메뉴 건너뛰기




Volumn 8, Issue 1, 2003, Pages 19-27

Regulation of cell apoptosis by protein kinase c δ

Author keywords

Apoptosis; C Abl; Caspases; Nucleus; Phosphorylation; Protein kinase C ; Translocation mitochondria

Indexed keywords

ANTINEOPLASTIC AGENT; CASPASE; CERAMIDE; CISPLATIN; COMPLEMENTARY DNA; CYTARABINE; ETOPOSIDE; GAMMA INTERFERON; GENOMIC DNA; HYDROGEN PEROXIDE; INTERLEUKIN 1BETA; METHYLGLYOXAL; MITOMYCIN; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C DELTA; PROTEIN TYROSINE KINASE; STREPTOZOCIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 0037246123     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021640817208     Document Type: Review
Times cited : (378)

References (105)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide range implications in tissue kinetics
    • Kerr JFR, Wyllie AH, Currie AR. Apoptosis: A basic biological phenomenon with wide range implications in tissue kinetics. Br J Cancer 1972; 26: 239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med 1997; 3: 614-620.
    • (1997) Nat Med , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 4
    • 0344389027 scopus 로고    scopus 로고
    • Caspases: The proteases of the apoptotic pathway
    • Nunez G, Benedict MA, Hu Y, Inohara, N. Caspases: The proteases of the apoptotic pathway. Oncogene 1998; 17: 3237-3245.
    • (1998) Oncogene , vol.17 , pp. 3237-3245
    • Nunez, G.1    Benedict, M.A.2    Hu, Y.3    Inohara, N.4
  • 5
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: More than a paradigm
    • Wajant H. The Fas signaling pathway: More than a paradigm. Science 2002; 296: 1635-1536.
    • (2002) Science , vol.296 , pp. 1635-1536
    • Wajant, H.1
  • 6
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi A, Dixit VM. Apoptosis control by death and decoy receptors. Curr Opin Cell Biol 1999; 11: 255-260.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 7
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen GS, Dixit VM. Caspases: Intracellular signaling by proteolysis. Cell 1997; 91: 443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 8
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 10
    • 0032762030 scopus 로고    scopus 로고
    • Mechanisms mediating caspase activation in cell death
    • Kumar S. Mechanisms mediating caspase activation in cell death. Cell Death Differ 1999; 6: 1060-1066.
    • (1999) Cell Death Differ , vol.6 , pp. 1060-1066
    • Kumar, S.1
  • 11
    • 0033582526 scopus 로고    scopus 로고
    • Distinct caspase cascades are initiated in receptormediated and chemical-induced apoptosis
    • Sun XM, MacFarlane M, Zhuang J, Wolf BB, Green DR, Cohen GM. Distinct caspase cascades are initiated in receptormediated and chemical-induced apoptosis. J Biol Chem 1999; 274: 5053-5060.
    • (1999) J Biol Chem , vol.274 , pp. 5053-5060
    • Sun, X.M.1    MacFarlane, M.2    Zhuang, J.3    Wolf, B.B.4    Green, D.R.5    Cohen, G.M.6
  • 12
    • 0034525423 scopus 로고    scopus 로고
    • Kinases: Positive and negative regulators of apoptosis
    • Franklin RA, McCubrey JA. Kinases: Positive and negative regulators of apoptosis. Leukemia 2000; 14: 2019-2034.
    • (2000) Leukemia , vol.14 , pp. 2019-2034
    • Franklin, R.A.1    McCubrey, J.A.2
  • 14
    • 0030904561 scopus 로고    scopus 로고
    • The PI 3-kinase/Akt signaling pathway delivers an anti-apoptotic signal
    • Kennedy SG, Wagner AJ, Conzen SD, et al. The PI 3-kinase/Akt signaling pathway delivers an anti-apoptotic signal. Gene Dev 2000; 11: 701-713.
    • (2000) Gene Dev , vol.11 , pp. 701-713
    • Kennedy, S.G.1    Wagner, A.J.2    Conzen, S.D.3
  • 15
    • 0034164455 scopus 로고    scopus 로고
    • The c-Jun N-terminal kinase pathway and apoptotic signaling
    • Chen YR, Tan TH. The c-Jun N-terminal kinase pathway and apoptotic signaling. Int J Oncol 2000; 16: 651-662.
    • (2000) Int J Oncol , vol.16 , pp. 651-662
    • Chen, Y.R.1    Tan, T.H.2
  • 16
    • 0034693878 scopus 로고    scopus 로고
    • Regulation of cell death by the Abl tyrosine kinase
    • Wang Y. Regulation of cell death by the Abl tyrosine kinase. Oncogene 2000; 19: 5643-5650.
    • (2000) Oncogene , vol.19 , pp. 5643-5650
    • Wang, Y.1
  • 17
    • 0032537024 scopus 로고    scopus 로고
    • Loss of protein kinase C function induces an apoptotic response
    • Whelan DHR, Parker PJ. Loss of protein kinase C function induces an apoptotic response. Oncogene 1998; 16: 1939-1944.
    • (1998) Oncogene , vol.16 , pp. 1939-1944
    • Whelan, D.H.R.1    Parker, P.J.2
  • 18
    • 0035834817 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase Cε and δ in neonatal rat ventricular myocytes
    • Heidkamp MC, Bayer AL, Martin JL, Samarel AM. Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase Cε and δ in neonatal rat ventricular myocytes. Circ Res 2001; 89: 882-890.
    • (2001) Circ Res , vol.89 , pp. 882-890
    • Heidkamp, M.C.1    Bayer, A.L.2    Martin, J.L.3    Samarel, A.M.4
  • 19
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug H, Sarre TF. Protein kinase C isoenzymes: Divergence in signal transduction? Biochem J 1993; 291: 329-343.
    • (1993) Biochem J , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 20
    • 0029965696 scopus 로고    scopus 로고
    • Protein kinase C isozymes and substrates
    • Jaken, S. Protein kinase C isozymes and substrates. Curr Opin Cell Biol 1996; 8: 168-173.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 168-173
    • Jaken, S.1
  • 21
    • 0029364428 scopus 로고
    • Protein kinase C. Seeing two domains
    • Newton AC. Protein kinase C. Seeing two domains. Curr Biol 1995; 5: 973-976.
    • (1995) Curr Biol , vol.5 , pp. 973-976
    • Newton, A.C.1
  • 22
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good JA, Ziegler WH, Parekh DB, Alessi DR, Cohen P, Parker PJ. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 1998; 281: 2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 23
    • 0030023982 scopus 로고    scopus 로고
    • Activation of protein kinase Cdelta in human myeloid leukemia cells treated with 1-beta-D-arabinofuranosylcytosine
    • Emoto Y, Kisaki H, Manome Y, Kharbanda S, Kufe D. Activation of protein kinase Cdelta in human myeloid leukemia cells treated with 1-beta-D-arabinofuranosylcytosine. Blood 1996; 87: 1990-1996.
    • (1996) Blood , vol.87 , pp. 1990-1996
    • Emoto, Y.1    Kisaki, H.2    Manome, Y.3    Kharbanda, S.4    Kufe, D.5
  • 24
    • 0023662114 scopus 로고
    • Identification of three additional members of rat protein kinase C family: Delta-, epsilon- and zeta-subspecies
    • Ono Y, Fujii T, Ogita K, Kikkawa U, Igarashi K, Nishizuka Y. Identification of three additional members of rat protein kinase C family: Delta-, epsilon- and zeta-subspecies. FEBS Lett 1987; 226: 125-128.
    • (1987) FEBS Lett , vol.226 , pp. 125-128
    • Ono, Y.1    Fujii, T.2    Ogita, K.3    Kikkawa, U.4    Igarashi, K.5    Nishizuka, Y.6
  • 25
    • 0033082319 scopus 로고    scopus 로고
    • Protein kinase C δ
    • Gschwendt M. Protein kinase C δ. Eur J Biochem 1999; 259: 555-564.
    • (1999) Eur J Biochem , vol.259 , pp. 555-564
    • Gschwendt, M.1
  • 26
    • 0031907117 scopus 로고    scopus 로고
    • Activation of protein kinase C triggers its ubiquitination and degradation
    • Zhimin Lu, Liu D, Hornia A, Devonish W, Pagano M, Foster DA. Activation of protein kinase C triggers its ubiquitination and degradation. Mol Cell Biol 1998; 18: 839-845.
    • (1998) Mol Cell Biol , vol.18 , pp. 839-845
    • Lu, Z.1    Liu, D.2    Hornia, A.3    Devonish, W.4    Pagano, M.5    Foster, D.A.6
  • 28
    • 0026472991 scopus 로고
    • Cell division arrest induced by phorbol ester in CHO cells overexpressing protein kinase Cδ subspecies
    • Watanabe T, Ono Y, Taniyama Y, et al. Cell division arrest induced by phorbol ester in CHO cells overexpressing protein kinase Cδ subspecies. Proc Natl Acad Sci USA 1992; 89: 10159-10163.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10159-10163
    • Watanabe, T.1    Ono, Y.2    Taniyama, Y.3
  • 29
    • 0037171731 scopus 로고    scopus 로고
    • Increased proliferation of B cells and auto-immunity in mice lacking protein kinase Cδ
    • Miyamoto A, Nakayama K, Imaki H, et al. Increased proliferation of B cells and auto-immunity in mice lacking protein kinase Cδ. Nature 2002; 416: 865-869.
    • (2002) Nature , vol.416 , pp. 865-869
    • Miyamoto, A.1    Nakayama, K.2    Imaki, H.3
  • 31
    • 0029001975 scopus 로고
    • Protein kinase C involvement in apoptosis
    • Lucas M, Sanchez-Margalet V. Protein kinase C involvement in apoptosis. Gen Pharmacol 1995; 265: 881-887.
    • (1995) Gen Pharmacol , vol.265 , pp. 881-887
    • Lucas, M.1    Sanchez-Margalet, V.2
  • 32
    • 0036209077 scopus 로고    scopus 로고
    • Novel "nonkinase" phorbol ester receptors: The C1 domain connection
    • Kazanietz MG. Novel "nonkinase" phorbol ester receptors: The C1 domain connection. Mol Pharmacol 2002; 61: 759-767.
    • (2002) Mol Pharmacol , vol.61 , pp. 759-767
    • Kazanietz, M.G.1
  • 33
    • 0032566717 scopus 로고    scopus 로고
    • A functional role for mitochondrial protein kinase Cα in Bcl2 phosphorylation and suppression of apoptosis
    • Ruvolo PP, Deng X, Carr BK, May WS. A functional role for mitochondrial protein kinase Cα in Bcl2 phosphorylation and suppression of apoptosis. J Biol Chem 1998; 273: 25436-25442.
    • (1998) J Biol Chem , vol.273 , pp. 25436-25442
    • Ruvolo, P.P.1    Deng, X.2    Carr, B.K.3    May, W.S.4
  • 34
    • 0032007292 scopus 로고    scopus 로고
    • Overexpression of protein kinase C isoform ε but not δ in human interleukin-3-dependent cells suppresses apoptosis and induces bcl-2 expression
    • Gubina E, Rinaudo MS, Szallasi Z, Blumberg PM, Mufson RA. Overexpression of protein kinase C isoform ε but not δ in human interleukin-3-dependent cells suppresses apoptosis and induces bcl-2 expression. Blood 1998; 91: 823-829.
    • (1998) Blood , vol.91 , pp. 823-829
    • Gubina, E.1    Rinaudo, M.S.2    Szallasi, Z.3    Blumberg, P.M.4    Mufson, R.A.5
  • 35
    • 0033547873 scopus 로고    scopus 로고
    • Protein kinase Cι activity is necessary for Bcr-Abl-mediated resistance to drug-induced apoptosis
    • Jamieson L, Carpenter L, Biden TJ, Fields AP. Protein kinase Cι activity is necessary for Bcr-Abl-mediated resistance to drug-induced apoptosis. J Biol Chem 1999; 274: 3927-3930.
    • (1999) J Biol Chem , vol.274 , pp. 3927-3930
    • Jamieson, L.1    Carpenter, L.2    Biden, T.J.3    Fields, A.P.4
  • 36
    • 0030795091 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of protein kinase Cθ in induction of apoptosis
    • Datta R, Kojima H, Yoshida K, Kufe D. Caspase-3-mediated cleavage of protein kinase Cθ in induction of apoptosis. J Biol Chem. 1997; 272: 20317-20320.
    • (1997) J Biol Chem , vol.272 , pp. 20317-20320
    • Datta, R.1    Kojima, H.2    Yoshida, K.3    Kufe, D.4
  • 37
    • 0034674678 scopus 로고    scopus 로고
    • Proteolytic cleavage and activation of protein kinase Cμ by caspase-3 in the apoptotic response of cells to 1-β-D-arabinofuranosylcytosine and other genotoxic agents
    • Endo K, Oki E, Biedermann V, et al. Proteolytic cleavage and activation of protein kinase Cμ by caspase-3 in the apoptotic response of cells to 1-β-D-arabinofuranosylcytosine and other genotoxic agents. J Biol Chem 2000; 275: 18476-18481.
    • (2000) J Biol Chem , vol.275 , pp. 18476-18481
    • Endo, K.1    Oki, E.2    Biedermann, V.3
  • 38
    • 0036311666 scopus 로고    scopus 로고
    • Induction and activation of protein kinase Cδ in hippocampus and cortex after kainic Acid treatment
    • Kaasinen SK, Goldsteins G, Alhonen L, Janne J, Koistinaho J. Induction and activation of protein kinase Cδ in hippocampus and cortex after kainic Acid treatment. Exp Neurol 2002; 176: 203-212.
    • (2002) Exp Neurol , vol.176 , pp. 203-212
    • Kaasinen, S.K.1    Goldsteins, G.2    Alhonen, L.3    Janne, J.4    Koistinaho, J.5
  • 39
    • 13344259987 scopus 로고
    • Proteolytic activation of protein kinase Cδ by an ICE-like protease in apoptotic cells
    • Emoto Y, Manome Y, Meinhardt G, et al. Proteolytic activation of protein kinase Cδ by an ICE-like protease in apoptotic cells. EMBO J 1995; 14: 6148-6156.
    • (1995) EMBO J , vol.14 , pp. 6148-6156
    • Emoto, Y.1    Manome, Y.2    Meinhardt, G.3
  • 40
    • 0032802771 scopus 로고    scopus 로고
    • Inhibition of T cell apoptosis by IFN-β rapidly reverses nuclear translocation of protein kinase C-delta
    • Scheel-Toellner D, Pilling D, Akbar AN, et al. Inhibition of T cell apoptosis by IFN-β rapidly reverses nuclear translocation of protein kinase C-delta. Eur J Immunol 1999; 8: 2603-2612.
    • (1999) Eur J Immunol , vol.8 , pp. 2603-2612
    • Scheel-Toellner, D.1    Pilling, D.2    Akbar, A.N.3
  • 42
    • 0032491318 scopus 로고    scopus 로고
    • Protein kinase Cδ is activated by caspase-dependent proteolysis during ultraviolet radiation-induced apoptosis of human keratinocytes
    • Denning MF, Wang Y, Nickoloff BJ, Wrone-Smith T. Protein kinase Cδ is activated by caspase-dependent proteolysis during ultraviolet radiation-induced apoptosis of human keratinocytes. J Biol Chem 1998; 273: 29995-30002.
    • (1998) J Biol Chem , vol.273 , pp. 29995-30002
    • Denning, M.F.1    Wang, Y.2    Nickoloff, B.J.3    Wrone-Smith, T.4
  • 43
    • 0032473917 scopus 로고    scopus 로고
    • Activation of protein kinase Cδ by the c-Abl tyrosine kinase in response to ionizing radiation
    • Yuan ZM, Utsugisawa T, Ishiko T, et al. Activation of protein kinase Cδ by the c-Abl tyrosine kinase in response to ionizing radiation. Oncogene 1998; 16: 1643-1648.
    • (1998) Oncogene , vol.16 , pp. 1643-1648
    • Yuan, Z.M.1    Utsugisawa, T.2    Ishiko, T.3
  • 44
    • 0035997948 scopus 로고    scopus 로고
    • Protein kinase Cδ overexpression enhances radiation sensitivity via extracellular regulated protein kinase 1/2 activation, abolishing the radiationinduced G(2)-M arrest
    • Lee YJ, Soh JW, Dean NM, et al. Protein kinase Cδ overexpression enhances radiation sensitivity via extracellular regulated protein kinase 1/2 activation, abolishing the radiationinduced G(2)-M arrest. Cell Growth Differ 2002; 13: 237-246.
    • (2002) Cell Growth Differ , vol.13 , pp. 237-246
    • Lee, Y.J.1    Soh, J.W.2    Dean, N.M.3
  • 45
    • 0033516666 scopus 로고    scopus 로고
    • Protein kinase C δ is essential for etoposide-induced apoptosis in salivary gland acinar cells
    • Reyland ME, Anderson SM, Matassa AA, Barzen KA, Quissell DO. Protein kinase C δ is essential for etoposide-induced apoptosis in salivary gland acinar cells. J Biol Chem 1999; 274: 19115-19123.
    • (1999) J Biol Chem , vol.274 , pp. 19115-19123
    • Reyland, M.E.1    Anderson, S.M.2    Matassa, A.A.3    Barzen, K.A.4    Quissell, D.O.5
  • 46
    • 0034654498 scopus 로고    scopus 로고
    • Increased activity of the protein kinase Cδ holoenzyme in the cytoplasmic particulate fraction precedes the activation of caspases in polyomavirus-transformed pyF111 rat fibroblasts exposed to calphostin C or topoisomerase-II inhibitors
    • Dal Pra I, Whitfield JF, Chiarini A, Armato U. Increased activity of the protein kinase Cδ holoenzyme in the cytoplasmic particulate fraction precedes the activation of caspases in polyomavirus-transformed pyF111 rat fibroblasts exposed to calphostin C or topoisomerase-II inhibitors. Exp Cell Res 2000; 255: 171-183.
    • (2000) Exp Cell Res , vol.255 , pp. 171-183
    • Dal Pra, I.1    Whitfield, J.F.2    Chiarini, A.3    Armato, U.4
  • 47
    • 0034604023 scopus 로고    scopus 로고
    • PKCδ is an apoptotic lamin kinase
    • Cross T, Griffiths G, Deacon E, et al. PKCδ is an apoptotic lamin kinase. Oncogene 2000; 19: 2331-2337.
    • (2000) Oncogene , vol.19 , pp. 2331-2337
    • Cross, T.1    Griffiths, G.2    Deacon, E.3
  • 48
    • 0037169509 scopus 로고    scopus 로고
    • Methylglyoxal enhances cisplatin-induced cytotoxicity by activating protein kinase Cδ
    • Godbout JP, Pesavento J, Hartman ME, Manson SR, Freund GG. Methylglyoxal enhances cisplatin-induced cytotoxicity by activating protein kinase Cδ. J Biol Chem 2002; 277: 2554-2561.
    • (2002) J Biol Chem , vol.277 , pp. 2554-2561
    • Godbout, J.P.1    Pesavento, J.2    Hartman, M.E.3    Manson, S.R.4    Freund, G.G.5
  • 49
    • 0034794309 scopus 로고    scopus 로고
    • Targeting of protein kinase Cδ to mitochondria in the oxidative stress response
    • Majumder PK, Mishra NC, Sun X, et al. Targeting of protein kinase Cδ to mitochondria in the oxidative stress response. Cell Growth Differ 2001; 129: 465-470.
    • (2001) Cell Growth Differ , vol.129 , pp. 465-470
    • Majumder, P.K.1    Mishra, N.C.2    Sun, X.3
  • 51
    • 0036523088 scopus 로고    scopus 로고
    • Caspase-3-dependent proteolytic cleavage of protein kinase Cδ is essential for oxidative stress-mediated dopaminergic cell death after exposure to methylcyclopentadienyl manganese tricarbonyl
    • Anantharam V, Kitazawa M, Wagner J, Kaul S, Kanthasamy AG. Caspase-3-dependent proteolytic cleavage of protein kinase Cδ is essential for oxidative stress-mediated dopaminergic cell death after exposure to methylcyclopentadienyl manganese tricarbonyl. J Neurosci 2002; 22: 1738-1751.
    • (2002) J Neurosci , vol.22 , pp. 1738-1751
    • Anantharam, V.1    Kitazawa, M.2    Wagner, J.3    Kaul, S.4    Kanthasamy, A.G.5
  • 52
    • 0035131424 scopus 로고    scopus 로고
    • Subtypespecific translocation of the δ subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells
    • Kajimoto T, Ohmori S, Shirai Y, Sakai N, Saito N. Subtypespecific translocation of the δ subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells. Mol Cell Biol 2001; 21: 1769-1783.
    • (2001) Mol Cell Biol , vol.21 , pp. 1769-1783
    • Kajimoto, T.1    Ohmori, S.2    Shirai, Y.3    Sakai, N.4    Saito, N.5
  • 53
    • 0033601231 scopus 로고    scopus 로고
    • Spontaneous neutrophil apoptosis involves caspase 3-mediated activation of protein kinase C-δ
    • Pongracz, J, Webb P, Wang K, Deacon E, Lunn OJ, Lord JM. Spontaneous neutrophil apoptosis involves caspase 3-mediated activation of protein kinase C-δ. J Biol Chem 1999; 274: 37329-37334.
    • (1999) J Biol Chem , vol.274 , pp. 37329-37334
    • Pongracz, J.1    Webb, P.2    Wang, K.3    Deacon, E.4    Lunn, O.J.5    Lord, J.M.6
  • 54
    • 0033168315 scopus 로고    scopus 로고
    • Caspase-mediated proteolysis and activation of protein kinase Cδ play a central role in neutrophil apoptosis
    • Khwaja A, Tatton L. Caspase-mediated proteolysis and activation of protein kinase Cδ play a central role in neutrophil apoptosis. Blood 1999; 94: 291-301.
    • (1999) Blood , vol.94 , pp. 291-301
    • Khwaja, A.1    Tatton, L.2
  • 55
    • 0039765390 scopus 로고    scopus 로고
    • Involvement of protein kinase C δ in phorbol ester-induced apoptosis in LNCaP prostate cancer cells. Lack of proteolytic cleavage of PKCδ
    • Fujii T, Garcia-Bermejo ML, Bernabo JL, et al. Involvement of protein kinase C δ in phorbol ester-induced apoptosis in LNCaP prostate cancer cells. Lack of proteolytic cleavage of PKCδ. J Biol Chem 2000; 275: 7574-7582.
    • (2000) J Biol Chem , vol.275 , pp. 7574-7582
    • Fujii, T.1    Garcia-Bermejo, M.L.2    Bernabo, J.L.3
  • 56
    • 0034698182 scopus 로고    scopus 로고
    • Mitochondrial translocation of protein kinase C delta in phorbol ester-induced cytochrome c release and apoptosis
    • Majumder PK, Pandey P, Sun X, et al. Mitochondrial translocation of protein kinase C delta in phorbol ester-induced cytochrome c release and apoptosis. J Biol Chem 2000; 275: 21793-21796.
    • (2000) J Biol Chem , vol.275 , pp. 21793-21796
    • Majumder, P.K.1    Pandey, P.2    Sun, X.3
  • 57
    • 0033233483 scopus 로고    scopus 로고
    • Protein kinase Cδ targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector
    • Li L, Lorenzo PS, Bogi K, Blumberg PM, Yuspa SH. Protein kinase Cδ targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector. Mol Cell Biol 1999; 19: 8547-8558.
    • (1999) Mol Cell Biol , vol.19 , pp. 8547-8558
    • Li, L.1    Lorenzo, P.S.2    Bogi, K.3    Blumberg, P.M.4    Yuspa, S.H.5
  • 58
    • 0036081393 scopus 로고    scopus 로고
    • Protein kinase Cδ modulates apoptosis induced by hyperglycemia in adult ventricular myocytes
    • Shizukuda Y, Reyland ME, Buttrick PM. Protein kinase Cδ modulates apoptosis induced by hyperglycemia in adult ventricular myocytes. Am J Physiol Heart Circ Physiol 2002; 282: H1625-634.
    • (2002) Am J Physiol Heart Circ Physiol , vol.282
    • Shizukuda, Y.1    Reyland, M.E.2    Buttrick, P.M.3
  • 59
    • 0036061642 scopus 로고    scopus 로고
    • Inhibition of protein kinase Cδ protects rat INS-1 cells against interleukin-1β and streptozotocin-induced apoptosis
    • Carpenter L, Cordery D, Biden TJ. Inhibition of protein kinase Cδ protects rat INS-1 cells against interleukin-1β and streptozotocin-induced apoptosis. Diabetes 2002; 51: 317-324.
    • (2002) Diabetes , vol.51 , pp. 317-324
    • Carpenter, L.1    Cordery, D.2    Biden, T.J.3
  • 60
    • 0029820016 scopus 로고    scopus 로고
    • Activation of the CPP32 protease in apoptosis induced by 1-beta-D arabinofuranosylcytosine and other DNA-damaging agents
    • Datta R, Banach D, Kojima H, et al. Activation of the CPP32 protease in apoptosis induced by 1-beta-D arabinofuranosylcytosine and other DNA-damaging agents. Blood 1996; 88: 1936-1943.
    • (1996) Blood , vol.88 , pp. 1936-1943
    • Datta, R.1    Banach, D.2    Kojima, H.3
  • 61
    • 0034677930 scopus 로고    scopus 로고
    • Interaction between protein kinase C delta and the c-Abl tyrosine kinase in the cellular response to oxidative stress
    • Sun X, Wu F, Datta R, Kharbanda S, Kufe D. Interaction between protein kinase C delta and the c-Abl tyrosine kinase in the cellular response to oxidative stress. J Biol Chem 2000; 275: 7470-7473.
    • (2000) J Biol Chem , vol.275 , pp. 7470-7473
    • Sun, X.1    Wu, F.2    Datta, R.3    Kharbanda, S.4    Kufe, D.5
  • 62
    • 0033022633 scopus 로고    scopus 로고
    • Translocation of protein kinase Cε and protein kinase Cδ to membrane is required for ultraviolet B-induced activation of mitogen-activated protein kinases and apoptosis
    • Chen N, Ma W, Huang C, Dong Z. Translocation of protein kinase Cε and protein kinase Cδ to membrane is required for ultraviolet B-induced activation of mitogen-activated protein kinases and apoptosis. J Biol Chem 1999; 274: 15389-15394.
    • (1999) J Biol Chem , vol.274 , pp. 15389-15394
    • Chen, N.1    Ma, W.2    Huang, C.3    Dong, Z.4
  • 63
    • 0035839635 scopus 로고    scopus 로고
    • PKCδ is required for mitochondrial-dependent apoptosis in salivary epithelial cells
    • Matassa AA, Carpenter L, Biden TJ, Humphries MJ, Reyland ME. PKCδ is required for mitochondrial-dependent apoptosis in salivary epithelial cells. J Biol Chem 2001; 276: 29719-29728.
    • (2001) J Biol Chem , vol.276 , pp. 29719-29728
    • Matassa, A.A.1    Carpenter, L.2    Biden, T.J.3    Humphries, M.J.4    Reyland, M.E.5
  • 64
    • 0035354188 scopus 로고    scopus 로고
    • Protein kinase Cα and protein kinase Cδ play opposite roles in the proliferation and apoptosis of glioma cells
    • Mandil R, Ashkenazi E, Blass M, et al. Protein kinase Cα and protein kinase Cδ play opposite roles in the proliferation and apoptosis of glioma cells. Cancer Res 2001; 61: 4612-4619.
    • (2001) Cancer Res , vol.61 , pp. 4612-4619
    • Mandil, R.1    Ashkenazi, E.2    Blass, M.3
  • 65
    • 0036132855 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide
    • Blass M, Kronfeld I, Kazimirsky G, Blumberg PM, Brodie C. Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide. Mol Cell Biol 2002; 22: 182-195.
    • (2002) Mol Cell Biol , vol.22 , pp. 182-195
    • Blass, M.1    Kronfeld, I.2    Kazimirsky, G.3    Blumberg, P.M.4    Brodie, C.5
  • 67
    • 0034812286 scopus 로고    scopus 로고
    • Basic fibroblast growth factor maintains calcium homeostasis and granulosa cell viability by stimulating calcium efflux via a PKC δ-dependent pathway
    • Peluso JJ, Pappalardo A, Fernandez G. Basic fibroblast growth factor maintains calcium homeostasis and granulosa cell viability by stimulating calcium efflux via a PKC δ-dependent pathway. Endocrinology 2001; 142: 4203-4211.
    • (2001) Endocrinology , vol.142 , pp. 4203-4211
    • Peluso, J.J.1    Pappalardo, A.2    Fernandez, G.3
  • 68
    • 0034668779 scopus 로고    scopus 로고
    • Divergence in the anti-apoptotic signaling pathways used by nerve growth factor and basic fibroblast growth factor (bFGF) in PC12 cells: Rescue by bFGF involves protein kinase Cδ
    • Wert MM, Palfrey HC. Divergence in the anti-apoptotic signaling pathways used by nerve growth factor and basic fibroblast growth factor (bFGF) in PC12 cells: Rescue by bFGF involves protein kinase Cδ. Biochem J 2000; 352: 175-182.
    • (2000) Biochem J , vol.352 , pp. 175-182
    • Wert, M.M.1    Palfrey, H.C.2
  • 69
    • 0033559903 scopus 로고    scopus 로고
    • Overexpression of protein kinase C isoforms protects RAW 264.7 macrophages from nitric oxide-induced apoptosis: Involvement of c-Jun N-terminal kinase/stress-activated protein kinase, p38 kinase, and CPP-32 protease pathways
    • Jun CD, Oh CD, Kwak HJ, et al. Overexpression of protein kinase C isoforms protects RAW 264.7 macrophages from nitric oxide-induced apoptosis: Involvement of c-Jun N-terminal kinase/stress-activated protein kinase, p38 kinase, and CPP-32 protease pathways. J Immunol 1999; 162: 3395-3401.
    • (1999) J Immunol , vol.162 , pp. 3395-3401
    • Jun, C.D.1    Oh, C.D.2    Kwak, H.J.3
  • 70
    • 0037189498 scopus 로고    scopus 로고
    • Infection of glioma cells with Sindbis virus induces selective activation and tyrosine phosphorylation of protein kinase Cδ. Implications for Sindbis virus-induced apoptosis
    • Zrachia A, Dobroslav M, Blass M, et al. Infection of glioma cells with Sindbis virus induces selective activation and tyrosine phosphorylation of protein kinase Cδ. Implications for Sindbis virus-induced apoptosis. J Biol Chem 2002; 277: 23693-23701.
    • (2002) J Biol Chem , vol.277 , pp. 23693-23701
    • Zrachia, A.1    Dobroslav, M.2    Blass, M.3
  • 71
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: Means for isozyme selectivity
    • Mochly-Rosen D, Gordon AS. Anchoring proteins for protein kinase C: Means for isozyme selectivity. FASEB J 1998; 12: 35-42.
    • (1998) FASEB J , vol.12 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 72
    • 0036144679 scopus 로고    scopus 로고
    • Caspase activation and disruption of mitochondrial membrane potential during UV radiation induced apoptosis of human keratinocytes requires activation of protein kinase C
    • Denning MF, Wang Y, Tibudan S, Alkan S, Nickoloff BJ, Qin JZ. Caspase activation and disruption of mitochondrial membrane potential during UV radiation induced apoptosis of human keratinocytes requires activation of protein kinase C. Cell Death Differ 2002; 9: 40-52.
    • (2002) Cell Death Differ , vol.9 , pp. 40-52
    • Denning, M.F.1    Wang, Y.2    Tibudan, S.3    Alkan, S.4    Nickoloff, B.J.5    Qin, J.Z.6
  • 73
    • 0035994003 scopus 로고    scopus 로고
    • MHC class II-mediated apoptosis of mature dendritic cells proceeds by activation of the protein kinase Cδ isoenzyme
    • Bertho N, Blancheteau VM, Setterblad N, et al. MHC class II-mediated apoptosis of mature dendritic cells proceeds by activation of the protein kinase Cδ isoenzyme. Int Immunol 2002; 14: 935-942.
    • (2002) Int Immunol , vol.14 , pp. 935-942
    • Bertho, N.1    Blancheteau, V.M.2    Setterblad, N.3
  • 74
    • 12644268232 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase Cδ by an ICE/CED 3-like protease induces characteristics of apoptosis
    • Ghayur T, Hugunin M, Talanian RV, et al. Proteolytic activation of protein kinase Cδ by an ICE/CED 3-like protease induces characteristics of apoptosis. J Exp Med 1996; 184: 2399-2404.
    • (1996) J Exp Med , vol.184 , pp. 2399-2404
    • Ghayur, T.1    Hugunin, M.2    Talanian, R.V.3
  • 75
    • 0034875172 scopus 로고    scopus 로고
    • Involvement of protein kinase Cδ in DNA damage-induced apoptosis
    • Basu A, Woolard MD, Johnson CL. Involvement of protein kinase Cδ in DNA damage-induced apoptosis. Cell Death Differ 2001; 8: 899-908.
    • (2001) Cell Death Differ , vol.8 , pp. 899-908
    • Basu, A.1    Woolard, M.D.2    Johnson, C.L.3
  • 76
    • 0040909283 scopus 로고    scopus 로고
    • Regulation of caspase activation and cis-diamminedichloroplatinum(II)-induced cell death by protein kinase C
    • Basu A, Akkaraju GR. Regulation of caspase activation and cis-diamminedichloroplatinum(II)-induced cell death by protein kinase C. Biochemistry 1999; 38: 4245-4251.
    • (1999) Biochemistry , vol.38 , pp. 4245-4251
    • Basu, A.1    Akkaraju, G.R.2
  • 77
    • 0034308104 scopus 로고    scopus 로고
    • Mitomycin C induces apoptosis in a caspases-dependent and Fas/CD95-independent manner in human gastric adenocarcinoma cells
    • Park IC, Park MJ, Hwang CS, et al. Mitomycin C induces apoptosis in a caspases-dependent and Fas/CD95-independent manner in human gastric adenocarcinoma cells. Cancer Lett 2000; 158: 125-132.
    • (2000) Cancer Lett , vol.158 , pp. 125-132
    • Park, I.C.1    Park, M.J.2    Hwang, C.S.3
  • 78
    • 0032211157 scopus 로고    scopus 로고
    • Phosphorylated forms of activated caspases are present in cytosol from HL-60 cells during etoposide-induced apoptosis
    • Martins LM, Kottke TJ, Kaufmann SH, Earnshaw WC. Phosphorylated forms of activated caspases are present in cytosol from HL-60 cells during etoposide-induced apoptosis. Blood 1998; 92: 3042-3049.
    • (1998) Blood , vol.92 , pp. 3042-3049
    • Martins, L.M.1    Kottke, T.J.2    Kaufmann, S.H.3    Earnshaw, W.C.4
  • 79
    • 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 1998; 282: 1318-1321.
    • (1998) Science , vol.282 , pp. 1318-1321
    • Cardone, M.H.1    Roy, N.2    Stennicke, H.R.3
  • 80
    • 0034820345 scopus 로고    scopus 로고
    • Novel protein kinase Cδ isoform insensitive to caspase-3
    • Sakurai Y, Onishi Y, Tanimoto Y, Kizaki H. Novel protein kinase Cδ isoform insensitive to caspase-3. Biol Pharm Bull 2001; 24: 973-937.
    • (2001) Biol Pharm Bull , vol.24 , pp. 973-937
    • Sakurai, Y.1    Onishi, Y.2    Tanimoto, Y.3    Kizaki, H.4
  • 81
    • 0028145277 scopus 로고
    • Tyrosine phosphorylation of protein kinase Cδ in response to its activation
    • Li W, Mischak H, Yu JC, et al. Tyrosine phosphorylation of protein kinase Cδ in response to its activation. J Biol Chem 1994; 269: 2349-2352.
    • (1994) J Biol Chem , vol.269 , pp. 2349-2352
    • Li, W.1    Mischak, H.2    Yu, J.C.3
  • 82
    • 0032474741 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line: Regulation of Src family kinase activity by protein kinase C-δ
    • Song JS, Swann PG, Szallasi Z, Blank U, Blumberg PM, Rivera J. Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line: Regulation of Src family kinase activity by protein kinase C-δ. Oncogene 1998; 16: 3357-3368.
    • (1998) Oncogene , vol.16 , pp. 3357-3368
    • Song, J.S.1    Swann, P.G.2    Szallasi, Z.3    Blank, U.4    Blumberg, P.M.5    Rivera, J.6
  • 83
    • 0032515055 scopus 로고    scopus 로고
    • Protein kinase Cδ (PKCdelta) inhibits the expression of glutamine synthetase in glial cells via the PKCδ regulatory domain and its tyrosine phosphorylation
    • Brodie C, Bogi K, Acs P, Lorenzo PS, Baskin L, Blumberg PM. Protein kinase Cδ (PKCdelta) inhibits the expression of glutamine synthetase in glial cells via the PKCδ regulatory domain and its tyrosine phosphorylation. J Biol Chem 1998; 273: 30713-30718.
    • (1998) J Biol Chem , vol.273 , pp. 30713-30718
    • Brodie, C.1    Bogi, K.2    Acs, P.3    Lorenzo, P.S.4    Baskin, L.5    Blumberg, P.M.6
  • 85
    • 0029924152 scopus 로고    scopus 로고
    • Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase Cδ
    • Denning MF, Dlugosz AA, Threadgill DW, Magnuson T, Yuspa SH. Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase Cδ. J Biol Chem 1996; 271: 5325-5331.
    • (1996) J Biol Chem , vol.271 , pp. 5325-5331
    • Denning, M.F.1    Dlugosz, A.A.2    Threadgill, D.W.3    Magnuson, T.4    Yuspa, S.H.5
  • 86
    • 0031684848 scopus 로고    scopus 로고
    • Protein kinase Cδ is an important signaling molecule in insulin-like growth factor receptor-mediated cell transformation
    • Li W, Jiang YX, Zhang J, et al. Protein kinase Cδ is an important signaling molecule in insulin-like growth factor receptor-mediated cell transformation. Mol Cell Biol 1998; 18: 5888-5898.
    • (1998) Mol Cell Biol , vol.18 , pp. 5888-5898
    • Li, W.1    Jiang, Y.X.2    Zhang, J.3
  • 87
    • 0037023769 scopus 로고    scopus 로고
    • Src family kinases phosphorylate protein kinase Cδ on tyrosine residues and modify the neoplastic phenotype of skin keratinocytes
    • Joseloff E, Cataisson C, Aamodt H, et al. Src family kinases phosphorylate protein kinase Cδ on tyrosine residues and modify the neoplastic phenotype of skin keratinocytes. J Biol Chem 2002; 277: 12318-12323.
    • (2002) J Biol Chem , vol.277 , pp. 12318-12323
    • Joseloff, E.1    Cataisson, C.2    Aamodt, H.3
  • 89
    • 0035907396 scopus 로고    scopus 로고
    • Targeting of the cAbl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress
    • Kumar S, Bharti A, Mishra NC, et al. Targeting of the cAbl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress. J Biol Chem 2001; 276: 17281-17285.
    • (2001) J Biol Chem , vol.276 , pp. 17281-17285
    • Kumar, S.1    Bharti, A.2    Mishra, N.C.3
  • 90
    • 0033600235 scopus 로고    scopus 로고
    • p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage
    • Yuan ZM, Shioya H, Ishiko T, et al. p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage. Nature 1999; 399: 814-817.
    • (1999) Nature , vol.399 , pp. 814-817
    • Yuan, Z.M.1    Shioya, H.2    Ishiko, T.3
  • 91
    • 0037072483 scopus 로고    scopus 로고
    • p73β is regulated by the protein kinase Cδ catalytic fragment generated in the apoptotic response to DNA damage
    • in press
    • Ren J, Datta R, Shioya H, et al. p73β is regulated by the protein kinase Cδ catalytic fragment generated in the apoptotic response to DNA damage. J Biol Chem 2002; (in press).
    • (2002) J Biol Chem
    • Ren, J.1    Datta, R.2    Shioya, H.3
  • 92
    • 0030006084 scopus 로고    scopus 로고
    • The stress response to ionizing radiation involves c-Abl-dependent phosphorylation of SHPTP1
    • Kharbanda S, Bharti A, Pei D, et al. The stress response to ionizing radiation involves c-Abl-dependent phosphorylation of SHPTP1. Proc Natl Acad Sci USA 1996; 93: 6898-6901.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6898-6901
    • Kharbanda, S.1    Bharti, A.2    Pei, D.3
  • 93
    • 0035216604 scopus 로고    scopus 로고
    • Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase Cδ in response to DNA damage
    • Yoshida K, Kufe D. Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase Cδ in response to DNA damage. Mol Pharmacol 2001; 60: 1431-1438.
    • (2001) Mol Pharmacol , vol.60 , pp. 1431-1438
    • Yoshida, K.1    Kufe, D.2
  • 95
    • 0034517792 scopus 로고    scopus 로고
    • Activation of PKC is sufficient to induce an apoptotic program in salivary gland acinar cells
    • Reyland ME, Barzen KA, Anderson SM, Quissell DO, Matassa AA. Activation of PKC is sufficient to induce an apoptotic program in salivary gland acinar cells. Cell Death Differ 2000; 7: 1200-1209.
    • (2000) Cell Death Differ , vol.7 , pp. 1200-1209
    • Reyland, M.E.1    Barzen, K.A.2    Anderson, S.M.3    Quissell, D.O.4    Matassa, A.A.5
  • 96
    • 0035931889 scopus 로고    scopus 로고
    • PKCδ mediates ionizing radiation-induced activation of c-Jun NH(2)terminal kinase through MKK7 in human thyroid cells
    • Mitsutake N, Namba H, Shklyaev SS, et al. PKCδ mediates ionizing radiation-induced activation of c-Jun NH(2)terminal kinase through MKK7 in human thyroid cells. Oncogene 2001; 20: 989-996.
    • (2001) Oncogene , vol.20 , pp. 989-996
    • Mitsutake, N.1    Namba, H.2    Shklyaev, S.S.3
  • 97
    • 0037034186 scopus 로고    scopus 로고
    • Downregulating PKCδ provides a PI3K/Akt-independent survival signal that overcomes apoptotic signals generated by c-Src overexpression
    • Zhong M, Lu Z, Foster DA. Downregulating PKCδ provides a PI3K/Akt-independent survival signal that overcomes apoptotic signals generated by c-Src overexpression. Oncogene 2002; 21: 1071-1078.
    • (2002) Oncogene , vol.21 , pp. 1071-1078
    • Zhong, M.1    Lu, Z.2    Foster, D.A.3
  • 98
    • 0030849152 scopus 로고    scopus 로고
    • Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids
    • Zhou O, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ. Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem 1997; 272: 18240-18244.
    • (1997) J Biol Chem , vol.272 , pp. 18240-18244
    • Zhou, O.1    Zhao, J.2    Stout, J.G.3    Luhm, R.A.4    Wiedmer, T.5    Sims, P.J.6
  • 99
    • 0034725570 scopus 로고    scopus 로고
    • Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cδ
    • Frasch SC, Henson PM, Kailey JM, et al. Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cδ. J Biol Chem 2000; 275: 23065-23073.
    • (2000) J Biol Chem , vol.275 , pp. 23065-23073
    • Frasch, S.C.1    Henson, P.M.2    Kailey, J.M.3
  • 100
    • 85047683702 scopus 로고    scopus 로고
    • Protein kinase Cδ amplifies ceramide formation via mitochondrial signaling in prostate cancer cells
    • Sumitomo M, Ohba M, Asakuma J, et al. Protein kinase Cδ amplifies ceramide formation via mitochondrial signaling in prostate cancer cells. J Clin Invest 2002; 109: 827-836.
    • (2002) J Clin Invest , vol.109 , pp. 827-836
    • Sumitomo, M.1    Ohba, M.2    Asakuma, J.3
  • 101
    • 0033560796 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase
    • Smith GCM, Jackson SP. The DNA-dependent protein kinase. Genes & Dev. 1999; 13: 916-934.
    • (1999) Genes & Dev , vol.13 , pp. 916-934
    • Smith, G.C.M.1    Jackson, S.P.2
  • 102
    • 0030945148 scopus 로고    scopus 로고
    • Functional interaction of DNA-PK and c-Abl in response to DNA damage
    • Kharbanda S, Pandey P, Jin S, et al. Functional interaction of DNA-PK and c-Abl in response to DNA damage. Nature 1997; 386: 732-735.
    • (1997) Nature , vol.386 , pp. 732-735
    • Kharbanda, S.1    Pandey, P.2    Jin, S.3
  • 103
    • 0031795922 scopus 로고    scopus 로고
    • Inactivation of DNA-dependent protein kinase by protein kinase Cδ: Implications for apoptosis
    • Bharti A, Kraeft SK, Gounder M, et al. Inactivation of DNA-dependent protein kinase by protein kinase Cδ: Implications for apoptosis. Mol Cell Biol 1998; 18: 6719-6728.
    • (1998) Mol Cell Biol , vol.18 , pp. 6719-6728
    • Bharti, A.1    Kraeft, S.K.2    Gounder, M.3
  • 104
    • 0024470862 scopus 로고
    • Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: A cautionary note
    • Kaufmann SH. Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: A cautionary note. Cancer Res 1989; 49: 5870-5878.
    • (1989) Cancer Res , vol.49 , pp. 5870-5878
    • Kaufmann, S.H.1
  • 105
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M, Nakagawa J, Doree M, Labbe JC, Nigg EA. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 1990; 61: 591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.