메뉴 건너뛰기




Volumn 18, Issue 4, 2003, Pages 1301-1312

Nuclear protein kinase C isoforms: Key players in multiple cell functions?

Author keywords

Apoptosis; Differentiation; Phosphorylation; Proliferation; Signal transduction

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; CHELERYTHRINE; CHELERYTHRINE CHLORIDE; DIACYLGLYCEROL; ETOPOSIDE; LIPID; NUCLEAR PROTEIN; PHOSPHOTRANSFERASE; PROTEIN KINASE C INHIBITOR; PROTEIN KINASE C ISOENZYME; PROTEIN SERINE THREONINE KINASE; ROTTLERIN; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 0142031096     PISSN: 02133911     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (42)

References (116)
  • 1
    • 0034776809 scopus 로고    scopus 로고
    • Protein kinase C isozymes, novel phorbol ester receptors and cancer chemotherapy
    • Barry O.P. and Kazanietz M.G. (2001). Protein kinase C isozymes, novel phorbol ester receptors and cancer chemotherapy. Curr. Pharm. Des. 7, 1725-1744.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1725-1744
    • Barry, O.P.1    Kazanietz, M.G.2
  • 2
    • 0029764358 scopus 로고    scopus 로고
    • Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: Fluorescent-labeled protein kinase C β I
    • Bastiaens P.I.H. and Jovin T.M. (1996). Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: Fluorescent-labeled protein kinase C β I. Proc. Natl. Acad. Sci. USA 93, 8407-8412.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8407-8412
    • Bastiaens, P.I.H.1    Jovin, T.M.2
  • 3
    • 0028359025 scopus 로고
    • Differential nuclear localization of protein kinase C isoforms in neuroblastoma x glioma hybrid cells
    • Beckmann R., Lindschau C., Haller H., Hucho F. and Buchner K. (1994). Differential nuclear localization of protein kinase C isoforms in neuroblastoma x glioma hybrid cells. Eur. J. Biochem. 222, 335-343.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 335-343
    • Beckmann, R.1    Lindschau, C.2    Haller, H.3    Hucho, F.4    Buchner, K.5
  • 4
    • 0036374278 scopus 로고    scopus 로고
    • Regulating the mammalian genome: The role of nuclear architecture
    • Berezney R. (2002). Regulating the mammalian genome: The role of nuclear architecture. Advan. Enzyme Regul. 42, 39-52.
    • (2002) Advan. Enzyme Regul. , vol.42 , pp. 39-52
    • Berezney, R.1
  • 5
    • 0033664370 scopus 로고    scopus 로고
    • RACK1 is up-regulated in angiogenesis and human carcinomas
    • Berns H., Humar R., Hengerer B., Kiefer F.N. and Battegay E.J. (2000). RACK1 is up-regulated in angiogenesis and human carcinomas. FASEB J. 14, 2549-2558.
    • (2000) FASEB J. , vol.14 , pp. 2549-2558
    • Berns, H.1    Humar, R.2    Hengerer, B.3    Kiefer, F.N.4    Battegay, E.J.5
  • 6
    • 0031811302 scopus 로고    scopus 로고
    • Accumulation of catalytically active PKC-ζ into the nucleus of HL-60 cell line plays a key role in the induction of granulocytic differentiation mediated by all-trans retinoic acid
    • Bertolaso L., Gibellini D., Secchiero P., Previati M., Falcione D., Visani G., Rizzoli R., Capitani S. and Zauli G. (1998). Accumulation of catalytically active PKC-ζ into the nucleus of HL-60 cell line plays a key role in the induction of granulocytic differentiation mediated by all-trans retinoic acid. Brit. J. Haematol. 100, 541-549.
    • (1998) Brit. J. Haematol. , vol.100 , pp. 541-549
    • Bertolaso, L.1    Gibellini, D.2    Secchiero, P.3    Previati, M.4    Falcione, D.5    Visani, G.6    Rizzoli, R.7    Capitani, S.8    Zauli, G.9
  • 8
    • 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 P.M. and Brodie C. (2002). Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide. Mol. Cell. Biol. 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
  • 9
    • 0037246123 scopus 로고    scopus 로고
    • Regulation of cell apoptosis by protein kinase C δ
    • Brodie C. and Blumberg P.M. (2003). Regulation of cell apoptosis by protein kinase C δ. Apoptosis 8, 19-27.
    • (2003) Apoptosis , vol.8 , pp. 19-27
    • Brodie, C.1    Blumberg, P.M.2
  • 11
    • 0028914602 scopus 로고
    • Protein kinase C in the transduction of signals toward and within the cell nucleus
    • Buchner K. (1995). Protein kinase C in the transduction of signals toward and within the cell nucleus. Eur. J. Biochem. 228, 211-221.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 211-221
    • Buchner, K.1
  • 12
    • 0033989653 scopus 로고    scopus 로고
    • The role of protein kinase C in the regulation of cell growth and in signalling to the cell nucleus
    • Buchner K. (2000). The role of protein kinase C in the regulation of cell growth and in signalling to the cell nucleus. J. Cancer Res. Clin. Oncol. 126, 1-11.
    • (2000) J. Cancer Res. Clin. Oncol. , vol.126 , pp. 1-11
    • Buchner, K.1
  • 13
    • 0037070603 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositol 3-kinase in nuclear translocation of protein kinase C ζ induced by C2-ceramide in rat hepatocytes
    • Calcerrada M.C., Miguel B.G., Martin L., Catalan R.E. and Martinez A.M. (2002). Involvement of phosphatidylinositol 3-kinase in nuclear translocation of protein kinase C ζ induced by C2-ceramide in rat hepatocytes. FEBS Lett. 514, 361-365.
    • (2002) FEBS Lett. , vol.514 , pp. 361-365
    • Calcerrada, M.C.1    Miguel, B.G.2    Martin, L.3    Catalan, R.E.4    Martinez, A.M.5
  • 17
    • 0032584661 scopus 로고    scopus 로고
    • A major, transformation-sensitive PKC-binding protein is also a PKC substrate involved in cytoskeletal remodeling
    • Chapline C., Cottom J., Tobin H., Hulmes J., Crabb J. and Jaken S. (1998). A major, transformation-sensitive PKC-binding protein is also a PKC substrate involved in cytoskeletal remodeling. J. Biol. Chem. 273, 19482-19489.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19482-19489
    • Chapline, C.1    Cottom, J.2    Tobin, H.3    Hulmes, J.4    Crabb, J.5    Jaken, S.6
  • 18
    • 0029866203 scopus 로고    scopus 로고
    • Identification of a major protein kinase C-binding protein and substrate in rat embryo fibroblasts. Decreased expression in transformed cells
    • Chapline C., Mousseau B., Ramsay K., Duddy S., Li Y., Kiley S.C. and Jaken S. (1996). Identification of a major protein kinase C-binding protein and substrate in rat embryo fibroblasts. Decreased expression in transformed cells. J. Biol. Chem. 271, 6417-6122.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6417-6122
    • Chapline, C.1    Mousseau, B.2    Ramsay, K.3    Duddy, S.4    Li, Y.5    Kiley, S.C.6    Jaken, S.7
  • 19
    • 0037166312 scopus 로고    scopus 로고
    • Protein kinase C-β II is an apoptotic lamin kinase in polyomavirus-transformed, etoposide-treated pyF111 rat fibroblasts
    • Chiarini A., Whitfield J.F., Armato U. and Dal Pra I. (2002). Protein kinase C-β II is an apoptotic lamin kinase in polyomavirus-transformed, etoposide-treated pyF111 rat fibroblasts. J. Biol. Chem. 277, 18827-18839.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18827-18839
    • Chiarini, A.1    Whitfield, J.F.2    Armato, U.3    Dal Pra, I.4
  • 21
    • 0036500525 scopus 로고    scopus 로고
    • Generation of diacylglycerol molecular species through the cell cycle: A role for 1-stearoyl, 2-arachidonyl glycerol in the activation of nuclear protein kinase C-βII at G2/M
    • Deacon E.M., Pettitt T.R., Webb P., Cross T., Chahal H., Wakelam M.J.O. and Lord J.M. (2002). Generation of diacylglycerol molecular species through the cell cycle: A role for 1-stearoyl, 2-arachidonyl glycerol in the activation of nuclear protein kinase C-βII at G2/M. J. Cell Sci. 115, 983-989.
    • (2002) J. Cell Sci. , vol.115 , pp. 983-989
    • Deacon, E.M.1    Pettitt, T.R.2    Webb, P.3    Cross, T.4    Chahal, H.5    Wakelam, M.J.O.6    Lord, J.M.7
  • 23
    • 0037110732 scopus 로고    scopus 로고
    • Nuclear import of PKCδ is required for apoptosis: Identification of a novel nuclear import sequence
    • DeVries T.A., Neville M.C. and Reyland M.E. (2002). Nuclear import of PKCδ is required for apoptosis: Identification of a novel nuclear import sequence. EMBO J. 22, 6050-6060.
    • (2002) EMBO J. , vol.22 , pp. 6050-6060
    • DeVries, T.A.1    Neville, M.C.2    Reyland, M.E.3
  • 24
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus
    • Divecha N., Banfic H. and Irvine R.F. (1991). The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. EMBO J. 10, 3207-3214.
    • (1991) EMBO J. , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 27
    • 0030875555 scopus 로고    scopus 로고
    • Phosphorylation at conserved carboxyl-terminus hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
    • Edwards A.S. and Newton A.C. (1997). Phosphorylation at conserved carboxyl-terminus hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C. J. Biol. Chem. 272, 18382-18390.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18382-18390
    • Edwards, A.S.1    Newton, A.C.2
  • 28
    • 0037382424 scopus 로고    scopus 로고
    • Protein kinase C δ activation and translocation to the nucleus are required for fatty acid-induced apoptosis of insulin-secreting cells
    • Eitel K., Staiger H., Rieger J., Mischak H., Brandhorst H., Brendel M.D., Bretzel R.G., Haring H.U. and Kellerer M. (2003). Protein kinase C δ activation and translocation to the nucleus are required for fatty acid-induced apoptosis of insulin-secreting cells. Diabetes 52, 991-997.
    • (2003) Diabetes , vol.52 , pp. 991-997
    • Eitel, K.1    Staiger, H.2    Rieger, J.3    Mischak, H.4    Brandhorst, H.5    Brendel, M.D.6    Bretzel, R.G.7    Haring, H.U.8    Kellerer, M.9
  • 29
    • 0036315410 scopus 로고    scopus 로고
    • Translocation of the classic protein kinase C isoforms in porcine oocytes: Implications of protein kinase C involvement in the regulation of nuclear activity and cortical granule exocytosis
    • Fan H.-Y., Tong C., Li M.-Y., Lian L., Chen D.-Y., Schatten H. and Sun Q.-S. (1990). Translocation of the classic protein kinase C isoforms in porcine oocytes: Implications of protein kinase C involvement in the regulation of nuclear activity and cortical granule exocytosis. Exp. Cell Res. 277, 183-191.
    • (2002) Exp. Cell Res. , vol.277 , pp. 183-191
    • Fan, H.-Y.1    Tong, C.2    Li, M.-Y.3    Lian, L.4    Chen, D.-Y.5    Schatten, H.6    Sun, Q.-S.7
  • 30
    • 0025363850 scopus 로고
    • Role of nuclear protein kinase C in the mitogenic response to platelet-derived growth factor
    • Fields A.P., Tyler G., Kraft A.S. and May W.S. (1990). Role of nuclear protein kinase C in the mitogenic response to platelet-derived growth factor. J. Cell Sci. 96, 107-114.
    • (1990) J. Cell Sci. , vol.96 , pp. 107-114
    • Fields, A.P.1    Tyler, G.2    Kraft, A.S.3    May, W.S.4
  • 32
    • 0035866371 scopus 로고    scopus 로고
    • Elevated protein kinase C βII is an early promotive event in colon carcinogenesis
    • Gökmen-Polar Y., Murray N.R., Velasco M.A., Gatalica Z. and Fieds A.P. (2001). Elevated protein kinase C βII is an early promotive event in colon carcinogenesis. Cancer Res. 61, 1375-1381.
    • (2001) Cancer Res. , vol.61 , pp. 1375-1381
    • Gökmen-Polar, Y.1    Murray, N.R.2    Velasco, M.A.3    Gatalica, Z.4    Fieds, A.P.5
  • 34
    • 0026067787 scopus 로고
    • Selective translocation of β II-protein kinase C to the nucleus of human promyelocytic (HL60) leukemia cells
    • Hocevar B.A. and Fields A.P. (1991). Selective translocation of β II-protein kinase C to the nucleus of human promyelocytic (HL60) leukemia cells. J. Biol. Chem. 266, 28-33.
    • (1991) J. Biol. Chem. , vol.266 , pp. 28-33
    • Hocevar, B.A.1    Fields, A.P.2
  • 35
    • 0027502241 scopus 로고
    • Identification of protein kinase C (PKC) phosphorylation sites on human lamin B. Potential role of PKC in nuclear lamina structural dynamics
    • Hocevar B.A., Burns D.J. and Fields A.P. (1993). Identification of protein kinase C (PKC) phosphorylation sites on human lamin B. Potential role of PKC in nuclear lamina structural dynamics. J. Biol. Chem. 268, 7545-7552.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7545-7552
    • Hocevar, B.A.1    Burns, D.J.2    Fields, A.P.3
  • 36
    • 0026510349 scopus 로고
    • Protein kinase C isotypes in human erythroleukemia cell proliferation and differentiation
    • Hocevar B.A., Morrow D.M., Tykocinski M.L. and Fields A.P. (1992). Protein kinase C isotypes in human erythroleukemia cell proliferation and differentiation. J. Cell Sci. 101, 671-679.
    • (1992) J. Cell Sci. , vol.101 , pp. 671-679
    • Hocevar, B.A.1    Morrow, D.M.2    Tykocinski, M.L.3    Fields, A.P.4
  • 37
    • 0035233927 scopus 로고    scopus 로고
    • Modulation of protein kinase C in antitumor treatment
    • Hofmann J. (2001). Modulation of protein kinase C in antitumor treatment. Rev. Physiol. Biochem. Pharmacol. 142, 1-96.
    • (2001) Rev. Physiol. Biochem. Pharmacol. , vol.142 , pp. 1-96
    • Hofmann, J.1
  • 38
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug H. and Sarre T.F. (1993). Protein kinase C isoenzymes: Divergence in signal transduction? Biochem. J. 291, 329-343.
    • (1993) Biochem. J. , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 39
    • 0028181082 scopus 로고
    • Identification and characterization of α-protein kinase C binding proteins in normal and transformed REF52 cells
    • Hyatt S.L., Liao L., Chapline C. and Jaken S. (1994). Identification and characterization of α-protein kinase C binding proteins in normal and transformed REF52 cells. Biochemistry 33, 1223-1228.
    • (1994) Biochemistry , vol.33 , pp. 1223-1228
    • Hyatt, S.L.1    Liao, L.2    Chapline, C.3    Jaken, S.4
  • 40
    • 0030614872 scopus 로고    scopus 로고
    • A protein kinase Cδ-binding protein SRBC whose expression is induced by serum starvation
    • Izumi Y., Hirai S., Tamai Y., Fujise-Matsuoka A., Nishimura Y. and Ohno S. (1997). A protein kinase Cδ-binding protein SRBC whose expression is induced by serum starvation. J. Biol. Chem. 272, 7381-7389.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7381-7389
    • Izumi, Y.1    Hirai, S.2    Tamai, Y.3    Fujise-Matsuoka, A.4    Nishimura, Y.5    Ohno, S.6
  • 41
    • 0034057863 scopus 로고    scopus 로고
    • Protein kinase C binding partners
    • Jaken S. and Parker P.J. (2000). Protein kinase C binding partners. Bioessays 22, 245-2354.
    • (2000) Bioessays , vol.22 , pp. 245-254
    • Jaken, S.1    Parker, P.J.2
  • 42
    • 0034041537 scopus 로고    scopus 로고
    • Nuclear targeting signal recognition: A key control point in nuclear transport?
    • Jans D.A., Xiao C. and Lam M.H.C. (2000). Nuclear targeting signal recognition: A key control point in nuclear transport? Bioessays 22, 532-544.
    • (2000) Bioessays , vol.22 , pp. 532-544
    • Jans, D.A.1    Xiao, C.2    Lam, M.H.C.3
  • 43
    • 0029745535 scopus 로고    scopus 로고
    • A protein kinase C translocation inhibitor as an isoenzyme-selective antagonist of cardiac function
    • Johnson J.A., Gray M.O., Chen C.-H. and Mochly-Rosen D. (1996). A protein kinase C translocation inhibitor as an isoenzyme-selective antagonist of cardiac function. J. Biol. Chem. 271, 24962-24966.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24962-24966
    • Johnson, J.A.1    Gray, M.O.2    Chen, C.-H.3    Mochly-Rosen, D.4
  • 44
    • 0030611049 scopus 로고    scopus 로고
    • Ca2+ differentially regulates conventional protein kinase Cs' membrane interaction and activation
    • Keranen L.M. and Newton A.C. (1997). Ca2+ differentially regulates conventional protein kinase Cs' membrane interaction and activation. J. Biol. Chem. 272, 25959-25967.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25959-25967
    • Keranen, L.M.1    Newton, A.C.2
  • 45
    • 0036947279 scopus 로고    scopus 로고
    • Protein kinase Cδ: Activation mechanisms and functions
    • Kikkawa U., Matsuzaki H. and Yamamoto T. (2002). Protein kinase Cδ: Activation mechanisms and functions. J. Biochem. 132, 831-839.
    • (2002) J. Biochem. , vol.132 , pp. 831-839
    • Kikkawa, U.1    Matsuzaki, H.2    Yamamoto, T.3
  • 46
    • 0027991782 scopus 로고
    • Membrane and nuclear protein kinase C activation in the early stages of diethylnitrosamine-induced rat hepatocarcinogenesis
    • La Porta C.A. and Comolli R. (1994). Membrane and nuclear protein kinase C activation in the early stages of diethylnitrosamine-induced rat hepatocarcinogenesis. Carcinogenesis 15, 1743-1747.
    • (1994) Carcinogenesis , vol.15 , pp. 1743-1747
    • La Porta, C.A.1    Comolli, R.2
  • 47
    • 0031427095 scopus 로고    scopus 로고
    • Changes in protein kinase C α, δ and in nuclear β isoform expression in tumour and lung metastatic nodules induced by diethylnitrosamine in the rat
    • La Porta C.A., Tessitore L. and Comolli R. (1997). Changes in protein kinase C α, δ and in nuclear β isoform expression in tumour and lung metastatic nodules induced by diethylnitrosamine in the rat. Carcinogenesis 18, 715-719.
    • (1997) Carcinogenesis , vol.18 , pp. 715-719
    • La Porta, C.A.1    Tessitore, L.2    Comolli, R.3
  • 48
    • 0024318707 scopus 로고
    • Type 3 protein kinase C localization to the nuclear envelope of phorbol ester-treated NIH 3T3 cells
    • Leach K.L., Powers E.A., Ruff V.A., Jaken S. and Kaufmann S. (1989). Type 3 protein kinase C localization to the nuclear envelope of phorbol ester-treated NIH 3T3 cells. J. Cell Biol. 109, 685-695.
    • (1989) J. Cell Biol. , vol.109 , pp. 685-695
    • Leach, K.L.1    Powers, E.A.2    Ruff, V.A.3    Jaken, S.4    Kaufmann, S.5
  • 49
    • 0028267821 scopus 로고
    • Protein kinase C domains involved in interactions with other proteins
    • Liao L., Hyatt S.L., Chapline C. and Jaken S. (1994). Protein kinase C domains involved in interactions with other proteins. Biochemistry 33, 1229-1233.
    • (1994) Biochemistry , vol.33 , pp. 1229-1233
    • Liao, L.1    Hyatt, S.L.2    Chapline, C.3    Jaken, S.4
  • 50
    • 0033068181 scopus 로고    scopus 로고
    • Protein kinase C α is an effector of hexamethylene bisacetamide-induced differentiation of Friend erythroleukemia cells
    • Mallia C.M., Aguirre V., McGary E., Scandurro A., Noguki C. and Beckman B.S. (1999). Protein kinase C α is an effector of hexamethylene bisacetamide-induced differentiation of Friend erythroleukemia cells. Exp. Cell Res. 246, 348-354.
    • (1999) Exp. Cell Res. , vol.246 , pp. 348-354
    • Mallia, C.M.1    Aguirre, V.2    McGary, E.3    Scandurro, A.4    Noguki, C.5    Beckman, B.S.6
  • 51
    • 0036036872 scopus 로고    scopus 로고
    • Protein kinase C-ζ overexpression induces erythroid phenotype in the monocytic leukaemia cell line U937
    • Mansat-De Ma V., De Thonel A., Gaulin V., Demu C., Laurent G. and Quillet-Mary A. (2002). Protein kinase C-ζ overexpression induces erythroid phenotype in the monocytic leukaemia cell line U937. Brit. J. Haematol. 118, 646-653.
    • (2002) Brit. J. Haematol. , vol.118 , pp. 646-653
    • Mansat-De Ma, V.1    De Thonel, A.2    Gaulin, V.3    Demu, C.4    Laurent, G.5    Quillet-Mary, A.6
  • 52
    • 0032853333 scopus 로고    scopus 로고
    • Topology of inositol lipid signal transduction in the nucleus
    • Maraldi N.M., Zini N., Santi S. and Manzoli F.A. (1999). Topology of inositol lipid signal transduction in the nucleus. J. Cell. Physiol. 181, 203-217.
    • (1999) J. Cell. Physiol. , vol.181 , pp. 203-217
    • Maraldi, N.M.1    Zini, N.2    Santi, S.3    Manzoli, F.A.4
  • 54
    • 0034652722 scopus 로고    scopus 로고
    • Enhanced nuclear diacylglycerol kinase activity in response to a mitogenic stimulation of quiescent Swiss 3T3 cells with insulin-like growth factor I
    • Martelli A.M., Tabellini G., Bortul R., Manzoli L., Bareggi R., Baldini G., Grill V., Zweyer M., Narducci P. and Cocco L. (2000). Enhanced nuclear diacylglycerol kinase activity in response to a mitogenic stimulation of quiescent Swiss 3T3 cells with insulin-like growth factor I. Cancer Res. 60, 815-821.
    • (2000) Cancer Res. , vol.60 , pp. 815-821
    • Martelli, A.M.1    Tabellini, G.2    Bortul, R.3    Manzoli, L.4    Bareggi, R.5    Baldini, G.6    Grill, V.7    Zweyer, M.8    Narducci, P.9    Cocco, L.10
  • 58
    • 0031029249 scopus 로고    scopus 로고
    • Nuclear translocation of PKC ζ during ischemia and its inhibition by wortmannin, an inhibitor of phosphatidylinositol 3-kinase
    • Mizukami Y., Hirata T. and Yoshida K. (1997). Nuclear translocation of PKC ζ during ischemia and its inhibition by wortmannin, an inhibitor of phosphatidylinositol 3-kinase. FEBS Lett. 401, 247-251.
    • (1997) FEBS Lett. , vol.401 , pp. 247-251
    • Mizukami, Y.1    Hirata, T.2    Yoshida, K.3
  • 59
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • Mochly-Rosen D. and Gordon A.S. (1998). Anchoring proteins for protein kinase C: A means for isozyme selectivity. FASEB J. 12, 35-42.
    • (1998) FASEB J. , vol.12 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 60
    • 0029198668 scopus 로고
    • The dynamic properties and possible functions of nuclear lamins
    • Moir R.D., Spann T.P. and Goldman R.D. (1995). The dynamic properties and possible functions of nuclear lamins. Int. Rev. Cytol., 162B, 141-182.
    • (1995) Int. Rev. Cytol. , vol.162 B , pp. 141-182
    • Moir, R.D.1    Spann, T.P.2    Goldman, R.D.3
  • 61
    • 0032496141 scopus 로고    scopus 로고
    • Phosphatidylglycerol is a physiologic activator of nuclear protein kinase C
    • Murray N.R. and Fields A.P. (1998). Phosphatidylglycerol is a physiologic activator of nuclear protein kinase C. J. Biol. Chem. 273, 11514-11520.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11514-11520
    • Murray, N.R.1    Fields, A.P.2
  • 62
    • 0033577858 scopus 로고    scopus 로고
    • Overexpression of protein kinase C βII induces colonic hyperproliferation and increased sensitivity to colon carcinogenesis
    • Murray N.R., Davidson L.A., Chapkin R.S., Gustafson W.C., Schattenberg D.G. and Fields A.P. (1999). Overexpression of protein kinase C βII induces colonic hyperproliferation and increased sensitivity to colon carcinogenesis. J. Cell Biol. 145, 699-711.
    • (1999) J. Cell Biol. , vol.145 , pp. 699-711
    • Murray, N.R.1    Davidson, L.A.2    Chapkin, R.S.3    Gustafson, W.C.4    Schattenberg, D.G.5    Fields, A.P.6
  • 63
    • 0028169459 scopus 로고
    • Presence of a β II protein kinase C-selective nuclear membrane activation factor in human leukemia cells
    • Murray N.R., Burns D.J. and Fields A.P. (1994). Presence of a β II protein kinase C-selective nuclear membrane activation factor in human leukemia cells. J. Biol. Chem. 269, 21385-12390.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21385-21390
    • Murray, N.R.1    Burns, D.J.2    Fields, A.P.3
  • 64
    • 0034221202 scopus 로고    scopus 로고
    • The role of protein kinase C isoforms in cell proliferation and apoptosis
    • Musashi M., Ota S. and Shiroshita N. (2000). The role of protein kinase C isoforms in cell proliferation and apoptosis. Int. J. Hematol. 72, 12-19.
    • (2000) Int. J. Hematol. , vol.72 , pp. 12-19
    • Musashi, M.1    Ota, S.2    Shiroshita, N.3
  • 65
    • 0028319088 scopus 로고
    • Selective nuclear translocation of protein kinase C α in Swiss 3T3 cells treated with IGF-I, PDGF and EGF
    • Neri L.M., Billi A.M., Manzoli L., Rubbini S., Gilmour R.S., Cocco L. and Martelli A.M. (1994). Selective nuclear translocation of protein kinase C α in Swiss 3T3 cells treated with IGF-I, PDGF and EGF. FEBS Lett. 347, 63-68.
    • (1994) FEBS Lett. , vol.347 , pp. 63-68
    • Neri, L.M.1    Billi, A.M.2    Manzoli, L.3    Rubbini, S.4    Gilmour, R.S.5    Cocco, L.6    Martelli, A.M.7
  • 66
    • 0032491522 scopus 로고    scopus 로고
    • Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-α
    • Neri L.M., Borgatti P., Capitani S. and Martelli A.M. (1998). Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-α. J. Biol. Chem. 273, 29738-29744.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29738-29744
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 67
    • 0032797276 scopus 로고    scopus 로고
    • Increase in nuclear phosphatidylinositol 3-kinase activity and phosphatidylinositol (3,4,5) trisphosphate synthesis precede PKC-ζ translocation to the nucleus of NGF-treated PC12 cells
    • Neri L.M., Martelli A.M., Colamussi M.L., Borgatti P., Marchisio M. and Capitani S. (1999). Increase in nuclear phosphatidylinositol 3-kinase activity and phosphatidylinositol (3,4,5) trisphosphate synthesis precede PKC-ζ translocation to the nucleus of NGF-treated PC12 cells. FASEB J. 13, 2299-2310.
    • (1999) FASEB J. , vol.13 , pp. 2299-2310
    • Neri, L.M.1    Martelli, A.M.2    Colamussi, M.L.3    Borgatti, P.4    Marchisio, M.5    Capitani, S.6
  • 68
    • 0036789740 scopus 로고    scopus 로고
    • Protein kinase C isoforms and lipid second messengers: A critical nuclear partnership?
    • Neri L.M., Borgatti P., Capitani S. and Martelli A.M. (2002a). Protein kinase C isoforms and lipid second messengers: A critical nuclear partnership? Histol. Histopathol. 17, 1311-1316.
    • (2002) Histol. Histopathol. , vol.17 , pp. 1311-1316
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 69
    • 0036200219 scopus 로고    scopus 로고
    • Proliferating or differentiating stimuli act on different lipid-dependent signaling pathways in nuclei of human leukemia cells
    • Neri L.M., Bortul R., Borgatti P., Tabellini G., Baldini G., Capitani S. and Martelli A.M. (2002b). Proliferating or differentiating stimuli act on different lipid-dependent signaling pathways in nuclei of human leukemia cells. Mol. Biol. Cell 13, 947-964.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 947-964
    • Neri, L.M.1    Bortul, R.2    Borgatti, P.3    Tabellini, G.4    Baldini, G.5    Capitani, S.6    Martelli, A.M.7
  • 70
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton A.C. (1997). Regulation of protein kinase C. Curr. Opin. Cell Biol. 9, 161-167.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 71
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton A.C. (2001). Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem. Rev. 101, 2353-2364.
    • (2001) Chem. Rev. , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 72
    • 0035110880 scopus 로고    scopus 로고
    • Experimental observations of a nuclear matrix
    • Nickerson J.A. (2001). Experimental observations of a nuclear matrix. J. Cell Sci. 114, 463-474.
    • (2001) J. Cell Sci. , vol.114 , pp. 463-474
    • Nickerson, J.A.1
  • 73
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y. (1995). Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9, 484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 74
    • 0029586689 scopus 로고
    • Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells
    • Ogawa H., Inouye S., Tsuji F.I., Yasuda K. and Umesono K. (1995). Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells. Proc. Natl. Acad. Sci. USA 92, 11899-11903.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11899-11903
    • Ogawa, H.1    Inouye, S.2    Tsuji, F.I.3    Yasuda, K.4    Umesono, K.5
  • 75
    • 0027650428 scopus 로고
    • Protein kinase C as a transducer of nuclear signals
    • Olson E.N., Burgess R. and Staudinger J. (1993). Protein kinase C as a transducer of nuclear signals. Cell Growth Diff. 4, 699-705.
    • (1993) Cell Growth Diff. , vol.4 , pp. 699-705
    • Olson, E.N.1    Burgess, R.2    Staudinger, J.3
  • 76
    • 0029124172 scopus 로고
    • Analysis of MAP 4 function in living cells using green fluorescent protein (GFP) chimeras
    • Olson K.R., McIntosh J.R. and Olmsted J.B. (1995). Analysis of MAP 4 function in living cells using green fluorescent protein (GFP) chimeras. J. Cell Biol. 130, 639-650.
    • (1995) J. Cell Biol. , vol.130 , pp. 639-650
    • Olson, K.R.1    McIntosh, J.R.2    Olmsted, J.B.3
  • 77
    • 0029927422 scopus 로고    scopus 로고
    • The role of proteases during apoptosis
    • Patel T., Gores G.J. and Kaufmann S.H. (1996). The role of proteases during apoptosis. FASEB J. 10, 587-597.
    • (1996) FASEB J. , vol.10 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 78
    • 0026720458 scopus 로고
    • Expression of intermediate filament proteins in TPA-induced MPC-11 and HL-60 cells
    • Paulin-Levasseur M. and Julien M. (1992). Expression of intermediate filament proteins in TPA-induced MPC-11 and HL-60 cells. Exp. Cell Res. 199, 363-372.
    • (1992) Exp. Cell Res. , vol.199 , pp. 363-372
    • Paulin-Levasseur, M.1    Julien, M.2
  • 79
    • 0035918217 scopus 로고    scopus 로고
    • Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase Cλ
    • Perander M., Bjorkoy G. and Johansen T. (2001). Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase Cλ. J. Biol. Chem. 276, 13015-13024.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13015-13024
    • Perander, M.1    Bjorkoy, G.2    Johansen, T.3
  • 80
    • 0032559826 scopus 로고    scopus 로고
    • An activated protein kinase C α gives a differentiation signal for hematopoietic progenitor cells and mimicks macrophages colony-stimulating factor-stimulated signaling events
    • Pierce A., Heyworth C.M., Nicholls S.E., Spooncer E., Dexter T.M., Lord J.M., Owen-Lynch P.J., Wark G. and Whetton A.D. (1998). An activated protein kinase C α gives a differentiation signal for hematopoietic progenitor cells and mimicks macrophages colony-stimulating factor-stimulated signaling events. J. Cell Biol. 140, 1511-1518.
    • (1998) J. Cell Biol. , vol.140 , pp. 1511-1518
    • Pierce, A.1    Heyworth, C.M.2    Nicholls, S.E.3    Spooncer, E.4    Dexter, T.M.5    Lord, J.M.6    Owen-Lynch, P.J.7    Wark, G.8    Whetton, A.D.9
  • 81
    • 0033785313 scopus 로고    scopus 로고
    • Apoptosis and cancer: Strategies for integrating programmed cell death
    • Reed C.J. (2000). Apoptosis and cancer: Strategies for integrating programmed cell death. Semin. Hematol. 37, 9-16.
    • (2000) Semin. Hematol. , vol.37 , pp. 9-16
    • Reed, C.J.1
  • 82
    • 0029311281 scopus 로고
    • Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
    • Rizzuto R., Brini M., Pizzo P., Murgia M. and Pozzan T. (1995). Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr. Biol. 5, 636-642.
    • (1995) Curr. Biol. , vol.5 , pp. 636-642
    • Rizzuto, R.1    Brini, M.2    Pizzo, P.3    Murgia, M.4    Pozzan, T.5
  • 84
    • 0032849088 scopus 로고    scopus 로고
    • New insights into the regulation of protein kinase C and novel phorbol ester receptors
    • Ron D. and Kazanietz M.G. (1999). New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J. 13, 1658-1673.
    • (1999) FASEB J. , vol.13 , pp. 1658-1673
    • Ron, D.1    Kazanietz, M.G.2
  • 85
    • 0028805699 scopus 로고
    • C2 region-derived peptides inhibit translocation and function of β protein kinase C in vivo
    • Ron D., Luo J. and Mochly-Rosen D. (1995). C2 region-derived peptides inhibit translocation and function of β protein kinase C in vivo. J. Biol. Chem. 270, 24180-24187.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24180-24187
    • Ron, D.1    Luo, J.2    Mochly-Rosen, D.3
  • 86
    • 0028801624 scopus 로고
    • An autoregulatory region in protein kinase C: The pseudoanchoring site
    • Ron D. and Mochly-Rosen D. (1995). An autoregulatory region in protein kinase C: The pseudoanchoring site. Proc. Natl. Acad. Sci. USA 92, 492-496.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 492-496
    • Ron, D.1    Mochly-Rosen, D.2
  • 87
    • 0034323375 scopus 로고    scopus 로고
    • Uncoupling of βIIPKC from its targeting protein RACK1 in response to ethanol in cultured cells and mouse brain
    • Ron D., Vagts A.J., Dohrman D.P., Yaka R., Jiang Z., Ya L., Crabbe J., Grisel J.E. and Diamond I. (2000). Uncoupling of βIIPKC from its targeting protein RACK1 in response to ethanol in cultured cells and mouse brain. FASEB J. 14, 2303-2314.
    • (2000) FASEB J. , vol.14 , pp. 2303-2314
    • Ron, D.1    Vagts, A.J.2    Dohrman, D.P.3    Yaka, R.4    Jiang, Z.5    Ya, L.6    Crabbe, J.7    Grisel, J.E.8    Diamond, I.9
  • 89
    • 0037090614 scopus 로고    scopus 로고
    • Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation
    • Ruchaud S., Korfali N., Villa P., Kottke T.J., Dingwall C., Kaufmann S.H. and Earnshaw W.C. (2002). Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. EMBO J. 21, 1967-1977.
    • (2002) EMBO J. , vol.21 , pp. 1967-1977
    • Ruchaud, S.1    Korfali, N.2    Villa, P.3    Kottke, T.J.4    Dingwall, C.5    Kaufmann, S.H.6    Earnshaw, W.C.7
  • 90
    • 0029791502 scopus 로고    scopus 로고
    • Transport of protein kinase C α into the nucleus requires intact cytoskeleton while the transport of a protein containing a canonical nuclear localization signal does not
    • Schmalz D., Kalkbrenner F., Hucho F. and Buchner K. (1996). Transport of protein kinase C α into the nucleus requires intact cytoskeleton while the transport of a protein containing a canonical nuclear localization signal does not. J. Cell Sci. 109, 2401-2406.
    • (1996) J. Cell Sci. , vol.109 , pp. 2401-2406
    • Schmalz, D.1    Kalkbrenner, F.2    Hucho, F.3    Buchner, K.4
  • 91
    • 0031826010 scopus 로고    scopus 로고
    • Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by proteins with a classical nuclear localization signal
    • Schmalz D., Hucho F. and Buchner K. (1998). Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by proteins with a classical nuclear localization signal. J. Cell Sci. 111, 1823-1830.
    • (1998) J. Cell Sci. , vol.111 , pp. 1823-1830
    • Schmalz, D.1    Hucho, F.2    Buchner, K.3
  • 93
    • 0032502793 scopus 로고    scopus 로고
    • Lamin B phosphorylation by protein kinase C α and proteolysis during apoptosis in human leukemia HL60 cells
    • Shimizu T., Cao C.X., Shao R.G. and Pommier Y. (1998). Lamin B phosphorylation by protein kinase C α and proteolysis during apoptosis in human leukemia HL60 cells. J. Biol. Chem. 273, 8669-8674.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8669-8674
    • Shimizu, T.1    Cao, C.X.2    Shao, R.G.3    Pommier, Y.4
  • 94
    • 0036855827 scopus 로고    scopus 로고
    • Activation mechanisms of protein kinase C: Maturation, catalytic activation, and targeting
    • Shirai Y. and Saito N. (2002). Activation mechanisms of protein kinase C: Maturation, catalytic activation, and targeting. J. Biochem. 132, 663-668.
    • (2002) J. Biochem. , vol.132 , pp. 663-668
    • Shirai, Y.1    Saito, N.2
  • 95
    • 0038348529 scopus 로고    scopus 로고
    • AKAP149 is a novel PP1 specifier required to maintain nuclear envelope integrity in G1 phase
    • Steen R.L., Beullens M., Landsverk H.B., Bollen M. and Collas P. (2003). AKAP149 is a novel PP1 specifier required to maintain nuclear envelope integrity in G1 phase. J. Cell Sci. 116, 2237-2246.
    • (2003) J. Cell Sci. , vol.116 , pp. 2237-2246
    • Steen, R.L.1    Beullens, M.2    Landsverk, H.B.3    Bollen, M.4    Collas, P.5
  • 96
    • 0030722721 scopus 로고    scopus 로고
    • A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition
    • Sun B., Murray N.R. and Fields A.P. (1997). A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition. J. Biol. Chem. 272, 26313-26317.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26313-26317
    • Sun, B.1    Murray, N.R.2    Fields, A.P.3
  • 98
    • 0029666264 scopus 로고    scopus 로고
    • βII protein kinase C is required for the G2/M phase transition of cell cycle
    • Thompson L.J. and Fields A.P. (1996). βII protein kinase C is required for the G2/M phase transition of cell cycle. J. Biol. Chem. 271, 15045-15053.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15045-15053
    • Thompson, L.J.1    Fields, A.P.2
  • 99
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N.A. and Lazebnik Y. (1998). Caspases: Enemies within. Science 281, 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 100
    • 0028170988 scopus 로고
    • Protein kinase C modulation in apoptotic rat thymocytes: An ultrastructural analysis
    • Trubiani O., Borgatti P. and Di Primio R. (1994). Protein kinase C modulation in apoptotic rat thymocytes: An ultrastructural analysis. Histochemistry 102, 311-316.
    • (1994) Histochemistry , vol.102 , pp. 311-316
    • Trubiani, O.1    Borgatti, P.2    Di Primio, R.3
  • 101
    • 0037203345 scopus 로고    scopus 로고
    • Lipoapoptosis: Its mechanisms and its diseases
    • Unger R.H. and Orci L. (2002). Lipoapoptosis: Its mechanisms and its diseases. Biochim. Biophys. Acta 1585, 202-212.
    • (2002) Biochim. Biophys. Acta , vol.1585 , pp. 202-212
    • Unger, R.H.1    Orci, L.2
  • 102
    • 0033938117 scopus 로고    scopus 로고
    • Life and death decisions: Regulation of apoptosis by proteolysis of signaling molecules
    • Utz P.J. and Anderson P. (2000). Life and death decisions: Regulation of apoptosis by proteolysis of signaling molecules. Cell Death Diff. 7, 589-602.
    • (2000) Cell Death Diff. , vol.7 , pp. 589-602
    • Utz, P.J.1    Anderson, P.2
  • 103
    • 0029052413 scopus 로고
    • Two nuclear localization signals present in the basic-helix 1 domains of MyoD promote its active nuclear translocation and can function independently
    • Vandromme M., Cavadore J.-C., Bonnieu A., Froeschlé A., Lamb N. and Fernandez A. (1995). Two nuclear localization signals present in the basic-helix 1 domains of MyoD promote its active nuclear translocation and can function independently. Proc. Natl. Acad. Sci. USA 92, 4646-4650.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4646-4650
    • Vandromme, M.1    Cavadore, J.-C.2    Bonnieu, A.3    Froeschlé, A.4    Lamb, N.5    Fernandez, A.6
  • 104
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux D.L. and Korsmeyer S.J. (1999). Cell death in development. Cell 96, 245-254.
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 105
  • 106
    • 0030939960 scopus 로고    scopus 로고
    • Opioid peptide gene expression in the primary hereditary cardiomyopathy of the Syrian hamster
    • Ventura C., Pintus G., Fiori M.G., Bennardini F., Pinna G. and Gaspa L. (1997). Opioid peptide gene expression in the primary hereditary cardiomyopathy of the Syrian hamster. J. Biol. Chem. 272, 6685-6692.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6685-6692
    • Ventura, C.1    Pintus, G.2    Fiori, M.G.3    Bennardini, F.4    Pinna, G.5    Gaspa, L.6
  • 107
    • 0032577693 scopus 로고    scopus 로고
    • Nuclear opioid receptors activate opioid peptide gene transcription in isolated myocardial nuclei
    • Ventura C., Maioli M., Pintus G., Posadino A.M. and Tadolini B. (1998). Nuclear opioid receptors activate opioid peptide gene transcription in isolated myocardial nuclei. J. Biol. Chem. 273, 13383-13386.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13383-13386
    • Ventura, C.1    Maioli, M.2    Pintus, G.3    Posadino, A.M.4    Tadolini, B.5
  • 108
    • 0033969185 scopus 로고    scopus 로고
    • Elf-pulsed magnetic fields modulate opioid peptide gene expression in myocardial cells
    • Ventura C., Maioli M., Pintus G., Gottardi G. and Bersani F. (2000). Elf-pulsed magnetic fields modulate opioid peptide gene expression in myocardial cells. Cardiovasc. Res. 45, 1054-1064.
    • (2000) Cardiovasc. Res. , vol.45 , pp. 1054-1064
    • Ventura, C.1    Maioli, M.2    Pintus, G.3    Gottardi, G.4    Bersani, F.5
  • 109
    • 0037418937 scopus 로고    scopus 로고
    • Dynorphin B is an agonist of nuclear opioid receptors coupling nuclear protein kinase C activation to the transcription of cardiogenic genes in GTR1 embryonic stem cells
    • in press
    • Ventura C., Zinellu E., Maninchedda E. and Maioli M. (2003). Dynorphin B is an agonist of nuclear opioid receptors coupling nuclear protein kinase C activation to the transcription of cardiogenic genes in GTR1 embryonic stem cells. Circ. Res., in press.
    • (2003) Circ. Res.
    • Ventura, C.1    Zinellu, E.2    Maninchedda, E.3    Maioli, M.4
  • 110
    • 0034632057 scopus 로고    scopus 로고
    • Analysis of the subcellular distribution of protein kinase C α using PKC-GFP fusion proteins
    • Wagner S., Harteneck C., Hucho F. and Buchner K. (2000). Analysis of the subcellular distribution of protein kinase C α using PKC-GFP fusion proteins. Exp. Cell Res. 258, 204-214.
    • (2000) Exp. Cell Res. , vol.258 , pp. 204-214
    • Wagner, S.1    Harteneck, C.2    Hucho, F.3    Buchner, K.4
  • 111
    • 0036200364 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C
    • White W.O., Seibenhener M.L. and Wooten M.W. (2002). Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C. J. Cell. Biochem. 85, 42-53.
    • (2002) J. Cell. Biochem. , vol.85 , pp. 42-53
    • White, W.O.1    Seibenhener, M.L.2    Wooten, M.W.3
  • 112
    • 0030758084 scopus 로고    scopus 로고
    • Transport of protein kinase C isoforms to the nucleus of PC12 cells by nerve growth factor: Association of atypical ζ-PKC with the nuclear matrix
    • Wooten M.W., Zhou G., Wooten M.C. and Seibenhener M.L. (1997). Transport of protein kinase C isoforms to the nucleus of PC12 cells by nerve growth factor: Association of atypical ζ-PKC with the nuclear matrix. J. Neurosci. Res. 49, 393-403.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 393-403
    • Wooten, M.W.1    Zhou, G.2    Wooten, M.C.3    Seibenhener, M.L.4
  • 113
    • 0035805635 scopus 로고    scopus 로고
    • Protein kinase C α - Mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C β1 in Swiss 3T3 cells
    • Xu A., Wang Y., Xu L.Y. and Gilmour R.S. (2001). Protein kinase C α - Mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C β1 in Swiss 3T3 cells. J. Biol. Chem. 276, 14980-14986.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14980-14986
    • Xu, A.1    Wang, Y.2    Xu, L.Y.3    Gilmour, R.S.4
  • 115
    • 0030723178 scopus 로고    scopus 로고
    • Nucleolin is a protein kinase C-ζ substrate. Connection between cell surface signaling and nucleus in PC12 cells
    • Zhou G., Seibenhener M.L. and Wooten M.W. (1997). Nucleolin is a protein kinase C-ζ substrate. Connection between cell surface signaling and nucleus in PC12 cells. J. Biol. Chem. 272, 31130-31137.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31130-31137
    • Zhou, G.1    Seibenhener, M.L.2    Wooten, M.W.3
  • 116
    • 0028989334 scopus 로고
    • Immunocytochemical evaluation of protein kinase C translocation to the inner nuclear matrix in 3T3 mouse fibroblasts after IGF-I treatment
    • Zini N., Martelli A.M., Neri L.M., Bavelloni A., Sabatelli P., Santi S. and Maraldi N.M. (1995). Immunocytochemical evaluation of protein kinase C translocation to the inner nuclear matrix in 3T3 mouse fibroblasts after IGF-I treatment. Histochemistry 103, 447-457.
    • (1995) Histochemistry , vol.103 , pp. 447-457
    • Zini, N.1    Martelli, A.M.2    Neri, L.M.3    Bavelloni, A.4    Sabatelli, P.5    Santi, S.6    Maraldi, N.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.