, PAGE C, et al: Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278:687-689, 1997
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3
  • 60
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochome c from mitochondria blocked
    • YANG J, LIU X, BHALLA K, et al: Prevention of apoptosis by Bcl-2: Release of cytochome c from mitochondria blocked. Science 275:1129-1132, 1997
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 61
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • HU Y, BENEDICT MA, WU D, et al: Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Natl Acad Sci USA 95:4386-4391, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3
  • 62
    • 0034778721 scopus 로고    scopus 로고
    • Role and regulation of activation of caspases in cisplatin-induced injury to renal tubular epithelial cells
    • KAUSHAL GP, KAUSHAL V, HONG X, SHAH S: Role and regulation of activation of caspases in cisplatin-induced injury to renal tubular epithelial cells. Kidney Int 60:1726-1736, 2001
    • (2001) Kidney Int , vol.60 , pp. 1726-1736
    • Kaushal, G.P.1    Kaushal, V.2    Hong, X.3    Shah, S.4
  • 63
    • 0032515027 scopus 로고    scopus 로고
    • Regulation of cell death protease caspase-9 by phosphorylation
    • CARDONE MH, ROY N, STENNICKE HR, et al: Regulation of cell death protease caspase-9 by phosphorylation. Science 282:1818-1321, 1998
    • (1998) Science , vol.282 , pp. 1818-11321
    • Cardone, M.H.1    Roy, N.2    Stennicke, H.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.