메뉴 건너뛰기




Volumn 16, Issue 10, 2007, Pages 1693-1707

The therapeutic role of targeting protein kinase C in solid and hematologic malignancies

Author keywords

Activators; Inhibitors; Protein kinase C; Tumorigenesis

Indexed keywords

ANTINEOPLASTIC AGENT; ASCORBIC ACID; BORTEZOMIB; BRYOSTATIN 1; CARBOPLATIN; CISPLATIN; CURCUMIN; CYTARABINE; DEHYDRODIDEMNIN B; DEXAMETHASONE; ENZASTAURIN; FLUDARABINE; GEMCITABINE; ISIS 3521; LENALIDOMIDE; LY 9000003; MELPHALAN; MIDOSTAURIN; PACLITAXEL; PEP 005; PEPLIN; PLACEBO; PROTEIN KINASE C; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA; PROTEIN KINASE C DELTA; PROTEIN KINASE C EPSILON; RESVERATROL; RETINOL; RITUXIMAB; TAMOXIFEN; UNCLASSIFIED DRUG; UNINDEXED DRUG; ISOENZYME;

EID: 35248870218     PISSN: 13543784     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543784.16.10.1693     Document Type: Article
Times cited : (53)

References (194)
  • 1
    • 84965812126 scopus 로고
    • The mechnism of carcinogenesis: A study of the significance of carcinogenic action and related phenomena
    • BERENBLUM I: The mechnism of carcinogenesis: a study of the significance of carcinogenic action and related phenomena. Cancer Res. (1941) 1(1):807-814.
    • (1941) Cancer Res , vol.1 , Issue.1 , pp. 807-814
    • BERENBLUM, I.1
  • 2
    • 0020326790 scopus 로고
    • Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters
    • CASTAGNA M, TAKAI Y, KAIBUCHI K et al.: Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters. J. Biol. Chem. (1982) 257(13):7847-7851.
    • (1982) J. Biol. Chem , vol.257 , Issue.13 , pp. 7847-7851
    • CASTAGNA, M.1    TAKAI, Y.2    KAIBUCHI, K.3
  • 3
    • 0003053406 scopus 로고
    • Characterization of a specific phorbol ester aporeceptor in mouse brain cytosol
    • LEACH KL, JAMES ML, BLUMBERG PM: Characterization of a specific phorbol ester aporeceptor in mouse brain cytosol. Proc. Natl. Acad. Sci. USA (1983) 80(14):4208-4212.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , Issue.14 , pp. 4208-4212
    • LEACH, K.L.1    JAMES, M.L.2    BLUMBERG, P.M.3
  • 4
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • NISHIZUKA Y: The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature (1984) 308(5961):693-698.
    • (1984) Nature , vol.308 , Issue.5961 , pp. 693-698
    • NISHIZUKA, Y.1
  • 5
    • 0037303088 scopus 로고    scopus 로고
    • Discovery and prospect of protein kinase C research: Epilogue
    • NISHIZUKA Y: Discovery and prospect of protein kinase C research: epilogue. J. Biochem. (Tokyo) (2003) 133(2):155-158.
    • (2003) J. Biochem. (Tokyo) , vol.133 , Issue.2 , pp. 155-158
    • NISHIZUKA, Y.1
  • 6
    • 1842394775 scopus 로고
    • Competitive inhibition by diacylglycerol of specific phorbol ester binding
    • SHARKEY NA, LEACH KL, BLUMBERG PM: Competitive inhibition by diacylglycerol of specific phorbol ester binding. Proc. Natl. Acad. Sci. USA (1984) 81(2):607-610.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , Issue.2 , pp. 607-610
    • SHARKEY, N.A.1    LEACH, K.L.2    BLUMBERG, P.M.3
  • 7
    • 33947603008 scopus 로고    scopus 로고
    • Protein kinase C and other diacylglycerol effectors in cancer
    • GRINER EM, KAZANIETZ MG: Protein kinase C and other diacylglycerol effectors in cancer. Nat. Rev. Cancer (2007) 7(4):281-294.
    • (2007) Nat. Rev. Cancer , vol.7 , Issue.4 , pp. 281-294
    • GRINER, E.M.1    KAZANIETZ, M.G.2
  • 8
    • 34250902930 scopus 로고    scopus 로고
    • Targeting the protein kinase C family: Are we there yet?
    • MACKAY HJ, TWELVES CJ: Targeting the protein kinase C family: are we there yet? Nat. Rev. Cancer (2007) 7(7):554-562.
    • (2007) Nat. Rev. Cancer , vol.7 , Issue.7 , pp. 554-562
    • MACKAY, H.J.1    TWELVES, C.J.2
  • 9
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • NISHIZUKA Y: Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. (1995) 9(7):484-496.
    • (1995) FASEB J , vol.9 , Issue.7 , pp. 484-496
    • NISHIZUKA, Y.1
  • 10
    • 85176674494 scopus 로고    scopus 로고
    • TSUTAKAWA SE, MEDZIHRADSZKY KF, FLINT AJ, BURLINGAME AL, KOSHLAND DE Jr: Determination of in vivo phosphorylation sites in protein kinase C. J. Biol. Chem. (1995) 270(45):26807-26812.
    • TSUTAKAWA SE, MEDZIHRADSZKY KF, FLINT AJ, BURLINGAME AL, KOSHLAND DE Jr: Determination of in vivo phosphorylation sites in protein kinase C. J. Biol. Chem. (1995) 270(45):26807-26812.
  • 11
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • KERANEN LM, DUTIL EM, NEWTON AC: Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr. Biol. (1995) 5(12):1394-1403.
    • (1995) Curr. Biol , vol.5 , Issue.12 , pp. 1394-1403
    • KERANEN, L.M.1    DUTIL, E.M.2    NEWTON, A.C.3
  • 12
    • 0030250879 scopus 로고    scopus 로고
    • Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase C-α
    • BORNANCIN F, PARKER PJ: Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase C-α. Curr. Biol. (1996) 6(9):1114-1123.
    • (1996) Curr. Biol , vol.6 , Issue.9 , pp. 1114-1123
    • BORNANCIN, F.1    PARKER, P.J.2
  • 13
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state
    • BORNANCIN F, PARKER PJ: Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state. J. Biol. Chem. (1997) 272(6):3544-3549.
    • (1997) J. Biol. Chem , vol.272 , Issue.6 , pp. 3544-3549
    • BORNANCIN, F.1    PARKER, P.J.2
  • 14
    • 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 et al.: Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science (1998) 281(5385):2042-2045.
    • (1998) Science , vol.281 , Issue.5385 , pp. 2042-2045
    • LE GOOD, J.A.1    ZIEGLER, W.H.2    PAREKH, D.B.3
  • 15
    • 0033565608 scopus 로고    scopus 로고
    • The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation
    • BEHN-KRAPPA A, NEWTON AC: The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation. Curr. Biol. (1999) 9(14):728-737.
    • (1999) Curr. Biol , vol.9 , Issue.14 , pp. 728-737
    • BEHN-KRAPPA, A.1    NEWTON, A.C.2
  • 16
    • 0032538539 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites required for protein kinase D activation
    • IGLESIAS T, WALDRON RT, ROZENGURT E: Identification of in vivo phosphorylation sites required for protein kinase D activation. J. Biol. Chem. (1998) 273(42):27662-27667.
    • (1998) J. Biol. Chem , vol.273 , Issue.42 , pp. 27662-27667
    • IGLESIAS, T.1    WALDRON, R.T.2    ROZENGURT, E.3
  • 18
    • 0033543570 scopus 로고    scopus 로고
    • Characterization of serin 916 as an in vivo autophosphorylation site for protein kinase D/protein kinase C-μ
    • MATTHEWS SA, ROZENGURT E, CANTRELL D: Characterization of serin 916 as an in vivo autophosphorylation site for protein kinase D/protein kinase C-μ. J. Biol. Chem. (1999) 274(37):26543-26549.
    • (1999) J. Biol. Chem , vol.274 , Issue.37 , pp. 26543-26549
    • MATTHEWS, S.A.1    ROZENGURT, E.2    CANTRELL, D.3
  • 19
    • 0027964870 scopus 로고
    • Molecular cloning and characterization of protein kinase D: A target for diacylglycerol and phorbol esters with a distinctive catalytic domain
    • VALVERDE AM, SINNETT-SMITH J, VAN LINT J, ROZENGURT E: Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain. Proc. Natl. Acad. Sci. USA (1994) 91(18):8572-8576.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.18 , pp. 8572-8576
    • VALVERDE, A.M.1    SINNETT-SMITH, J.2    VAN LINT, J.3    ROZENGURT, E.4
  • 20
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrates
    • BLACKSHEAR PJ: The MARCKS family of cellular protein kinase C substrates. J. Biol. Chem. (1993) 268(3):1501-1504.
    • (1993) J. Biol. Chem , vol.268 , Issue.3 , pp. 1501-1504
    • BLACKSHEAR, P.J.1
  • 21
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • MOCHLY-ROSEN D: Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science (1995) 268(5208):247-251.
    • (1995) Science , vol.268 , Issue.5208 , pp. 247-251
    • MOCHLY-ROSEN, D.1
  • 22
    • 0033119158 scopus 로고    scopus 로고
    • Pharmacologic modulation of protein kinase C isozymes: The role of RACKs and subcellular localisation
    • CSUKAI M, MOCHLY-ROSEN D: Pharmacologic modulation of protein kinase C isozymes: the role of RACKs and subcellular localisation. Pharmacol. Res. (1999) 39(4):253-259.
    • (1999) Pharmacol. Res , vol.39 , Issue.4 , pp. 253-259
    • CSUKAI, M.1    MOCHLY-ROSEN, D.2
  • 23
    • 0034194092 scopus 로고    scopus 로고
    • Identification of PKC-isoform-specific biological actions using pharmacological approaches
    • WAY KJ, CHOU E, KING GL: Identification of PKC-isoform-specific biological actions using pharmacological approaches. Trends Pharmacol. Sci. (2000) 21(5):181-187.
    • (2000) Trends Pharmacol. Sci , vol.21 , Issue.5 , pp. 181-187
    • WAY, K.J.1    CHOU, E.2    KING, G.L.3
  • 24
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • NISHIZUKA Y: Studies and perspectives of protein kinase C. Science (1986) 233(4761):305-312.
    • (1986) Science , vol.233 , Issue.4761 , pp. 305-312
    • NISHIZUKA, Y.1
  • 25
    • 0024416291 scopus 로고
    • The Albert Lasker medical awards. The family of protein kinase C for signal transduction
    • NISHIZUKA Y: The Albert Lasker medical awards. The family of protein kinase C for signal transduction. JAMA (1989) 262(13):1826-1833.
    • (1989) JAMA , vol.262 , Issue.13 , pp. 1826-1833
    • NISHIZUKA, Y.1
  • 27
    • 0028082161 scopus 로고
    • Protein kinase C - a question of specificity
    • DEKKER LV, PARKER PJ: Protein kinase C - a question of specificity. Trends Biochem. Sci. (1994) 19(2):73-77.
    • (1994) Trends Biochem. Sci , vol.19 , Issue.2 , pp. 73-77
    • DEKKER, L.V.1    PARKER, P.J.2
  • 28
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • NEWTON AC: Protein kinase C: structure, function, and regulation. J. Biol. Chem. (1995) 270(48):28495-28498.
    • (1995) J. Biol. Chem , vol.270 , Issue.48 , pp. 28495-28498
    • NEWTON, A.C.1
  • 29
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • NEWTON AC: Regulation of protein kinase C. Curr. Opin. Cell Biol. (1997) 9(2):161-167.
    • (1997) Curr. Opin. Cell Biol , vol.9 , Issue.2 , pp. 161-167
    • NEWTON, A.C.1
  • 30
    • 0034168037 scopus 로고    scopus 로고
    • Protein kinase C-mediated regulation of the cell cycle
    • BLACK JD: Protein kinase C-mediated regulation of the cell cycle. Front Biosci. (2000) 5:D406-D423.
    • (2000) Front Biosci , vol.5
    • BLACK, J.D.1
  • 31
    • 0024323584 scopus 로고
    • Elevated protein kinase C expression in human breast tumor biopsies relative to normal breast tissue
    • O'BRIAN C. VOGEL VG, SINGLETARY SE, WARD NE: Elevated protein kinase C expression in human breast tumor biopsies relative to normal breast tissue. Cancer Res. (1989) 49(12):3215-3217.
    • (1989) Cancer Res , vol.49 , Issue.12 , pp. 3215-3217
    • O'BRIAN, C.1    VOGEL, V.G.2    SINGLETARY, S.E.3    WARD, N.E.4
  • 32
    • 0022653769 scopus 로고
    • Effects of 12-O-tetradecanoylphorbol-13-acetate on adhesiveness and lung-colonizing ability of Lewis lung carcinoma cells
    • TAKENAGA K, TAKAHASHI K: Effects of 12-O-tetradecanoylphorbol-13-acetate on adhesiveness and lung-colonizing ability of Lewis lung carcinoma cells. Cancer Res. (1986) 46(1):375-380.
    • (1986) Cancer Res , vol.46 , Issue.1 , pp. 375-380
    • TAKENAGA, K.1    TAKAHASHI, K.2
  • 33
    • 0027536464 scopus 로고
    • Protein kinase C: A novel target for inhibiting gastric cancer cell invasion
    • SCHWARTZ GK, JIANG J, KELSEN D, ALBINO AP: Protein kinase C: a novel target for inhibiting gastric cancer cell invasion. J. Natl. Cancer Inst. (1993) 85(5):402-407.
    • (1993) J. Natl. Cancer Inst , vol.85 , Issue.5 , pp. 402-407
    • SCHWARTZ, G.K.1    JIANG, J.2    KELSEN, D.3    ALBINO, A.P.4
  • 34
    • 0035866371 scopus 로고    scopus 로고
    • Elevated protein kinase C-βII is an early promotive event in colon carcinogenesis
    • GOKMEN-POLAR Y, MURRAY NR, VELASCO MA, GATALICA Z, FIELDS AP: Elevated protein kinase C-βII is an early promotive event in colon carcinogenesis. Cancer Res. (2001) 61(4):1375-1381.
    • (2001) Cancer Res , vol.61 , Issue.4 , pp. 1375-1381
    • GOKMEN-POLAR, Y.1    MURRAY, N.R.2    VELASCO, M.A.3    GATALICA, Z.4    FIELDS, A.P.5
  • 35
    • 0036177115 scopus 로고    scopus 로고
    • Targeting protein kinase C: New therapeutic opportunities against high-grade malignant gliomas?
    • DA ROCHA AB, MANS DR, REGNER A, SCHWARTSMANN G: Targeting protein kinase C: new therapeutic opportunities against high-grade malignant gliomas? Oncologist (2002) 7(1):17-33.
    • (2002) Oncologist , vol.7 , Issue.1 , pp. 17-33
    • DA ROCHA, A.B.1    MANS, D.R.2    REGNER, A.3    SCHWARTSMANN, G.4
  • 36
    • 8944231156 scopus 로고    scopus 로고
    • Inhibition of growth of human tumor cell lines in nude mice by an antisense of oligonucleotide inhibitor of protein kinase C-α expression
    • DEAN N, MCKAY R, MIRAGLIA L et al.: Inhibition of growth of human tumor cell lines in nude mice by an antisense of oligonucleotide inhibitor of protein kinase C-α expression. Cancer Res. (1996) 56(15):3499-3507.
    • (1996) Cancer Res , vol.56 , Issue.15 , pp. 3499-3507
    • DEAN, N.1    MCKAY, R.2    MIRAGLIA, L.3
  • 37
    • 18244409933 scopus 로고    scopus 로고
    • Diffuse large B-cell lymphoma outcome prediction by gene-expression profiling and supervised machine learning
    • SHIPP MA, ROSS KN, TAMAYO P et al.: Diffuse large B-cell lymphoma outcome prediction by gene-expression profiling and supervised machine learning. Nat. Med. (2002) 8(1):68-74.
    • (2002) Nat. Med , vol.8 , Issue.1 , pp. 68-74
    • SHIPP, M.A.1    ROSS, K.N.2    TAMAYO, P.3
  • 38
    • 25144466151 scopus 로고    scopus 로고
    • Expression of PKC-β or cyclin D2 predicts for inferior survival in diffuse large B-cell lymphoma
    • HANS CP, WEISENBURGER DD, GREINER TC et al.: Expression of PKC-β or cyclin D2 predicts for inferior survival in diffuse large B-cell lymphoma. Mod. Pathol. (2005) 18(10):1377-1384.
    • (2005) Mod. Pathol , vol.18 , Issue.10 , pp. 1377-1384
    • HANS, C.P.1    WEISENBURGER, D.D.2    GREINER, T.C.3
  • 39
    • 13944266008 scopus 로고    scopus 로고
    • PKC-θ mediates pre-TCR signaling and contributes to Notch3-induced T-cell leukemia
    • FELLI MP, VACCA A, CALCE A et al.: PKC-θ mediates pre-TCR signaling and contributes to Notch3-induced T-cell leukemia. Oncogene (2005) 24(6):992-1000.
    • (2005) Oncogene , vol.24 , Issue.6 , pp. 992-1000
    • FELLI, M.P.1    VACCA, A.2    CALCE, A.3
  • 40
    • 0037145725 scopus 로고    scopus 로고
    • Differential expression of protein kinase C isoenzymes related to high nitric oxide synthase activity in a T lymphoma cell line
    • GORELIK G, BARREIRO ARCOS ML, KLECHA AJ, CREMASCHI GA: Differential expression of protein kinase C isoenzymes related to high nitric oxide synthase activity in a T lymphoma cell line. Biochim. Biophys. Acta (2002) 1588(2):179-188.
    • (2002) Biochim. Biophys. Acta , vol.1588 , Issue.2 , pp. 179-188
    • GORELIK, G.1    BARREIRO ARCOS ML2    KLECHA, A.J.3    CREMASCHE, G.A.4
  • 41
    • 0033248120 scopus 로고    scopus 로고
    • Protein kinase C-θ cooperates with calcineurin to induce Fas ligand expression during activation-induced T cell death
    • VILLALBA M, KASIBHATLA S, GENESTIER. L et al.: Protein kinase C-θ cooperates with calcineurin to induce Fas ligand expression during activation-induced T cell death. J. Immunol. (1999) 163(11):5813-5819.
    • (1999) J. Immunol , vol.163 , Issue.11 , pp. 5813-5819
    • VILLALBA, M.1    KASIBHATLA, S.2    GENESTIER, L.3
  • 42
    • 0025075255 scopus 로고
    • Abnormal behavior of Protein kinase C in the human myeloma cell line, RPMI 8226
    • PARANT MR, KLEIN B, VIAL H: Abnormal behavior of Protein kinase C in the human myeloma cell line, RPMI 8226. FEBS Lett. (1990) 269(2):331-335.
    • (1990) FEBS Lett , vol.269 , Issue.2 , pp. 331-335
    • PARANT, M.R.1    KLEIN, B.2    VIAL, H.3
  • 43
    • 0038268137 scopus 로고    scopus 로고
    • Protein kinase C-δ is commonly expressed in multiple myeloma cells and its downregulation by rottlerin causes apoptosis
    • NI H, ERGIN M, TIBUDAN SS et al.: Protein kinase C-δ is commonly expressed in multiple myeloma cells and its downregulation by rottlerin causes apoptosis. Br. J. Haematol. (2003) 121(6):849-856.
    • (2003) Br. J. Haematol , vol.121 , Issue.6 , pp. 849-856
    • NI, H.1    ERGIN, M.2    TIBUDAN, S.S.3
  • 44
    • 0035881511 scopus 로고    scopus 로고
    • Protein kinase C-δ and η isoenzymes control the shedding of the interleukin 6 receptor α in myeloma cells
    • THABARD W, COLLETTE M, BATAILLE R, AMIOT M: Protein kinase C-δ and η isoenzymes control the shedding of the interleukin 6 receptor α in myeloma cells. Biochem. J. (2001) 358(Part 1):193-200.
    • (2001) Biochem. J , vol.358 , Issue.PART 1 , pp. 193-200
    • THABARD, W.1    COLLETTE, M.2    BATAILLE, R.3    AMIOT, M.4
  • 45
    • 18544377343 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-induced migration of multiple myeloma cells is associated with β1 integrin- and phosphatidylinositol 3-kinasc-dependent PKC-α activation
    • PODAR K, TAI YT, LIN BK et al.: Vascular endothelial growth factor-induced migration of multiple myeloma cells is associated with β1 integrin- and phosphatidylinositol 3-kinasc-dependent PKC-α activation. J. Biol. Chem. (2002) 277(10):7875-7881.
    • (2002) J. Biol. Chem , vol.277 , Issue.10 , pp. 7875-7881
    • PODAR, K.1    TAI, Y.T.2    LIN, B.K.3
  • 46
    • 23944524848 scopus 로고    scopus 로고
    • Wnts induce migration and invasion of myeloma plasma cells
    • QIANG YW, WALSH K. YAO L et al.: Wnts induce migration and invasion of myeloma plasma cells. Blood (2005) 106(5):1786-1793.
    • (2005) Blood , vol.106 , Issue.5 , pp. 1786-1793
    • QIANG, Y.W.1    WALSH, K.Y.L.2
  • 47
    • 15144349717 scopus 로고    scopus 로고
    • Cytochrome C-dependent and -independent induction of apoptosis in multiple myeloma cells
    • CHAUHAN D, PANDEY P, OGATA A et al.: Cytochrome C-dependent and -independent induction of apoptosis in multiple myeloma cells. J. Biol. Chem. (1997) 272(48):29995-29997.
    • (1997) J. Biol. Chem , vol.272 , Issue.48 , pp. 29995-29997
    • CHAUHAN, D.1    PANDEY, P.2    OGATA, A.3
  • 48
    • 13544255403 scopus 로고    scopus 로고
    • The pathophysiologic role of VEGF in hematologic malignancies: Therapeutic implications
    • PODAR K, ANDERSON KC: The pathophysiologic role of VEGF in hematologic malignancies: therapeutic implications. Blood (2005) 105(4):1383-1395.
    • (2005) Blood , vol.105 , Issue.4 , pp. 1383-1395
    • PODAR, K.1    ANDERSON, K.C.2
  • 49
    • 22044440425 scopus 로고    scopus 로고
    • Cyclin D dysregulation: An early and unifying pathogenic event in multiple myeloma
    • BERGSAGEL PL, KUEHL WM, ZRAN F et al.: Cyclin D dysregulation: an early and unifying pathogenic event in multiple myeloma. Blood (2005) 106(1):296-303.
    • (2005) Blood , vol.106 , Issue.1 , pp. 296-303
    • BERGSAGEL, P.L.1    KUEHL, W.M.2    ZRAN, F.3
  • 50
    • 4444225963 scopus 로고    scopus 로고
    • A global expression-based analysis of the consequences of the t(4;14) translocation in myeloma
    • DRING AM, DAVIES FE, FENTON JA et al.: A global expression-based analysis of the consequences of the t(4;14) translocation in myeloma. Clin. Cancer Res. (2004) 10(17):5692-5701.
    • (2004) Clin. Cancer Res , vol.10 , Issue.17 , pp. 5692-5701
    • DRING, A.M.1    DAVIES, F.E.2    FENTON, J.A.3
  • 51
    • 33846914141 scopus 로고    scopus 로고
    • Targeting PKC in multiple myeloma: In vitro and in vivo effects of the novel, orally available small-molecule inhibitor enzastaurin (LY317615.HCl)
    • PODAR K, RAAB MS, ZHANG J et al.: Targeting PKC in multiple myeloma: in vitro and in vivo effects of the novel, orally available small-molecule inhibitor enzastaurin (LY317615.HCl). Blood (2007) 109(4):1669-1677.
    • (2007) Blood , vol.109 , Issue.4 , pp. 1669-1677
    • PODAR, K.1    RAAB, M.S.2    ZHANG, J.3
  • 52
    • 10044298444 scopus 로고    scopus 로고
    • The link between PKC-α regulation and cellular transformation
    • MICHIE AM, NAKAGAWA R. The link between PKC-α regulation and cellular transformation. Immunol. Lett. (2005) 96(2):155-162.
    • (2005) Immunol. Lett , vol.96 , Issue.2 , pp. 155-162
    • MICHIE, A.M.1    NAKAGAWA, R.2
  • 53
    • 0030946540 scopus 로고    scopus 로고
    • Protein kinase C isozyme-mediated cell cycle arrest involves induction of p21 (waf1/cip1) and p27(kip1) and hypophosphorylation of the retinoblastoma protein in intestinal epithelial cells
    • FREY MR, SAXON ML, ZHAO X et al.: Protein kinase C isozyme-mediated cell cycle arrest involves induction of p21 (waf1/cip1) and p27(kip1) and hypophosphorylation of the retinoblastoma protein in intestinal epithelial cells. J. Biol. Chem. (1997) 272(14):9424-9435.
    • (1997) J. Biol. Chem , vol.272 , Issue.14 , pp. 9424-9435
    • FREY, M.R.1    SAXON, M.L.2    ZHAO, X.3
  • 54
    • 0033828604 scopus 로고    scopus 로고
    • Activation of protein kinase C-α inhibits growth of pancreatic cancer cells via p21 (cip)-mediated G(1) arrest
    • DETJEN KM, BREMBECK FH, WELZEL M et al.: Activation of protein kinase C-α inhibits growth of pancreatic cancer cells via p21 (cip)-mediated G(1) arrest. J. Cell Sci. (2000) 113(Part 17):3025-3035.
    • (2000) J. Cell Sci , vol.113 , Issue.PART 17 , pp. 3025-3035
    • DETJEN, K.M.1    BREMBECK, F.H.2    WELZEL, M.3
  • 55
    • 0033581829 scopus 로고    scopus 로고
    • The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells
    • SLOSBERG ED, KLEIN MG, YAO Y et al.: The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells. Oncogene (1999) 18(48):6658-6666.
    • (1999) Oncogene , vol.18 , Issue.48 , pp. 6658-6666
    • SLOSBERG, E.D.1    KLEIN, M.G.2    YAO, Y.3
  • 56
    • 33746909044 scopus 로고    scopus 로고
    • Protein kinase C-α but not PKC-ζ suppresses intestinal tumor formation in ApcMin/+ mice
    • OSTER H, LEITGES M: Protein kinase C-α but not PKC-ζ suppresses intestinal tumor formation in ApcMin/+ mice. Cancer Res. (2006) 66(14):6955-6963.
    • (2006) Cancer Res , vol.66 , Issue.14 , pp. 6955-6963
    • OSTER, H.1    LEITGES, M.2
  • 57
    • 0027326410 scopus 로고
    • Protein kinase C-α activates RAF-1 by direct phosphorylation
    • KOLCH W, HEIDECKER G, KOCHS G et al.: Protein kinase C-α activates RAF-1 by direct phosphorylation. Nature (1993) 364(6434):249-252.
    • (1993) Nature , vol.364 , Issue.6434 , pp. 249-252
    • KOLCH, W.1    HEIDECKER, G.2    KOCHS, G.3
  • 58
    • 0032566717 scopus 로고    scopus 로고
    • A functional role for mitochondrial protein kinase C-α in Bcl2 phosphorylation and suppression of apoptosis
    • RUVOLO PP, DENG X, CARR BK, MAY WS: A functional role for mitochondrial protein kinase C-α in Bcl2 phosphorylation and suppression of apoptosis. J. Biol Chem. (1998) 273(39):25436-25442.
    • (1998) J. Biol Chem , vol.273 , Issue.39 , pp. 25436-25442
    • RUVOLO, P.P.1    DENG, X.2    CARR, B.K.3    MAY, W.S.4
  • 59
    • 0033542806 scopus 로고    scopus 로고
    • Antisense inhibition of protein kinase C-α reverses the transformed phenotype in human lung carcinoma cells
    • WANG XY, REPASKY E, LIU HT: Antisense inhibition of protein kinase C-α reverses the transformed phenotype in human lung carcinoma cells. Exp. Cell Res. (1999) 250(1):253-263.
    • (1999) Exp. Cell Res , vol.250 , Issue.1 , pp. 253-263
    • WANG, X.Y.1    REPASKY, E.2    LIU, H.T.3
  • 60
    • 0027256373 scopus 로고
    • Expression of the antisense cDNA for protein kinase C-α attenuates resistance in doxorubicin-resistant MCF-7 breast carcinoma cells
    • AHMAD S, GLAZER RI: Expression of the antisense cDNA for protein kinase C-α attenuates resistance in doxorubicin-resistant MCF-7 breast carcinoma cells. Mol. Pharmacol. (1993) 43(6):858-862.
    • (1993) Mol. Pharmacol , vol.43 , Issue.6 , pp. 858-862
    • AHMAD, S.1    GLAZER, R.I.2
  • 61
    • 0033618911 scopus 로고    scopus 로고
    • Protein kinase C-α promotes apoptotic cell death in gastric cancer cells depending upon loss of anchorage
    • OKUDA H, ADACHI M, MIYAZAWA M, HINODA Y, IMAI K: Protein kinase C-α promotes apoptotic cell death in gastric cancer cells depending upon loss of anchorage. Oncogene (1999) 18(40):5604-5609.
    • (1999) Oncogene , vol.18 , Issue.40 , pp. 5604-5609
    • OKUDA, H.1    ADACHI, M.2    MIYAZAWA, M.3    HINODA, Y.4    IMAI, K.5
  • 62
    • 0028903545 scopus 로고
    • MCF-7 breast cancer cells transfected with protein kinase C-α exhibit altered expression of other protein kinase C isoforms and display a more aggressive neoplastic phenotype
    • WAYS DK, KUKOLY CA, DEVENTE J et al.: MCF-7 breast cancer cells transfected with protein kinase C-α exhibit altered expression of other protein kinase C isoforms and display a more aggressive neoplastic phenotype. J. Clin. Invest. (1995) 95(4):1906-1915.
    • (1995) J. Clin. Invest , vol.95 , Issue.4 , pp. 1906-1915
    • WAYS, D.K.1    KUKOLY, C.A.2    DEVENTE, J.3
  • 63
    • 0035354188 scopus 로고    scopus 로고
    • Protein kinase C-α and protein kinase C-δ play opposite roles in the proliferation and apoptosis of glioma cells
    • MANDIL R, ASHKENAZI E, BLASS M et al.: Protein kinase C-α and protein kinase C-δ play opposite roles in the proliferation and apoptosis of glioma cells. Cancer Res. (2001) 61(11):4612-4619.
    • (2001) Cancer Res , vol.61 , Issue.11 , pp. 4612-4619
    • MANDIL, R.1    ASHKENAZI, E.2    BLASS, M.3
  • 64
    • 0034045930 scopus 로고    scopus 로고
    • Involvement of p21(Waf1/Cip1) in protein kinase C-α-induced cell cycle progression
    • BESSON A, YONG VW: Involvement of p21(Waf1/Cip1) in protein kinase C-α-induced cell cycle progression. Mol. Cell. Biol. (2000) 20(13):4580-4590.
    • (2000) Mol. Cell. Biol , vol.20 , Issue.13 , pp. 4580-4590
    • BESSON, A.1    YONG, V.W.2
  • 65
    • 0027180238 scopus 로고
    • Protein kinase C isotypes in human erythroleukemia (K562) cell proliferation and differentiation. Evidence that βII protein kinase C is required for proliferation
    • MURRAY NR, BAUMGARDNER GP, BURNS DJ, FIELDS AP: Protein kinase C isotypes in human erythroleukemia (K562) cell proliferation and differentiation. Evidence that βII protein kinase C is required for proliferation. J. Biol. Chem. (1993) 268(21):15847-15853.
    • (1993) J. Biol. Chem , vol.268 , Issue.21 , pp. 15847-15853
    • MURRAY, N.R.1    BAUMGARDNER, G.P.2    BURNS, D.J.3    FIELDS, A.P.4
  • 66
    • 31544447786 scopus 로고    scopus 로고
    • Subversion of protein kinase C-α signaling in hematopoietic progenitor cells results in the generation of a B-cell chronic lymphocytic leukemia-like population in vivo
    • NAKAGAWA R, SOH JW, MICHIE AM: Subversion of protein kinase C-α signaling in hematopoietic progenitor cells results in the generation of a B-cell chronic lymphocytic leukemia-like population in vivo. Cancer Res. (2006) 66(1):527-534.
    • (2006) Cancer Res , vol.66 , Issue.1 , pp. 527-534
    • NAKAGAWA, R.1    SOH, J.W.2    MICHIE, A.M.3
  • 67
    • 0026595961 scopus 로고
    • Crosslinking of the T cell-specific accessory molecules CD7 and CD28 modulates T cell adhesion
    • SHIMIZU Y, VAN SEVENTER GA, ENNIS E et al.: Crosslinking of the T cell-specific accessory molecules CD7 and CD28 modulates T cell adhesion. J. Exp. Med. (1992) 175(2):577-582.
    • (1992) J. Exp. Med , vol.175 , Issue.2 , pp. 577-582
    • SHIMIZU, Y.1    VAN SEVENTER, G.A.2    ENNIS, E.3
  • 68
    • 0028176083 scopus 로고
    • Tyrosine phosphorylation of pp125FAK in platelets requires coordinated signaling through integrin and agonist receptors
    • SHATTIL SJ, HAIMOVICH B, CUNNINGHAM M et al.: Tyrosine phosphorylation of pp125FAK in platelets requires coordinated signaling through integrin and agonist receptors. J. Biol. Chem. (1994) 269(20):14738-14745.
    • (1994) J. Biol. Chem , vol.269 , Issue.20 , pp. 14738-14745
    • SHATTIL, S.J.1    HAIMOVICH, B.2    CUNNINGHAM, M.3
  • 69
    • 0033565261 scopus 로고    scopus 로고
    • NG T. SHIMA D, SQUIRE A et al.: PKC-α regulates β1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J. (1999) 18(14):3909-3923.
    • NG T. SHIMA D, SQUIRE A et al.: PKC-α regulates β1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J. (1999) 18(14):3909-3923.
  • 70
    • 17944372904 scopus 로고    scopus 로고
    • Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility
    • NG T, PARSONS M, HUGHES WE et al.: Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility. EMBO J. (2001) 20(11):2723-2741.
    • (2001) EMBO J , vol.20 , Issue.11 , pp. 2723-2741
    • NG, T.1    PARSONS, M.2    HUGHES, W.E.3
  • 71
    • 18444412912 scopus 로고    scopus 로고
    • Site-directed perturbation of protein kinase C-integrin interaction blocks carcinoma cell chemotaxis
    • PARSONS M, KEPPLER MD, KLINE A et al.: Site-directed perturbation of protein kinase C-integrin interaction blocks carcinoma cell chemotaxis. Mol. Cell. Biol. (2002) 22(16):5897-5911.
    • (2002) Mol. Cell. Biol , vol.22 , Issue.16 , pp. 5897-5911
    • PARSONS, M.1    KEPPLER, M.D.2    KLINE, A.3
  • 72
    • 33744936606 scopus 로고    scopus 로고
    • Upregulation and activation of PKC-α by ErbB2 through Src promotes breast cancer cell invasion that can be blocked by combined treatment with PKC-α and Src inhibitors
    • TAN M, LI P, SUN M, YIN G, YU D: Upregulation and activation of PKC-α by ErbB2 through Src promotes breast cancer cell invasion that can be blocked by combined treatment with PKC-α and Src inhibitors. Oncogene (2006) 25(23):3286-3295.
    • (2006) Oncogene , vol.25 , Issue.23 , pp. 3286-3295
    • TAN, M.1    LI, P.2    SUN, M.3    YIN, G.4    YU, D.5
  • 73
    • 0035880256 scopus 로고    scopus 로고
    • Vascular endothelial growth factor triggers signaling cascades mediating multiple myeloma cell growth and migration
    • PODAR K, TAI YT, DAVIES FE et al.: Vascular endothelial growth factor triggers signaling cascades mediating multiple myeloma cell growth and migration. Blood (2001) 98(2):428-435.
    • (2001) Blood , vol.98 , Issue.2 , pp. 428-435
    • PODAR, K.1    TAI, Y.T.2    DAVIES, F.E.3
  • 74
    • 0036344276 scopus 로고    scopus 로고
    • PKC-β controls IκB kinase lipid raft recruitment and activation in response to BCR signaling
    • SU TT, GUO B, KAWAKAMI Y et al.: PKC-β controls IκB kinase lipid raft recruitment and activation in response to BCR signaling. Nat. Immunol. (2002) 3(8):780-786.
    • (2002) Nat. Immunol , vol.3 , Issue.8 , pp. 780-786
    • SU, T.T.1    GUO, B.2    KAWAKAMI, Y.3
  • 75
    • 0037124307 scopus 로고    scopus 로고
    • Protein kinase C-β controls NF-κB activation in B cells through selective regulation of the IκB kinase α
    • SAIJO K, MECKLENBRAUKER I, SANTANA A et al.: Protein kinase C-β controls NF-κB activation in B cells through selective regulation of the IκB kinase α. J. Exp. Med. (2002) 195(12):1647-1652.
    • (2002) J. Exp. Med , vol.195 , Issue.12 , pp. 1647-1652
    • SAIJO, K.1    MECKLENBRAUKER, I.2    SANTANA, A.3
  • 76
    • 27944503997 scopus 로고    scopus 로고
    • PKC-β regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1
    • SHINOHARA H, YASUDA T, AIBA Y et al.: PKC-β regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1. J. Exp. Med. (2005) 202(10):1423-1431.
    • (2005) J. Exp. Med , vol.202 , Issue.10 , pp. 1423-1431
    • SHINOHARA, H.1    YASUDA, T.2    AIBA, Y.3
  • 77
    • 0024284828 scopus 로고
    • Overproduction of protein kinase C causes disordered growth control in rat fibroblasts
    • HOUSEY GM, JOHNSON MD, HSIAO WL et al.: Overproduction of protein kinase C causes disordered growth control in rat fibroblasts. Cell (1988) 52(3):343-354.
    • (1988) Cell , vol.52 , Issue.3 , pp. 343-354
    • HOUSEY, G.M.1    JOHNSON, M.D.2    HSIAO, W.L.3
  • 78
    • 0025167963 scopus 로고
    • Overexpression of protein kinase C in HT29 colon cancer cells causes growth inhibition and tumor suppression
    • CHOI PM, TCHOU-WONG KM, WEINSTEIN IB: Overexpression of protein kinase C in HT29 colon cancer cells causes growth inhibition and tumor suppression. Mol. Cell. Biol. (1990) 10(9):4650-4657.
    • (1990) Mol. Cell. Biol , vol.10 , Issue.9 , pp. 4650-4657
    • CHOI, P.M.1    TCHOU-WONG, K.M.2    WEINSTEIN, I.B.3
  • 79
    • 0028015667 scopus 로고
    • Specific role for protein kinase C-β in cell differentiation
    • GAMARD CJ, BLOBE GC, HANNUN YA, OBEID LM: Specific role for protein kinase C-β in cell differentiation. Cell Growth Differ. (1994) 5(4):405-409.
    • (1994) Cell Growth Differ , vol.5 , Issue.4 , pp. 405-409
    • GAMARD, C.J.1    BLOBE, G.C.2    HANNUN, Y.A.3    OBEID, L.M.4
  • 80
    • 2642709170 scopus 로고    scopus 로고
    • Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth
    • XIA P, AIELLO LP, ISHII H et al.: Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth. J. Clin. Invest. (1996) 98(9):2018-2026.
    • (1996) J. Clin. Invest , vol.98 , Issue.9 , pp. 2018-2026
    • XIA, P.1    AIELLO, L.P.2    ISHII, H.3
  • 81
    • 0033118228 scopus 로고    scopus 로고
    • VEGF activates protein kinase C-dependent, but Ras-independent Raf-MEK-MAP kinase pathway for DNA synthesis in primary endothelial cells
    • TAKAHASHI T, UENO H, SHIBUYA M: VEGF activates protein kinase C-dependent, but Ras-independent Raf-MEK-MAP kinase pathway for DNA synthesis in primary endothelial cells. Oncogene (1999) 18(13):2221-2230.
    • (1999) Oncogene , vol.18 , Issue.13 , pp. 2221-2230
    • TAKAHASHI, T.1    UENO, H.2    SHIBUYA, M.3
  • 82
    • 0033199874 scopus 로고    scopus 로고
    • Protein kinase C lies on the signaling pathway for vascular endothelial growth factor-mediated tumor development and angiogenesis
    • YOSHIJI H, KURIYAMA S, WAYS DK et al.: Protein kinase C lies on the signaling pathway for vascular endothelial growth factor-mediated tumor development and angiogenesis. Cancer Res. (1999) 59(17):4413-4418.
    • (1999) Cancer Res , vol.59 , Issue.17 , pp. 4413-4418
    • YOSHIJI, H.1    KURIYAMA, S.2    WAYS, D.K.3
  • 83
    • 0037154156 scopus 로고    scopus 로고
    • Characterization of protein kinase C-β isoform's action on retinoblastoma protein phosphorylation, vascular endothelial growth factor-induced endothelial cell proliferation, and retinal neovascularization
    • SUZUMA K, TAKAHARA N, SUZUMA I et al.: Characterization of protein kinase C-β isoform's action on retinoblastoma protein phosphorylation, vascular endothelial growth factor-induced endothelial cell proliferation, and retinal neovascularization. Proc. Natl. Acad. Sci. USA (2002) 99(2):721-726.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.2 , pp. 721-726
    • SUZUMA, K.1    TAKAHARA, N.2    SUZUMA, I.3
  • 84
    • 25844484590 scopus 로고    scopus 로고
    • Protein kinase C-dependent protein kinase D activation modulates ERK signal pathway and endothelial cell proliferation by vascular endothelial growth factor
    • WONG C, JIN ZG: Protein kinase C-dependent protein kinase D activation modulates ERK signal pathway and endothelial cell proliferation by vascular endothelial growth factor. J. Biol. Chem. (2005) 280(39):33262-33269.
    • (2005) J. Biol. Chem , vol.280 , Issue.39 , pp. 33262-33269
    • WONG, C.1    JIN, Z.G.2
  • 85
    • 33748990105 scopus 로고    scopus 로고
    • Protein kinase C and downstream signaling pathways in a three-dimensional model of phorbol ester-induced angiogenesis
    • TAYLOR CJ, MOTAMED K, LILLY B: Protein kinase C and downstream signaling pathways in a three-dimensional model of phorbol ester-induced angiogenesis. Angiogenesis (2006) 9(2):39-51.
    • (2006) Angiogenesis , vol.9 , Issue.2 , pp. 39-51
    • TAYLOR, C.J.1    MOTAMED, K.2    LILLY, B.3
  • 86
    • 33745200542 scopus 로고    scopus 로고
    • Protein kinase C-β as a therapeutic target in breast cancer
    • SLEDGE GW Jr, GOKMEN-POLAR Y: Protein kinase C-β as a therapeutic target in breast cancer. Semin. Oncol. (2006) 33(3 Suppl. 9):S15-S18.
    • (2006) Semin. Oncol , vol.33 , Issue.3 SUPPL. 9
    • SLEDGE Jr, G.W.1    GOKMEN-POLAR, Y.2
  • 87
    • 0034888620 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor effects of a protein kinase C-α inhibitor in human hepatocellular and gastric cancer xenografts
    • TEICHER BA, MENON K, ALVAREZ E et al.: Antiangiogenic and antitumor effects of a protein kinase C-α inhibitor in human hepatocellular and gastric cancer xenografts. In Vivo (Athens, Greece) (2001) 15(3):185-193.
    • (2001) In Vivo (Athens, Greece) , vol.15 , Issue.3 , pp. 185-193
    • TEICHER, B.A.1    MENON, K.2    ALVAREZ, E.3
  • 88
    • 34249746834 scopus 로고    scopus 로고
    • Protein kinase C inhibitor enzastaurin induces in vitro and in vivo antitumor activity in Waldenstrom's macroglobulinemia
    • MOREAU AS, JIA X, NGO HT et al.: Protein kinase C inhibitor enzastaurin induces in vitro and in vivo antitumor activity in Waldenstrom's macroglobulinemia. Blood (2007).
    • (2007) Blood
    • MOREAU, A.S.1    JIA, X.2    NGO, H.T.3
  • 89
    • 1842454982 scopus 로고    scopus 로고
    • The enigmatic protein kinase C-δ: Complex roles in cell proliferation and survival
    • JACKSON DN, FOSTER DA: The enigmatic protein kinase C-δ: complex roles in cell proliferation and survival. FASEB J. (2004) 18(6):627-636.
    • (2004) FASEB J , vol.18 , Issue.6 , pp. 627-636
    • JACKSON, D.N.1    FOSTER, D.A.2
  • 90
    • 13344259987 scopus 로고
    • Proteolytic activation of protein kinase C-δ by an ICE-like protease in apoptotic cells
    • EMOTO Y, MANOME Y, MEINHARDT G et al.: Proteolytic activation of protein kinase C-δ by an ICE-like protease in apoptotic cells. EMBO J. (1995) 14(24):6148-6156.
    • (1995) EMBO J , vol.14 , Issue.24 , pp. 6148-6156
    • EMOTO, Y.1    MANOME, Y.2    MEINHARDT, G.3
  • 91
    • 12644268232 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase C-δ by an ICE/CED 3-like protease induces characteristics of apoptosis
    • GHAYUR T, HUGUNIN M, TALANIAN RV et al.: Proteolytic activation of protein kinase C-δ by an ICE/CED 3-like protease induces characteristics of apoptosis. J. Exp. Med. (1996) 184(6):2399-2404.
    • (1996) J. Exp. Med , vol.184 , Issue.6 , pp. 2399-2404
    • GHAYUR, T.1    HUGUNIN, M.2    TALANIAN, R.V.3
  • 92
    • 0031795922 scopus 로고    scopus 로고
    • Inactivation of DNA-dependent protein kinase by protein kinase C-δ: Implications for apoptosis
    • BHARTI A, KRAEFT SK, GOUNDER M et al.: Inactivation of DNA-dependent protein kinase by protein kinase C-δ: implications for apoptosis. Mol. Cell. Biol. (1998) 18(11):6719-6728.
    • (1998) Mol. Cell. Biol , vol.18 , Issue.11 , pp. 6719-6728
    • BHARTI, A.1    KRAEFT, S.K.2    GOUNDER, M.3
  • 93
    • 0032473917 scopus 로고    scopus 로고
    • Activation of protein kinase C-δ by the c-Abl tyrosine kinase in response to ionizing radiation
    • YUAN ZM, UTSUGISAWA T, ISHIKO T et al.: Activation of protein kinase C-δ by the c-Abl tyrosine kinase in response to ionizing radiation. Oncogene (1998) 16(13):1643-1648.
    • (1998) Oncogene , vol.16 , Issue.13 , pp. 1643-1648
    • YUAN, Z.M.1    UTSUGISAWA, T.2    ISHIKO, T.3
  • 94
    • 0034604023 scopus 로고    scopus 로고
    • PKC-δ is an apoptotic lamin kinase
    • CROSS T, GRIFFITHS G, DEACON E et al.: PKC-δ is an apoptotic lamin kinase. Oncogene (2000) 19(19):2331-2337.
    • (2000) Oncogene , vol.19 , Issue.19 , pp. 2331-2337
    • CROSS, T.1    GRIFFITHS, G.2    DEACON, E.3
  • 95
    • 0034725570 scopus 로고    scopus 로고
    • Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase C-δ
    • FRASCH SC, HENSON PM, KAILEY JM et al.: Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase C-δ. J. Biol. Chem. (2000) 275(30):23065-23073.
    • (2000) J. Biol. Chem , vol.275 , Issue.30 , pp. 23065-23073
    • FRASCH, S.C.1    HENSON, P.M.2    KAILEY, J.M.3
  • 96
    • 0030023982 scopus 로고    scopus 로고
    • Activation of protein kinase C-δ in human myeloid leukemia cells treated with 1-β-D-arabinofuranosylcytosine
    • EMOTO Y, KISAKI H, MANOME Y, KHARBANDA S, KUFE D: Activation of protein kinase C-δ in human myeloid leukemia cells treated with 1-β-D-arabinofuranosylcytosine. Blood (1996) 87(5):1990-1996.
    • (1996) Blood , vol.87 , Issue.5 , pp. 1990-1996
    • EMOTO, Y.1    KISAKI, H.2    MANOME, Y.3    KHARBANDA, S.4    KUFE, D.5
  • 97
    • 0032491318 scopus 로고    scopus 로고
    • Protein kinase C-δ 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 C-δ is activated by caspase-dependent proteolysis during ultraviolet radiation-induced apoptosis of human keratinocytes. J. Biol. Chem. (1998) 273(45):29995-30002.
    • (1998) J. Biol. Chem , vol.273 , Issue.45 , pp. 29995-30002
    • DENNING, M.F.1    WANG, Y.2    NICKOLOFF, B.J.3    WRONE-SMITH, T.4
  • 98
    • 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(27):19115-19123.
    • (1999) J. Biol. Chem , vol.274 , Issue.27 , pp. 19115-19123
    • REYLAND, M.E.1    ANDERSON, S.M.2    MATASSA, A.A.3    BARZEN, K.A.4    QUISSELL, D.O.5
  • 99
    • 24644517020 scopus 로고    scopus 로고
    • Involvement of proteolytic activation of PKCδ in cisplatin-induced apoptosis in human small cell lung cancer H69 cells
    • PERSAUD SD, HOANG V, HUANG J, BASU A: Involvement of proteolytic activation of PKCδ in cisplatin-induced apoptosis in human small cell lung cancer H69 cells. Int. J. Oncol. (2005) 27(1):149-154.
    • (2005) Int. J. Oncol , vol.27 , Issue.1 , pp. 149-154
    • PERSAUD, S.D.1    HOANG, V.2    HUANG, J.3    BASU, A.4
  • 100
    • 33646901676 scopus 로고    scopus 로고
    • Suppression of apoptosis in the protein kinase C-δ null mouse in vivo
    • HUMPHRIES MJ, LIMESAND KH, SCHNEIDER JC et al.: Suppression of apoptosis in the protein kinase C-δ null mouse in vivo. J. Biol. Chem. (2006) 281(14):9728-9737.
    • (2006) J. Biol. Chem , vol.281 , Issue.14 , pp. 9728-9737
    • HUMPHRIES, M.J.1    LIMESAND, K.H.2    SCHNEIDER, J.C.3
  • 101
    • 26644461205 scopus 로고    scopus 로고
    • Phorbol ester-induced G1 phase arrest selectively mediated by protein kinase C-δ-dependent induction of p21
    • NAKAGAWA M, OLIVA JL, KOTHAPALLI D et al.: Phorbol ester-induced G1 phase arrest selectively mediated by protein kinase C-δ-dependent induction of p21. J. Biol. Chem. (2005) 280(40):33926-33934.
    • (2005) J. Biol. Chem , vol.280 , Issue.40 , pp. 33926-33934
    • NAKAGAWA, M.1    OLIVA, J.L.2    KOTHAPALLI, D.3
  • 102
    • 0033597645 scopus 로고    scopus 로고
    • Protein kinase C-δ inhibition of S-phase transition in capillary endothelial cells involves the cyclin-dependent kinase inhibitor p27(Kip1)
    • ASHTON AW, WATANABE G, ALBANESE C et al.: Protein kinase C-δ inhibition of S-phase transition in capillary endothelial cells involves the cyclin-dependent kinase inhibitor p27(Kip1). J. Biol. Chem. (1999) 274(30):20805-20811.
    • (1999) J. Biol. Chem , vol.274 , Issue.30 , pp. 20805-20811
    • ASHTON, A.W.1    WATANABE, G.2    ALBANESE, C.3
  • 103
    • 0030973402 scopus 로고    scopus 로고
    • Protein kinase C-δ inhibits the proliferation of vascular smooth muscle cells by suppressing G1 cyclin expression
    • FUKUMOTO S, NISHIZAWA Y, HOSOI M et al.: Protein kinase C-δ inhibits the proliferation of vascular smooth muscle cells by suppressing G1 cyclin expression. J. Biol. Chem. (1997) 272(21):13816-13822.
    • (1997) J. Biol. Chem , vol.272 , Issue.21 , pp. 13816-13822
    • FUKUMOTO, S.1    NISHIZAWA, Y.2    HOSOI, M.3
  • 104
    • 0027418816 scopus 로고
    • Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity
    • MISCHAK H, GOODNIGHT JA, KOLCH W et al.: Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J. Biol. Chem. (1993) 268(9):6090-6096.
    • (1993) J. Biol. Chem , vol.268 , Issue.9 , pp. 6090-6096
    • MISCHAK, H.1    GOODNIGHT, J.A.2    KOLCH, W.3
  • 105
    • 0032565768 scopus 로고    scopus 로고
    • Protein kinase C-ε is oncogenic in colon epithelial cells by interaction with the ras signal transduction pathway
    • PERLETTI GP, CONCARI P, BRUSAFERRI S et al.: Protein kinase C-ε is oncogenic in colon epithelial cells by interaction with the ras signal transduction pathway. Oncogene (1998) 16(25):3345-3348.
    • (1998) Oncogene , vol.16 , Issue.25 , pp. 3345-3348
    • PERLETTI, G.P.1    CONCARI, P.2    BRUSAFERRI, S.3
  • 106
    • 0033521742 scopus 로고    scopus 로고
    • PKC-δ acts as a growth and tumor suppressor in rat colonic epithelial cells
    • PERLETTI GP, MARRAS E, CONCARI P, PICCININI F, TASHJIAN AH Jr: PKC-δ acts as a growth and tumor suppressor in rat colonic epithelial cells. Oncogene (1999) 18(5):1251-1256.
    • (1999) Oncogene , vol.18 , Issue.5 , pp. 1251-1256
    • PERLETTI, G.P.1    MARRAS, E.2    CONCARI, P.3    PICCININI, F.4    TASHJIAN Jr, A.H.5
  • 107
    • 0030735367 scopus 로고    scopus 로고
    • The von Hippel-Lindau gene product inhibits vascular permeability factor/vascular endothelial growth Factor expression in renal cell carcinoma by blocking protein kinase C pathways
    • PAL S, CLAFFEY KP, DVORAK HF, MUKHOPADHYAY D: The von Hippel-Lindau gene product inhibits vascular permeability factor/vascular endothelial growth Factor expression in renal cell carcinoma by blocking protein kinase C pathways. J. Biol. Chem. (1997) 272(44):27509-27512.
    • (1997) J. Biol. Chem , vol.272 , Issue.44 , pp. 27509-27512
    • PAL, S.1    CLAFFEY, K.P.2    DVORAK, H.F.3    MUKHOPADHYAY, D.4
  • 108
    • 0034617086 scopus 로고    scopus 로고
    • Inhibition of insulin-like growth factor-I-mediated cell signaling by the von Hippel-Lindau gene product in renal cancer
    • DATTA K, NAMBUDRIPAD R, PAL S et al.: Inhibition of insulin-like growth factor-I-mediated cell signaling by the von Hippel-Lindau gene product in renal cancer. J. Biol. Chem. (2000) 275(27):20700-20706.
    • (2000) J. Biol. Chem , vol.275 , Issue.27 , pp. 20700-20706
    • DATTA, K.1    NAMBUDRIPAD, R.2    PAL, S.3
  • 109
    • 0033581954 scopus 로고    scopus 로고
    • Increased protein kinase C-δ in mammary tumor cells: Relationship to transformation and metastatic progression
    • KILEY SC, CLARK KJ, DUDDY SK, WELCH DR, JAKEN S: Increased protein kinase C-δ in mammary tumor cells: relationship to transformation and metastatic progression. Oncogene (1999) 18(48):6748-6757.
    • (1999) Oncogene , vol.18 , Issue.48 , pp. 6748-6757
    • KILEY, S.C.1    CLARK, K.J.2    DUDDY, S.K.3    WELCH, D.R.4    JAKEN, S.5
  • 110
    • 0033168515 scopus 로고    scopus 로고
    • Protein kinase C-δ involvement in mammary tumor cell metastasis
    • KILEY SC, CLARK KJ, GOODNOUGH M, WELCH DR, JAKEN S: Protein kinase C-δ involvement in mammary tumor cell metastasis. Cancer Res. (1999) 59(13):3230-3238.
    • (1999) Cancer Res , vol.59 , Issue.13 , pp. 3230-3238
    • KILEY, S.C.1    CLARK, K.J.2    GOODNOUGH, M.3    WELCH, D.R.4    JAKEN, S.5
  • 111
    • 0034668779 scopus 로고    scopus 로고
    • Divergence in the anti-apoptotic signalling pathways used by nerve growth factor and basic fibroblast growth Factor (bFGF) in PC12 cells: Rescue by bFGF involves protein kinase C-δ
    • WERT MM, PALFREY HC: Divergence in the anti-apoptotic signalling pathways used by nerve growth factor and basic fibroblast growth Factor (bFGF) in PC12 cells: rescue by bFGF involves protein kinase C-δ. Biochem. J. (2000) 352(Part 1):175-182.
    • (2000) Biochem. J , vol.352 , Issue.PART 1 , pp. 175-182
    • WERT, M.M.1    PALFREY, H.C.2
  • 112
    • 0037111661 scopus 로고    scopus 로고
    • Constitutively activated phosphatidylinositol-3 kinase (PI-3K) is involved in the defect of apoptosis in B-CLL: Association with protein kinase C-δ
    • RINGSHAUSEN I, SCHNELLER F, BOGNER C et al.: Constitutively activated phosphatidylinositol-3 kinase (PI-3K) is involved in the defect of apoptosis in B-CLL: association with protein kinase C-δ. Blood (2002) 100(10):3741-3748.
    • (2002) Blood , vol.100 , Issue.10 , pp. 3741-3748
    • RINGSHAUSEN, I.1    SCHNELLER, F.2    BOGNER, C.3
  • 113
    • 0037443030 scopus 로고    scopus 로고
    • Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKC-δ promotes cellular survival and chemotherapeutic resistance
    • CLARK AS, WEST KA, BLUMBERG PM, DENNIS PA: Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKC-δ promotes cellular survival and chemotherapeutic resistance. Cancer Res. (2003) 63(4):780-786.
    • (2003) Cancer Res , vol.63 , Issue.4 , pp. 780-786
    • CLARK, A.S.1    WEST, K.A.2    BLUMBERG, P.M.3    DENNIS, P.A.4
  • 114
    • 18844427567 scopus 로고    scopus 로고
    • Upregulation of PKC-δ contributes to antiestrogen resistance in mammary tumor cells
    • NABHA SM, GLAROS S, HONG M et al.: Upregulation of PKC-δ contributes to antiestrogen resistance in mammary tumor cells. Oncogene (2005) 24(19):3166-3176.
    • (2005) Oncogene , vol.24 , Issue.19 , pp. 3166-3176
    • NABHA, S.M.1    GLAROS, S.2    HONG, M.3
  • 115
    • 24944563309 scopus 로고    scopus 로고
    • Protein kinase C-ε is a predictive biomarker of aggressive breast cancer and a validated target for RNA interference anticancer therapy
    • PAN Q, BAO LW, KLEER CG et al.: Protein kinase C-ε is a predictive biomarker of aggressive breast cancer and a validated target for RNA interference anticancer therapy. Cancer Res. (2005) 65(18):8366-8371.
    • (2005) Cancer Res , vol.65 , Issue.18 , pp. 8366-8371
    • PAN, Q.1    BAO, L.W.2    KLEER, C.G.3
  • 116
    • 0029086492 scopus 로고
    • Comparison of protein kinase C activity and isoform expression in cisplatin-sensitive and -resistant ovarian carcinoma cells
    • BASU A, WEIXEL KM: Comparison of protein kinase C activity and isoform expression in cisplatin-sensitive and -resistant ovarian carcinoma cells. Int. J. Cancer (1995) 62(4):457-460.
    • (1995) Int. J. Cancer , vol.62 , Issue.4 , pp. 457-460
    • BASU, A.1    WEIXEL, K.M.2
  • 117
    • 0037144492 scopus 로고    scopus 로고
    • Protein kinase C-ε promotes survival of lung cancer cells by suppressing apoptosis through dysregulation of the mitochondrial caspase pathway
    • DING L, WANG H, LANG W. XIAO L: Protein kinase C-ε promotes survival of lung cancer cells by suppressing apoptosis through dysregulation of the mitochondrial caspase pathway. J. Biol. Chem. (2002) 277(38):35305-35313.
    • (2002) J. Biol. Chem , vol.277 , Issue.38 , pp. 35305-35313
    • DING, L.1    WANG, H.2    LANG, W.X.L.3
  • 118
    • 23844474726 scopus 로고    scopus 로고
    • Protein kinase C-ε regulates the apoptosis and survival of glioma cells
    • OKHRIMENKO H, LU W, XIANG C et al.: Protein kinase C-ε regulates the apoptosis and survival of glioma cells. Cancer Res. (2005) 65(16):7301-7309.
    • (2005) Cancer Res , vol.65 , Issue.16 , pp. 7301-7309
    • OKHRIMENKO, H.1    LU, W.2    XIANG, C.3
  • 119
    • 33747356750 scopus 로고    scopus 로고
    • Protein kinase C-ε activates protein kinase B/ Akt via DNA-PK to protect against TNF-α-induced cell death
    • LU D, HUANG J, BASU A: Protein kinase C-ε activates protein kinase B/ Akt via DNA-PK to protect against TNF-α-induced cell death. J. Biol. Chem (2006) 281(32):22799-22807.
    • (2006) J. Biol. Chem , vol.281 , Issue.32 , pp. 22799-22807
    • LU, D.1    HUANG, J.2    BASU, A.3
  • 120
    • 0027182090 scopus 로고
    • The ε isoform of protein kinase C is an oncogene when overexpressed in rat fibroblasts
    • CACACE AM, GUADAGNO SN, KRAUSS RS, FABBRO D, WEINSTEIN IB: The ε isoform of protein kinase C is an oncogene when overexpressed in rat fibroblasts. Oncogene (1993) 8(8):2095-2104.
    • (1993) Oncogene , vol.8 , Issue.8 , pp. 2095-2104
    • CACACE, A.M.1    GUADAGNO, S.N.2    KRAUSS, R.S.3    FABBRO, D.4    WEINSTEIN, I.B.5
  • 121
    • 0025912599 scopus 로고
    • Failure of wild-type or a mutant form of protein kinase C-α to transform fibroblasts
    • BORNER C, FILIPUZZI I, WEINSTEIN IB, IMBER R: Failure of wild-type or a mutant form of protein kinase C-α to transform fibroblasts. Nature (1991) 353(6339):78-80.
    • (1991) Nature , vol.353 , Issue.6339 , pp. 78-80
    • BORNER, C.1    FILIPUZZI, I.2    WEINSTEIN, I.B.3    IMBER, R.4
  • 122
    • 0344874067 scopus 로고    scopus 로고
    • BRENNER W, FARBER G, HERGET T et al.: Protein kinase C-η is associated with progression of renal cell carcinoma (RCC) Anticancer Res. (2003) 23(5A):4001-4006
    • BRENNER W, FARBER G, HERGET T et al.: Protein kinase C-η is associated with progression of renal cell carcinoma (RCC) Anticancer Res. (2003) 23(5A):4001-4006
  • 123
    • 0031812872 scopus 로고    scopus 로고
    • BECK JF, BOHNET B, BRUGGER D et al.: Expression analysis of protein kinase C isozymes and multidrug resistance associated genes in ovarian cancer cells. Anticancer Res. (1998) 18(2A):701-705.
    • BECK JF, BOHNET B, BRUGGER D et al.: Expression analysis of protein kinase C isozymes and multidrug resistance associated genes in ovarian cancer cells. Anticancer Res. (1998) 18(2A):701-705.
  • 124
    • 3042538269 scopus 로고    scopus 로고
    • Protein kinase C-θ is highly expressed in gastrointestinal stromal tumors but not in other mesenchymal neoplasias
    • BLAY P, ASTUDILLO A, BUESA JM et al.: Protein kinase C-θ is highly expressed in gastrointestinal stromal tumors but not in other mesenchymal neoplasias. Clin. Cancer Res. (2004) 10(12 Part 1):4089-4095.
    • (2004) Clin. Cancer Res , vol.10 , Issue.12 PART 1 , pp. 4089-4095
    • BLAY, P.1    ASTUDILLO, A.2    BUESA, J.M.3
  • 125
    • 23844521568 scopus 로고    scopus 로고
    • The protein kinase C-β-selective inhibitor, enzastaurin (LY317615.HCl), suppresses signaling through the AKT pathway, induces apoptosis, and suppresses growth of human colon cancer and glioblastoma xenografts
    • GRAFF JR, MCNULTY AM, HANNA KR et al.: The protein kinase C-β-selective inhibitor, enzastaurin (LY317615.HCl), suppresses signaling through the AKT pathway, induces apoptosis, and suppresses growth of human colon cancer and glioblastoma xenografts. Cancer Res. (2005) 65(16):7462-7469.
    • (2005) Cancer Res , vol.65 , Issue.16 , pp. 7462-7469
    • GRAFF, J.R.1    MCNULTY, A.M.2    HANNA, K.R.3
  • 126
    • 33748670455 scopus 로고    scopus 로고
    • Phase I dose escalation and pharmacokinetic study of enzastaurin, an oral protein kinase C-β inhibitor, in patients with advanced cancer
    • CARDUCCI MA, MUSIB L, KIES MS et al.: Phase I dose escalation and pharmacokinetic study of enzastaurin, an oral protein kinase C-β inhibitor, in patients with advanced cancer. J. Clin. Oncol. (2006) 24(25):4092-4099.
    • (2006) J. Clin. Oncol , vol.24 , Issue.25 , pp. 4092-4099
    • CARDUCCI, M.A.1    MUSIB, L.2    KIES, M.S.3
  • 127
    • 0035657643 scopus 로고    scopus 로고
    • Protein kinase C inhibitors as novel anticancer drugs
    • GOEKJIAN PG, JIROUSEK MR, Protein kinase C inhibitors as novel anticancer drugs. Expert Opin. Investig. Drugs (2001) 10(12):2117-2140.
    • (2001) Expert Opin. Investig. Drugs , vol.10 , Issue.12 , pp. 2117-2140
    • GOEKJIAN, P.G.1    JIROUSEK, M.R.2
  • 128
    • 0036137647 scopus 로고    scopus 로고
    • Antiangiogenic effects of a protein kinase C-β-selective small molecule
    • TEICHER BA, ALVAREZ E, MENON K et al.: Antiangiogenic effects of a protein kinase C-β-selective small molecule. Cancer Chemother. Pharmacol. (2002) 49(1):69-77.
    • (2002) Cancer Chemother. Pharmacol , vol.49 , Issue.1 , pp. 69-77
    • TEICHER, B.A.1    ALVAREZ, E.2    MENON, K.3
  • 129
    • 0442329299 scopus 로고    scopus 로고
    • LY317615 decreases plasma VEGF levels in human tumor xenograft-bearing mice
    • KEYES KA, MANN L, SHERMAN M et al.: LY317615 decreases plasma VEGF levels in human tumor xenograft-bearing mice. Cancer Chemother. Pharmacol. (2004) 53(2):133-140.
    • (2004) Cancer Chemother. Pharmacol , vol.53 , Issue.2 , pp. 133-140
    • KEYES, K.A.1    MANN, L.2    SHERMAN, M.3
  • 130
    • 33745204140 scopus 로고    scopus 로고
    • Development and validation of a drug activity biomarker that shows target inhibition in cancer patients receiving enzastaurin, a novel protein kinase C-β inhibitor
    • GREEN LJ, MARDER P, RAY C et al.: Development and validation of a drug activity biomarker that shows target inhibition in cancer patients receiving enzastaurin, a novel protein kinase C-β inhibitor. Clin. Cancer Res. (2006) 12(11 Part 1):3408-3415.
    • (2006) Clin. Cancer Res , vol.12 , Issue.11 PART 1 , pp. 3408-3415
    • GREEN, L.J.1    MARDER, P.2    RAY, C.3
  • 131
    • 4243406643 scopus 로고    scopus 로고
    • Phase I study of LY317615, a protein kinase C-β inhibitor
    • HERBST RS, THORNTON DE, KIES MS: Phase I study of LY317615, a protein kinase C-β inhibitor. Proc. ASCO (2002) 21:A82.
    • (2002) Proc. ASCO , vol.21
    • HERBST, R.S.1    THORNTON, D.E.2    KIES, M.S.3
  • 132
    • 33646555670 scopus 로고    scopus 로고
    • Results from Phase II trial of enzastaurin LY317615, patients with recurrent high grade gliomas
    • FINE HA, KIM L, ROYCE C et al.: Results from Phase II trial of enzastaurin (LY317615) in patients with recurrent high grade gliomas. J. Clin. Oncol. (2005) 23(16S):1504.
    • (2005) J. Clin. Oncol , vol.23 , Issue.16 S , pp. 1504
    • FINE, H.A.1    KIM, L.2    ROYCE, C.3
  • 133
    • 34249075706 scopus 로고    scopus 로고
    • Phase II study of enzastaurin, a protein kinase C-β inhibitor, in patients with relapsed or refractory diffuse large B-cell lymphoma
    • ROBERTSON MJ, KAHL BS, VOSE JM et al.: Phase II study of enzastaurin, a protein kinase C-β inhibitor, in patients with relapsed or refractory diffuse large B-cell lymphoma. J. Clin. Oncol. (2007) 25(13):1741-1746.
    • (2007) J. Clin. Oncol , vol.25 , Issue.13 , pp. 1741-1746
    • ROBERTSON, M.J.1    KAHL, B.S.2    VOSE, J.M.3
  • 134
    • 33748328365 scopus 로고    scopus 로고
    • Enzastaurin (LY317615), a protein kinase C-β inhibitor, inhibits the AKT pathway and induces apoptosis in multiple myeloma cell lines
    • RIZVI MA, GHIAS K, DAVIES KM et al.: Enzastaurin (LY317615), a protein kinase C-β inhibitor, inhibits the AKT pathway and induces apoptosis in multiple myeloma cell lines. Mol. Cancer Ther. (2006) 5(7):1783-1789.
    • (2006) Mol. Cancer Ther , vol.5 , Issue.7 , pp. 1783-1789
    • RIZVI, M.A.1    GHIAS, K.2    DAVIES, K.M.3
  • 135
    • 0035064790 scopus 로고    scopus 로고
    • Mechanisms of resistance imatinib (ST1571) in preclinical models and in leukemia patients
    • WEISBERG E, GRIFFIN JD: Mechanisms of resistance imatinib (ST1571) in preclinical models and in leukemia patients. Drug Resist. Updat. (2001) 4(1):22-28.
    • (2001) Drug Resist. Updat , vol.4 , Issue.1 , pp. 22-28
    • WEISBERG, E.1    GRIFFIN, J.D.2
  • 136
    • 22144455380 scopus 로고    scopus 로고
    • Activation mutations of human c-KIT resistant to imatinib mesylate are sensitive to the tyrosine kinase inhibitor PKC412
    • GROWNEY JD, CLARK JJ, ADELSPERGER J et al.: Activation mutations of human c-KIT resistant to imatinib mesylate are sensitive to the tyrosine kinase inhibitor PKC412. Blood (2005) 106(2):721-724.
    • (2005) Blood , vol.106 , Issue.2 , pp. 721-724
    • GROWNEY, J.D.1    CLARK, J.J.2    ADELSPERGER, J.3
  • 137
    • 0036175273 scopus 로고    scopus 로고
    • Actions of the selective protein kinase C inhibitor PKC412 on B-chronic lymphocytic leukemia cells in vitro
    • GANESHAGURU K, WICKREMASINGHE RG, JONES DT et al.: Actions of the selective protein kinase C inhibitor PKC412 on B-chronic lymphocytic leukemia cells in vitro. Haematologica (2002) 87(2):167-176.
    • (2002) Haematologica , vol.87 , Issue.2 , pp. 167-176
    • GANESHAGURU, K.1    WICKREMASINGHE, R.G.2    JONES, D.T.3
  • 138
    • 0013312329 scopus 로고    scopus 로고
    • Inhibition of FLT3 in MLL. Validation of a therapeutic target identified by gene expression based classification
    • ARMSTRONG SA, KUNG AL, MABON ME et al.: Inhibition of FLT3 in MLL. Validation of a therapeutic target identified by gene expression based classification. Cancer cell (2003) 3(2):173-183.
    • (2003) Cancer cell , vol.3 , Issue.2 , pp. 173-183
    • ARMSTRONG, S.A.1    KUNG, A.L.2    MABON, M.E.3
  • 139
    • 0142119964 scopus 로고    scopus 로고
    • PKC412 overcomes resistance to imatinib in a murine model of FIP1L1-PDGFR-α-induced myeloproliferative disease
    • COOLS J, STOVER EH, BOULTON CI, et al.: PKC412 overcomes resistance to imatinib in a murine model of FIP1L1-PDGFR-α-induced myeloproliferative disease. Cancer cell (2003) 3(5):459-469.
    • (2003) Cancer cell , vol.3 , Issue.5 , pp. 459-469
    • COOLS, J.1    STOVER, E.H.2    BOULTON, C.I.3
  • 140
    • 31744438381 scopus 로고    scopus 로고
    • FGFR3 as a therapeutic target of the small molecule inhibitor PKC412 in hematopoietic malignancies
    • CHEN J, LEE BH, WILLIAMS IR et al.: FGFR3 as a therapeutic target of the small molecule inhibitor PKC412 in hematopoietic malignancies. Oncogene (2005) 24(56):8259-8267.
    • (2005) Oncogene , vol.24 , Issue.56 , pp. 8259-8267
    • CHEN, J.1    LEE, B.H.2    WILLIAMS, I.R.3
  • 141
    • 33947579975 scopus 로고    scopus 로고
    • Identification of MCL1 as a novel target in neoplastic mast cells in systemic mastocytosis: Inhibition of mast cell survival by MCL1 antisense oligonucleotides and synergism with PKC412
    • AICHBERGER KJ, MAYERHOFER M, GLEIXNER KV et al.: Identification of MCL1 as a novel target in neoplastic mast cells in systemic mastocytosis: inhibition of mast cell survival by MCL1 antisense oligonucleotides and synergism with PKC412. Blood (2007) 109(7):3031-3041.
    • (2007) Blood , vol.109 , Issue.7 , pp. 3031-3041
    • AICHBERGER, K.J.1    MAYERHOFER, M.2    GLEIXNER, K.V.3
  • 142
  • 143
    • 33746381245 scopus 로고    scopus 로고
    • Inhibitors of the PI3-kinase/ Akt pathway induce mitotic catastrophe in non-small cell lung cancer cells
    • HEMSTROM TH, SANDSTROM M, ZHIVOTOVSKY B: Inhibitors of the PI3-kinase/ Akt pathway induce mitotic catastrophe in non-small cell lung cancer cells. Int. J. Cancer (2006) 119(5):1028-1038.
    • (2006) Int. J. Cancer , vol.119 , Issue.5 , pp. 1028-1038
    • HEMSTROM, T.H.1    SANDSTROM, M.2    ZHIVOTOVSKY, B.3
  • 144
    • 33846899418 scopus 로고    scopus 로고
    • PKC412 demonstrates JNK-dependent activity against human multiple myeloma cells
    • SHARKEY J, KHONG T, SPENCER A: PKC412 demonstrates JNK-dependent activity against human multiple myeloma cells. Blood (2007) 109(4):1712-1719.
    • (2007) Blood , vol.109 , Issue.4 , pp. 1712-1719
    • SHARKEY, J.1    KHONG, T.2    SPENCER, A.3
  • 145
    • 33845601781 scopus 로고    scopus 로고
    • Effects of PKC412, nilotinib, and imatinib against GIST-associated PDGFRA mutants with differential imatinib sensitivity
    • WEISBERG E, WRIGHT RD, JIANG J et al.: Effects of PKC412, nilotinib, and imatinib against GIST-associated PDGFRA mutants with differential imatinib sensitivity. Gastroenterology (2006) 131(6):1734-1742.
    • (2006) Gastroenterology , vol.131 , Issue.6 , pp. 1734-1742
    • WEISBERG, E.1    WRIGHT, R.D.2    JIANG, J.3
  • 146
    • 21844455259 scopus 로고    scopus 로고
    • N-Benzoylstaurosporine (PKC412) inhibits Akt kinase inducing apoptosis in multiple myeloma cells
    • BAHLIS NJ, MIAO Y, KOC ON et al.: N-Benzoylstaurosporine (PKC412) inhibits Akt kinase inducing apoptosis in multiple myeloma cells. Leuk. Lymphoma (2005) 46(6):899-908.
    • (2005) Leuk. Lymphoma , vol.46 , Issue.6 , pp. 899-908
    • BAHLIS, N.J.1    MIAO, Y.2    KOC, O.N.3
  • 147
    • 0036667939 scopus 로고    scopus 로고
    • The clinical development of the bryostatins
    • CLAMP A, JAYSON GC: The clinical development of the bryostatins. Anticancer Drugs (2002) 13(7):673-683.
    • (2002) Anticancer Drugs , vol.13 , Issue.7 , pp. 673-683
    • CLAMP, A.1    JAYSON, G.C.2
  • 148
    • 0023253596 scopus 로고
    • Bryostatin 1, an activator of protein kinase C, inhibits tumor promotion by phorbol esters in SENCAR mouse skin
    • HENNINGS H, BLUMBERG PM, PETTIT GR et al.: Bryostatin 1, an activator of protein kinase C, inhibits tumor promotion by phorbol esters in SENCAR mouse skin. Carcinogenesis (1987) 8(9):1343-1346.
    • (1987) Carcinogenesis , vol.8 , Issue.9 , pp. 1343-1346
    • HENNINGS, H.1    BLUMBERG, P.M.2    PETTIT, G.R.3
  • 149
    • 0032721005 scopus 로고    scopus 로고
    • Pharmacology and clinical experience with bryostatin 1: A novel anticancer drug
    • PHILIP PA, ZONDER JA: Pharmacology and clinical experience with bryostatin 1: a novel anticancer drug. Expert Opin. Investig. Drugs (1999) 8(12):2189-2199.
    • (1999) Expert Opin. Investig. Drugs , vol.8 , Issue.12 , pp. 2189-2199
    • PHILIP, P.A.1    ZONDER, J.A.2
  • 150
    • 0022375243 scopus 로고
    • Bryostatins: Potent, new mitogens that mimic phorbol ester tumor promoters
    • SMITH JB, SMITH L, PETTIT GR: Bryostatins: potent, new mitogens that mimic phorbol ester tumor promoters. Biochem. Biophys. Res. Commun. (1985) 132(3):939-945.
    • (1985) Biochem. Biophys. Res. Commun , vol.132 , Issue.3 , pp. 939-945
    • SMITH, J.B.1    SMITH, L.2    PETTIT, G.R.3
  • 151
    • 0023749283 scopus 로고
    • Bryostatin 1 activates protein kinase C and induces monocytic differentiation of HL-60 cells
    • STONE RM, SARIBAN E, PETTIT GR, KUFE DW: Bryostatin 1 activates protein kinase C and induces monocytic differentiation of HL-60 cells. Blood (1988) 72(1):208-213.
    • (1988) Blood , vol.72 , Issue.1 , pp. 208-213
    • STONE, R.M.1    SARIBAN, E.2    PETTIT, G.R.3    KUFE, D.W.4
  • 152
    • 0024504383 scopus 로고
    • Varied differentiation responses of human leukemias to bryostatin 1
    • KRAFT AS, WILLIAM F, PETTIT GR, LILLY MB: Varied differentiation responses of human leukemias to bryostatin 1. Cancer Res. (1989) 49(5):1287-1293.
    • (1989) Cancer Res , vol.49 , Issue.5 , pp. 1287-1293
    • KRAFT, A.S.1    WILLIAM, F.2    PETTIT, G.R.3    LILLY, M.B.4
  • 153
    • 0024445695 scopus 로고
    • Bryostatin 1 induces differentiation of B-chronic lymphocytic leukemia cells
    • DREXLER HG, GIGNAC SM, JONES RA et al.: Bryostatin 1 induces differentiation of B-chronic lymphocytic leukemia cells. Blood (1989) 74(5):1747-1757.
    • (1989) Blood , vol.74 , Issue.5 , pp. 1747-1757
    • DREXLER, H.G.1    GIGNAC, S.M.2    JONES, R.A.3
  • 154
    • 0027474602 scopus 로고
    • Differential effects of bryostatin 1 on human non-Hodgkin's B-lymphoma cell lines
    • MOHAMMAD RM, AL-KATIB A, PETTIT GR, SENSENBRENNER LL: Differential effects of bryostatin 1 on human non-Hodgkin's B-lymphoma cell lines. Leuk. Res. (1993) 17(1):1-8.
    • (1993) Leuk. Res , vol.17 , Issue.1 , pp. 1-8
    • MOHAMMAD, R.M.1    AL-KATIB, A.2    PETTIT, G.R.3    SENSENBRENNER, L.L.4
  • 155
    • 0141889267 scopus 로고    scopus 로고
    • STATI mediates differentiation of chronic lymphocytic leukemia cells in response to bryostatin 1
    • BATTLE TE, FRANK DA: STATI mediates differentiation of chronic lymphocytic leukemia cells in response to bryostatin 1. Blood (2003) 102(8):3016-3024.
    • (2003) Blood , vol.102 , Issue.8 , pp. 3016-3024
    • BATTLE, T.E.1    FRANK, D.A.2
  • 156
    • 0034851019 scopus 로고    scopus 로고
    • Phase II study of bryostatin 1 in patients with relapsed multiple myeloma
    • VARTERASIAN ML, PEMBERTON PA, HULBURD K et al.: Phase II study of bryostatin 1 in patients with relapsed multiple myeloma. Investig. New Drugs (2001) 19(3):245-247.
    • (2001) Investig. New Drugs , vol.19 , Issue.3 , pp. 245-247
    • VARTERASIAN, M.L.1    PEMBERTON, P.A.2    HULBURD, K.3
  • 157
    • 0242298228 scopus 로고    scopus 로고
    • A Phase II trial of bryostatin-1 administered by weekly 24-h infusion in recurrent epithelial ovarian carcinoma
    • CLAMP AR, BLACKHALL FH, VASEY P et al.: A Phase II trial of bryostatin-1 administered by weekly 24-h infusion in recurrent epithelial ovarian carcinoma. Br. J. Cancer (2003) 89(7):1152-1154.
    • (2003) Br. J. Cancer , vol.89 , Issue.7 , pp. 1152-1154
    • CLAMP, A.R.1    BLACKHALL, F.H.2    VASEY, P.3
  • 158
    • 0028126624 scopus 로고
    • Bryostatin 1 protects protein kinase C-δ from down-regulation in mouse keratinocytes in parallel with its inhibition of phorbol ester-induced differentiation
    • SZALLASI Z, DENNING MF, SMITH CB et al.: Bryostatin 1 protects protein kinase C-δ from down-regulation in mouse keratinocytes in parallel with its inhibition of phorbol ester-induced differentiation. Mol. Pharmacol. (1994) 46(5):840-850.
    • (1994) Mol. Pharmacol , vol.46 , Issue.5 , pp. 840-850
    • SZALLASI, Z.1    DENNING, M.F.2    SMITH, C.B.3
  • 159
    • 0035992301 scopus 로고    scopus 로고
    • Phase I trial and correlative laboratory studies of bryostatin 1 (NSC 339555) and high-dose 1-B-D-arabinofuranosylcytosine in patients with refractory acute leukemia
    • CRAGG LH, ANDREEFF M, FELDMAN E et al.: Phase I trial and correlative laboratory studies of bryostatin 1 (NSC 339555) and high-dose 1-B-D-arabinofuranosylcytosine in patients with refractory acute leukemia. Clin. Cancer Res. (2002) 8(7):2123-2133.
    • (2002) Clin. Cancer Res , vol.8 , Issue.7 , pp. 2123-2133
    • CRAGG, L.H.1    ANDREEFF, M.2    FELDMAN, E.3
  • 160
    • 0029084804 scopus 로고
    • A Phase I trial of bryostatin 1 in patients with advanced malignancy using a 24 h intravenous infusion
    • JAYSON GC, CROWTHER D, PRENDIVILLE J et al.: A Phase I trial of bryostatin 1 in patients with advanced malignancy using a 24 h intravenous infusion. Br. J. Cancer (1995) 72(2):461-468.
    • (1995) Br. J. Cancer , vol.72 , Issue.2 , pp. 461-468
    • JAYSON, G.C.1    CROWTHER, D.2    PRENDIVILLE, J.3
  • 161
    • 0031982782 scopus 로고    scopus 로고
    • Phase I study of bryostatin 1 in patients with relapsed non-Hodgkin's lymphoma and chronic lymphocytic leukemia
    • VARTERASIAN ML, MOHAMMAD RM, EILENDER DS et al.: Phase I study of bryostatin 1 in patients with relapsed non-Hodgkin's lymphoma and chronic lymphocytic leukemia. J. Clin. Oncol. (1998) 16(1):56-62.
    • (1998) J. Clin. Oncol , vol.16 , Issue.1 , pp. 56-62
    • VARTERASIAN, M.L.1    MOHAMMAD, R.M.2    EILENDER, D.S.3
  • 162
    • 12944249449 scopus 로고    scopus 로고
    • Phase II trial of bryostatin 1 in patients with relapsed low-grade non-Hodgkin's lymphoma and chronic lymphocytic leukemia
    • VARTERASIAN ML, MOHAMMAD RM, SHURAFA MS et al.: Phase II trial of bryostatin 1 in patients with relapsed low-grade non-Hodgkin's lymphoma and chronic lymphocytic leukemia. Clin. Cancer Res. (2000) 6(3):825-828.
    • (2000) Clin. Cancer Res , vol.6 , Issue.3 , pp. 825-828
    • VARTERASIAN, M.L.1    MOHAMMAD, R.M.2    SHURAFA, M.S.3
  • 163
    • 0026481364 scopus 로고
    • Potentiation of the activity of 1-β-D-arabinofuranosylcytosine by the protein kinase C activator bryostatin 1 in HL-60 cells: Association with enhanced fragmentation of mature DNA
    • GRANT S, JARVIS WD, SWERDLOW PS et al.: Potentiation of the activity of 1-β-D-arabinofuranosylcytosine by the protein kinase C activator bryostatin 1 in HL-60 cells: association with enhanced fragmentation of mature DNA. Cancer Res. (1992) 52(22):6270-6278.
    • (1992) Cancer Res , vol.52 , Issue.22 , pp. 6270-6278
    • GRANT, S.1    JARVIS, W.D.2    SWERDLOW, P.S.3
  • 164
    • 0031965131 scopus 로고    scopus 로고
    • Bryostatin 1-tamoxifen combinations show synergistic effects on the inhibition of growth of P388 cells in vitro
    • MCGOWN AT, JAYSON G, PETTIT GR et al.: Bryostatin 1-tamoxifen combinations show synergistic effects on the inhibition of growth of P388 cells in vitro. Br. J. Cancer (1998) 77(2):216-220.
    • (1998) Br. J. Cancer , vol.77 , Issue.2 , pp. 216-220
    • MCGOWN, A.T.1    JAYSON, G.2    PETTIT, G.R.3
  • 165
    • 0032776390 scopus 로고    scopus 로고
    • Induction of apoptosis and differentiation by fludarabine in human leukemia cells (U937): Interactions with the macrocyclic lactone bryostatin 1
    • VRANA JA, WANG Z, RAO AS et al.: Induction of apoptosis and differentiation by fludarabine in human leukemia cells (U937): interactions with the macrocyclic lactone bryostatin 1. Leukemia (1999) 13(7):1046-1055.
    • (1999) Leukemia , vol.13 , Issue.7 , pp. 1046-1055
    • VRANA, J.A.1    WANG, Z.2    RAO, A.S.3
  • 166
    • 0032169905 scopus 로고    scopus 로고
    • Effect of bryostatin 1 on taxol-induced apoptosis and cytotoxicity in human leukemia cells (U937)
    • WANG S, GUO CY, CASTILLO A, DENT P, GRANT S: Effect of bryostatin 1 on taxol-induced apoptosis and cytotoxicity in human leukemia cells (U937). Biochem. Pharmacol. (1998) 56(5):635-644.
    • (1998) Biochem. Pharmacol , vol.56 , Issue.5 , pp. 635-644
    • WANG, S.1    GUO, C.Y.2    CASTILLO, A.3    DENT, P.4    GRANT, S.5
  • 167
    • 0037403698 scopus 로고    scopus 로고
    • Combination therapy with irinotecan and protein kinase C inhibitors in malignant glioma
    • CHEN TC, SU S, FRY D, LIEBES L: Combination therapy with irinotecan and protein kinase C inhibitors in malignant glioma. Cancer (2003) 97(9 Suppl.):2363-2373.
    • (2003) Cancer , vol.97 , Issue.9 SUPPL. , pp. 2363-2373
    • CHEN, T.C.1    SU, S.2    FRY, D.3    LIEBES, L.4
  • 168
    • 0033981511 scopus 로고    scopus 로고
    • Antitumor compounds from tunicates
    • RINEHART KL: Antitumor compounds from tunicates. Med. Res. Rev. (2000) 20(1):1-27.
    • (2000) Med. Res. Rev , vol.20 , Issue.1 , pp. 1-27
    • RINEHART, K.L.1
  • 169
    • 3042781436 scopus 로고    scopus 로고
    • Aplidin induces the mitochondrial apoptotic pathway via oxidative stress-mediated JNK and p38 activation and protein kinase C-δ
    • GARCIA-FERNANDEZ LF, LOSADA A, ALCAIDE V et al.: Aplidin induces the mitochondrial apoptotic pathway via oxidative stress-mediated JNK and p38 activation and protein kinase C-δ. Oncogene (2002) 21(49):7533-7544.
    • (2002) Oncogene , vol.21 , Issue.49 , pp. 7533-7544
    • GARCIA-FERNANDEZ, L.F.1    LOSADA, A.2    ALCAIDE, V.3
  • 170
    • 0022892593 scopus 로고
    • Inhibition of protein kinase C mediated signal transduction by camoxifen. Importance for antitumour activity
    • HORGAN K, COOKE E, HALLETT MB, MANSEL RE: Inhibition of protein kinase C mediated signal transduction by camoxifen. Importance for antitumour activity. Biochem. Pharmacol. (1986) 35(24):4463-4465.
    • (1986) Biochem. Pharmacol , vol.35 , Issue.24 , pp. 4463-4465
    • HORGAN, K.1    COOKE, E.2    HALLETT, M.B.3    MANSEL, R.E.4
  • 171
    • 0030006468 scopus 로고    scopus 로고
    • Tamoxifen modulates protein kinase C via oxidative stress in estrogen receptor-negative breast cancer cells
    • GUNDIMEDAU, CHEN ZH, GOPALAKRISHNA R: Tamoxifen modulates protein kinase C via oxidative stress in estrogen receptor-negative breast cancer cells. J. Biol. Chem. (1996) 271(23):13504-13514.
    • (1996) J. Biol. Chem , vol.271 , Issue.23 , pp. 13504-13514
    • GUNDIMEDAU, C.H.E.N.1    ZH, G.R.2
  • 172
    • 33746753299 scopus 로고    scopus 로고
    • Preclinical and clinical development of novel agents that target the protein kinase C family
    • SEROVA M, GHOUL A, BENHADJI KA et al.: Preclinical and clinical development of novel agents that target the protein kinase C family. Semin. Oncol. (2006) 33(4):466-478.
    • (2006) Semin. Oncol , vol.33 , Issue.4 , pp. 466-478
    • SEROVA, M.1    GHOUL, A.2    BENHADJI, K.A.3
  • 173
    • 0030797705 scopus 로고    scopus 로고
    • Toxicological and pharmacokinetic properties of chemically modified antisense oligonucleotide inhibitors of PKC-α and C-raf kinase
    • HENRY SP, MONTEITH D, BENNETT F, LEVIN AA: Toxicological and pharmacokinetic properties of chemically modified antisense oligonucleotide inhibitors of PKC-α and C-raf kinase. Anticancer Drug Des. (1997) 12(5):409-420.
    • (1997) Anticancer Drug Des , vol.12 , Issue.5 , pp. 409-420
    • HENRY, S.P.1    MONTEITH, D.2    BENNETT, F.3    LEVIN, A.A.4
  • 174
    • 0028292570 scopus 로고
    • Inhibition of protein kinase C-α expression in human A549 cells by antisense oligonucleotides inhibits induction of intercellular adhesion molecule 1 (ICAM-1) mRNA by phorbol esters
    • DEAN NM, MCKAY R, CONDON TP, BENNETT CF: Inhibition of protein kinase C-α expression in human A549 cells by antisense oligonucleotides inhibits induction of intercellular adhesion molecule 1 (ICAM-1) mRNA by phorbol esters. J. Biol. Chem. (1994) 269(23):16416-16424.
    • (1994) J. Biol. Chem , vol.269 , Issue.23 , pp. 16416-16424
    • DEAN, N.M.1    MCKAY, R.2    CONDON, T.P.3    BENNETT, C.F.4
  • 175
    • 0029833019 scopus 로고    scopus 로고
    • Treatment of glioblastoma U-87 by systemic administration of an antisense protein kinase C-α phosphorothioate oligodeoxynucleotide
    • YAZAKI T, AHMAD S, CHAHLAVI A et al.: Treatment of glioblastoma U-87 by systemic administration of an antisense protein kinase C-α phosphorothioate oligodeoxynucleotide. Mol. Pharmacol. (1996) 50(2):236-242.
    • (1996) Mol. Pharmacol , vol.50 , Issue.2 , pp. 236-242
    • YAZAKI, T.1    AHMAD, S.2    CHAHLAVI, A.3
  • 176
    • 2442543262 scopus 로고    scopus 로고
    • The role of protein kinase C-α (PKC-α) in cancer and its modulation by the novel PKC-α-specific inhibitor aprinocarsen
    • HANAUSKE AR, SUNDELL K, LAHN M: The role of protein kinase C-α (PKC-α) in cancer and its modulation by the novel PKC-α-specific inhibitor aprinocarsen. Curr. Pharm. Des. (2004) 10(16):1923-1936.
    • (2004) Curr. Pharm. Des , vol.10 , Issue.16 , pp. 1923-1936
    • HANAUSKE, A.R.1    SUNDELL, K.2    LAHN, M.3
  • 177
    • 0032730633 scopus 로고    scopus 로고
    • Phase I study of an antisense oligonucleotide to protein kinase C-α (ISIS 3521/CGP 64128A) in patients with cancer
    • YUEN AR, HALSEY J, FISHER GA et al.: Phase I study of an antisense oligonucleotide to protein kinase C-α (ISIS 3521/CGP 64128A) in patients with cancer. Clin. Cancer Res. (1999) 5(11):3357-3363.
    • (1999) Clin. Cancer Res , vol.5 , Issue.11 , pp. 3357-3363
    • YUEN, A.R.1    HALSEY, J.2    FISHER, G.A.3
  • 178
    • 9144226837 scopus 로고    scopus 로고
    • A Phase II trial of aprinocarsen, an antisense oligonucleotide inhibitor of protein kinase C-α, administered as a 21-day infusion to patients with advanced ovarian carcinoma
    • ADVANI R, PEETHAMBARAM P, LUM BL et al.: A Phase II trial of aprinocarsen, an antisense oligonucleotide inhibitor of protein kinase C-α, administered as a 21-day infusion to patients with advanced ovarian carcinoma. Cancer (2004) 100(2):321-326.
    • (2004) Cancer , vol.100 , Issue.2 , pp. 321-326
    • ADVANI, R.1    PEETHAMBARAM, P.2    LUM, B.L.3
  • 179
    • 4644305430 scopus 로고    scopus 로고
    • Phase II study of ISIS 3521, an antisense oligodeoxynucleotide to protein kinase C-α, in patients with previously treated low-grade non-Hodgkin's lymphoma
    • RAO S, WATKINS D, CUNNINGHAM D et al.: Phase II study of ISIS 3521, an antisense oligodeoxynucleotide to protein kinase C-α, in patients with previously treated low-grade non-Hodgkin's lymphoma. Ann. Oncol. (2004) 15(9):1413-1418.
    • (2004) Ann. Oncol , vol.15 , Issue.9 , pp. 1413-1418
    • RAO, S.1    WATKINS, D.2    CUNNINGHAM, D.3
  • 180
    • 14644438523 scopus 로고    scopus 로고
    • Efficacy and toxicity of the antisense oligonucleotide aprinocarsen directed against protein kinase C-α delivered as a 21-day continuous intravenous infusion in patients with recurrent high-grade astrocytomas
    • GROSSMAN SA, ALAVI JB, SUPKO JG et al.: Efficacy and toxicity of the antisense oligonucleotide aprinocarsen directed against protein kinase C-α delivered as a 21-day continuous intravenous infusion in patients with recurrent high-grade astrocytomas. Neuro Oncol. (2005) 7(1):32-40.
    • (2005) Neuro Oncol , vol.7 , Issue.1 , pp. 32-40
    • GROSSMAN, S.A.1    ALAVI, J.B.2    SUPKO, J.G.3
  • 181
    • 33645453677 scopus 로고    scopus 로고
    • Phase III study of gemcitabine and cisplatin with or without aprinocarsen, a protein kinase C-α antisense oligonucleotide, in patients with advanced-stage non-small-cell lung cancer
    • PAZ-ARES L, DOUILLARD JY, KORALEWSKI P et al.: Phase III study of gemcitabine and cisplatin with or without aprinocarsen, a protein kinase C-α antisense oligonucleotide, in patients with advanced-stage non-small-cell lung cancer. J. Clin. Oncoll. (2006) 24(9):1428-1434.
    • (2006) J. Clin. Oncoll , vol.24 , Issue.9 , pp. 1428-1434
    • PAZ-ARES, L.1    DOUILLARD, J.Y.2    KORALEWSKI, P.3
  • 182
    • 2342613651 scopus 로고    scopus 로고
    • Characterization of the interaction of ingenol 3-angelate with protein kinase C
    • KEDEI N, LUNDBERG DJ, TOTH A et al.: Characterization of the interaction of ingenol 3-angelate with protein kinase C. Cancer Res. (2004) 64(9):3243-3255.
    • (2004) Cancer Res , vol.64 , Issue.9 , pp. 3243-3255
    • KEDEI, N.1    LUNDBERG, D.J.2    TOTH, A.3
  • 183
    • 23744432856 scopus 로고    scopus 로고
    • PEP005, a selective small-molecule activator of protein kinase C, has potent antileukemic activity mediated via the δ isoform of PKC
    • HAMPSON P, CHAHAL H, KHANIM F et al.: PEP005, a selective small-molecule activator of protein kinase C, has potent antileukemic activity mediated via the δ isoform of PKC. Blood (2005) 106(4):1362-1368.
    • (2005) Blood , vol.106 , Issue.4 , pp. 1362-1368
    • HAMPSON, P.1    CHAHAL, H.2    KHANIM, F.3
  • 184
    • 33846657965 scopus 로고    scopus 로고
    • Proceedings of the first international conference on PEP005
    • 357-362
    • OGBOURNE SM, HAMPSON P, LORD JM et al.: Proceedings of the first international conference on PEP005. Anticancer Drugs (2007) 18(3):357-362.
    • (2007) Anticancer Drugs , vol.18 , Issue.3
    • OGBOURNE, S.M.1    HAMPSON, P.2    LORD, J.M.3
  • 185
    • 0142166328 scopus 로고    scopus 로고
    • Cancer chemoprevention with dietary phytochemicals
    • SURH YJ: Cancer chemoprevention with dietary phytochemicals. Nat. Reb. Cancer (2003) 3(10):768-780.
    • (2003) Nat. Reb. Cancer , vol.3 , Issue.10 , pp. 768-780
    • SURH, Y.J.1
  • 186
    • 33744490370 scopus 로고    scopus 로고
    • Biological effects of curcumin and its role in cancer chemoprevention and therapy
    • SINGH S, KHAR A: Biological effects of curcumin and its role in cancer chemoprevention and therapy. Anticancer Agents Med. Chem. (2006) 6(3):259-270.
    • (2006) Anticancer Agents Med. Chem , vol.6 , Issue.3 , pp. 259-270
    • SINGH, S.1    KHAR, A.2
  • 188
    • 2142784187 scopus 로고    scopus 로고
    • Biological properties of curcumin - cellular and molecular mechanisms of action
    • JOE B, VIJAYKUMAR M, LOKESH BR: Biological properties of curcumin - cellular and molecular mechanisms of action. Crit. Rev. Food Sci. Nutr. (2004) 44(2):97-111.
    • (2004) Crit. Rev. Food Sci. Nutr , vol.44 , Issue.2 , pp. 97-111
    • JOE, B.1    VIJAYKUMAR, M.2    LOKESH, B.R.3
  • 189
    • 33644901007 scopus 로고    scopus 로고
    • Multiple biological activities of curcumin: A short review
    • MAHESHWARI RK, SINGH AK, GADDIPATI J, SRIMAL RC: Multiple biological activities of curcumin: a short review. Life Sci. (2006) 78(18):2081-2087.
    • (2006) Life Sci , vol.78 , Issue.18 , pp. 2081-2087
    • MAHESHWARI, R.K.1    SINGH, A.K.2    GADDIPATI, J.3    SRIMAL, R.C.4
  • 190
    • 0141955061 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) inhibits constitutive and IL-6-inducible STAT3 phosphorylation in human multiple mycloma cells
    • BHARTI AC, DONATO N, AGGARWAL BB: Curcumin (diferuloylmethane) inhibits constitutive and IL-6-inducible STAT3 phosphorylation in human multiple mycloma cells. J. Immunol. (2003) 171(7):3863-3871.
    • (2003) J. Immunol , vol.171 , Issue.7 , pp. 3863-3871
    • BHARTI, A.C.1    DONATO, N.2    AGGARWAL, B.B.3
  • 191
    • 0037305821 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) down-regulates the constitutive activation of NF-κB and IκBα kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis
    • BHARTI AC, DONATO N, SINGH S, AGGARWAL BB: Curcumin (diferuloylmethane) down-regulates the constitutive activation of NF-κB and IκBα kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis. Blood (2003) 101(3):1053-1062.
    • (2003) Blood , vol.101 , Issue.3 , pp. 1053-1062
    • BHARTI, A.C.1    DONATO, N.2    SINGH, S.3    AGGARWAL, B.B.4
  • 192
    • 0027173480 scopus 로고
    • Inhibitory effects of curcumin on protein kinase C activity induced by 12-O-tetradccanoyl-phorbol-13-acetate in NIH 3T3 cells
    • LIU JY, LIN SJ, LIN JK: Inhibitory effects of curcumin on protein kinase C activity induced by 12-O-tetradccanoyl-phorbol-13-acetate in NIH 3T3 cells. Carrinogenesis (1993) 14(5):857-861.
    • (1993) Carrinogenesis , vol.14 , Issue.5 , pp. 857-861
    • LIU, J.Y.1    LIN, S.J.2    LIN, J.K.3
  • 193
    • 33846531680 scopus 로고    scopus 로고
    • Modulation of protein kinase C by curcumin; inhibition and activation switched by calcium ions
    • MAHMMOUD YA: Modulation of protein kinase C by curcumin; inhibition and activation switched by calcium ions. Br. J. Pharmacol. (2007) 150(2):200-208.
    • (2007) Br. J. Pharmacol , vol.150 , Issue.2 , pp. 200-208
    • MAHMMOUD, Y.A.1
  • 194
    • 5744224686 scopus 로고    scopus 로고
    • Therapeutic potential of natural compounds that regulate the activity of protein kinase C
    • CARTER CA, KANE CJ: Therapeutic potential of natural compounds that regulate the activity of protein kinase C. Curr. Med. Chem. (2004) 11(21):2883-2902.
    • (2004) Curr. Med. Chem , vol.11 , Issue.21 , pp. 2883-2902
    • CARTER, C.A.1    KANE, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.