메뉴 건너뛰기




Volumn 42, Issue 1, 2003, Pages 45-55

Interaction of palmitoylcarnitine with protein kinase C in neuroblastoma NB-2a cells

Author keywords

Neuroblastoma; Palmitoylcarnitine; Phorbol ester binding; Phosphorylation; Protein kinase C

Indexed keywords

PALMITOYLCARNITINE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; SERINE;

EID: 0037210368     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(02)00067-0     Document Type: Article
Times cited : (11)

References (86)
  • 1
    • 0024368011 scopus 로고
    • Poration by alpha-toxin and streptolysin O: An approach to analyze intracellular processes
    • Ahnert-Hilger G., Mach W., Fohr K.J., Gratzl M. Poration by alpha-toxin and streptolysin O: an approach to analyze intracellular processes. Meth. Cell Biol. 31:1989;63-90.
    • (1989) Meth. Cell Biol. , vol.31 , pp. 63-90
    • Ahnert-Hilger, G.1    Mach, W.2    Fohr, K.J.3    Gratzl, M.4
  • 2
    • 0025367731 scopus 로고
    • A method for measuring protein kinase C activity in permeabilized T lymphocytes by using peptide substrates. Evidence for multiple pathways of kinase activation
    • Alexander D.R., Graves J.D., Lucas S.C., Cantrell D.A., Crumpton M.J. A method for measuring protein kinase C activity in permeabilized T lymphocytes by using peptide substrates. Evidence for multiple pathways of kinase activation. Biochem. J. 268:1990;303-308.
    • (1990) Biochem. J. , vol.268 , pp. 303-308
    • Alexander, D.R.1    Graves, J.D.2    Lucas, S.C.3    Cantrell, D.A.4    Crumpton, M.J.5
  • 3
    • 0027200336 scopus 로고
    • Potential role of phospholipase A2 in HL-60 cell differentiation to macrophages induced by protein kinase C activation
    • Asaoka Y., Yoshida K., Sasaki Y., Nishizuka Y. Potential role of phospholipase A2 in HL-60 cell differentiation to macrophages induced by protein kinase C activation. Proc. Natl. Acad. Sci. U.S.A. 90:1993;4917-4921.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 4917-4921
    • Asaoka, Y.1    Yoshida, K.2    Sasaki, Y.3    Nishizuka, Y.4
  • 4
    • 0014566695 scopus 로고
    • Establishment of functional clonal lines of neurons from mouse neuroblastoma
    • Augusti-Tocco G., Sato G. Establishment of functional clonal lines of neurons from mouse neuroblastoma. Proc. Natl. Acad. Sci. U.S.A. 64:1969;311-315.
    • (1969) Proc. Natl. Acad. Sci. U.S.A. , vol.64 , pp. 311-315
    • Augusti-Tocco, G.1    Sato, G.2
  • 5
    • 0033565608 scopus 로고    scopus 로고
    • The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation
    • Behn-Krappa A., Newton A.C. The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation. Curr. Biol. 9:1999;728-737.
    • (1999) Curr. Biol. , vol.9 , pp. 728-737
    • Behn-Krappa, A.1    Newton, A.C.2
  • 6
  • 7
    • 0041411152 scopus 로고    scopus 로고
    • Comparison of the roles of the C1a and C1b domains of protein kinase C alpha in ligand induced translocation in NIH 3T3 cells
    • Bogi K., Lorenzo P.S., Acs P., Szallasi Z., Wagner G.S., Blumberg P.M. Comparison of the roles of the C1a and C1b domains of protein kinase C alpha in ligand induced translocation in NIH 3T3 cells. FEBS Lett. 456:1999;27-30.
    • (1999) FEBS Lett. , vol.456 , pp. 27-30
    • Bogi, K.1    Lorenzo, P.S.2    Acs, P.3    Szallasi, Z.4    Wagner, G.S.5    Blumberg, P.M.6
  • 8
    • 0001926779 scopus 로고
    • Lipid regulation of protein kinase
    • Lester, D.S., Epand, R.M. (Eds.). Ellis Horwood, New York
    • Burns, D.J., Bell, R.M., 1992. Lipid regulation of protein kinase. In: Lester, D.S., Epand, R.M. (Eds.), Protein Kinase C: Current Concepts and Future Perspectives. Ellis Horwood, New York, pp. 25-40.
    • (1992) Protein Kinase C: Current Concepts and Future Perspectives , pp. 25-40
    • Burns, D.J.1    Bell, R.M.2
  • 9
    • 0026062945 scopus 로고
    • Protein kinase C contains two phorbol ester binding domains
    • Burns D.J., Bell R.M. Protein kinase C contains two phorbol ester binding domains. J. Biol. Chem. 266:1991;18330-18338.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18330-18338
    • Burns, D.J.1    Bell, R.M.2
  • 12
    • 0027104825 scopus 로고
    • The role of protein kinase C isoenzymes in the regulation of cell proliferation and differentiation
    • Clemens M.J., Trayner I., Menaya J. The role of protein kinase C isoenzymes in the regulation of cell proliferation and differentiation. J. Cell Sci. 103:1992;881-887.
    • (1992) J. Cell Sci. , vol.103 , pp. 881-887
    • Clemens, M.J.1    Trayner, I.2    Menaya, J.3
  • 13
    • 0042099466 scopus 로고    scopus 로고
    • The C2 domain of protein kinase C alpha is directly involved in the diacylglycerol-dependent binding of the C1 domain to the membrane
    • Conesa-Zamora P., Gomez-Fernandez J.C., Corbalan-Garcia S. The C2 domain of protein kinase C alpha is directly involved in the diacylglycerol-dependent binding of the C1 domain to the membrane. Biochim. Biophys. Acta. 1487:2000;246-254.
    • (2000) Biochim. Biophys. Acta , vol.1487 , pp. 246-254
    • Conesa-Zamora, P.1    Gomez-Fernandez, J.C.2    Corbalan-Garcia, S.3
  • 14
    • 0030946258 scopus 로고    scopus 로고
    • Regulated binding of the protein kinase C substrate GAP-43 to the V0/C2 region of protein kinase C-delta
    • Dekker L.V., Parker P.J. Regulated binding of the protein kinase C substrate GAP-43 to the V0/C2 region of protein kinase C-delta. J. Biol. Chem. 272:1997;12747-12753.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12747-12753
    • Dekker, L.V.1    Parker, P.J.2
  • 16
    • 0027332733 scopus 로고
    • Expression of an oncogenic rasHa gene in murine keratinocytes induces tyrosine phosphorylation and reduced activity of protein kinase C delta
    • Denning M.F., Dlugosz A.A., Howett M.K., Yuspa S.H. Expression of an oncogenic rasHa gene in murine keratinocytes induces tyrosine phosphorylation and reduced activity of protein kinase C delta. J. Biol. Chem. 268:1993;26079-26081.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26079-26081
    • Denning, M.F.1    Dlugosz, A.A.2    Howett, M.K.3    Yuspa, S.H.4
  • 17
    • 0029924152 scopus 로고    scopus 로고
    • Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta
    • Denning M.F., Dlugosz A.A., Threadgill D.W., Magnuson T., Yuspa S.H. Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta. J. Biol. Chem. 271:1996;5325-5331.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5325-5331
    • Denning, M.F.1    Dlugosz, A.A.2    Threadgill, D.W.3    Magnuson, T.4    Yuspa, S.H.5
  • 18
    • 0028799452 scopus 로고
    • Cholesterol sulfate activates multiple protein kinase C isoenzymes and induces granular cell differentiation in cultured murine keratinocytes
    • Denning M.F., Kazanietz M.G., Blumberg P.M., Yuspa S.H. Cholesterol sulfate activates multiple protein kinase C isoenzymes and induces granular cell differentiation in cultured murine keratinocytes. Cell Growth Differ. 6:1995;1619-1626.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1619-1626
    • Denning, M.F.1    Kazanietz, M.G.2    Blumberg, P.M.3    Yuspa, S.H.4
  • 19
    • 0029655983 scopus 로고    scopus 로고
    • Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo
    • Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J. Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo. Mol. Cell Biol. 16:1996;105-114.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 105-114
    • Diaz-Meco, M.T.1    Municio, M.M.2    Sanchez, P.3    Lozano, J.4    Moscat, J.5
  • 21
    • 0034616296 scopus 로고    scopus 로고
    • Dual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol
    • Dutil E.M., Newton A.C. Dual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol. J. Biol. Chem. 275:2000;10697-10701.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10697-10701
    • Dutil, E.M.1    Newton, A.C.2
  • 22
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
    • Dutil E.M., Toker A., Newton A.C. Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1). Curr. Biol. 8:1998;1366-1375.
    • (1998) Curr. Biol. , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 23
    • 0030875555 scopus 로고    scopus 로고
    • Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
    • Edwards A.S., Newton A.C. Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C. J. Biol. Chem. 272:1997;18382-18390.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18382-18390
    • Edwards, A.S.1    Newton, A.C.2
  • 24
    • 0025334605 scopus 로고
    • The role of membrane biophysical properties in the regulation of protein kinase C activity
    • Epand R.M., Lester D.S. The role of membrane biophysical properties in the regulation of protein kinase C activity. Trends Pharmacol. Sci. 11:1990;317-320.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 317-320
    • Epand, R.M.1    Lester, D.S.2
  • 25
    • 0034595645 scopus 로고    scopus 로고
    • Regulation of receptor-mediated protein kinase C membrane trafficking by autophosphorylation
    • Feng X., Becker K.P., Stribling S.D., Peters K.G., Hannun Y.A. Regulation of receptor-mediated protein kinase C membrane trafficking by autophosphorylation. J. Biol. Chem. 275:2000;17024-17034.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17024-17034
    • Feng, X.1    Becker, K.P.2    Stribling, S.D.3    Peters, K.G.4    Hannun, Y.A.5
  • 26
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna R., Jaken S. Protein kinase C signaling and oxidative stress. Free Radic. Biol. Med. 28:2000;1349-1361.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 28
    • 0026738349 scopus 로고
    • Examination of the role of the proteolytically-activated form of protein kinase C in the differentiation of human haemopoietic cells
    • Hardy S.J., Haylock D.N., Lopez A.F., Murray A.W. Examination of the role of the proteolytically-activated form of protein kinase C in the differentiation of human haemopoietic cells. Differentiation. 50:1992;189-202.
    • (1992) Differentiation , vol.50 , pp. 189-202
    • Hardy, S.J.1    Haylock, D.N.2    Lopez, A.F.3    Murray, A.W.4
  • 29
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubstrate prototope in its regulatory domain
    • House C., Kemp B.E. Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science. 238:1987;1726-1728.
    • (1987) Science , vol.238 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 30
    • 0025305538 scopus 로고
    • Protein kinase C pseudosubstrate prototope: Structure-function relationships
    • House C., Kemp B.E. Protein kinase C pseudosubstrate prototope: structure-function relationships. Cell Signal. 2:1990;187-190.
    • (1990) Cell Signal , vol.2 , pp. 187-190
    • House, C.1    Kemp, B.E.2
  • 31
    • 0017716047 scopus 로고
    • Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain
    • Inoue M., Kishimoto A., Takai Y., Nishizuka Y. Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain. J. Biol. Chem. 252:1977;7610-7616.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7610-7616
    • Inoue, M.1    Kishimoto, A.2    Takai, Y.3    Nishizuka, Y.4
  • 32
    • 0034057863 scopus 로고    scopus 로고
    • Protein kinase C binding partners
    • Jaken S., Parker P.J. Protein kinase C binding partners. Bioessays. 22:2000;245-254.
    • (2000) Bioessays , vol.22 , pp. 245-254
    • Jaken, S.1    Parker, P.J.2
  • 34
    • 0028914673 scopus 로고
    • Characterization of the cysteine-rich region of the Caenorhabditis elegans protein Unc-13 as a high affinity phorbol ester receptor. Analysis of ligand-binding interactions, lipid cofactor requirements, and inhibitor sensitivity
    • Kazanietz M.G., Lewin N.E., Bruns J.D., Blumberg P.M. Characterization of the cysteine-rich region of the Caenorhabditis elegans protein Unc-13 as a high affinity phorbol ester receptor. Analysis of ligand-binding interactions, lipid cofactor requirements, and inhibitor sensitivity. J. Biol. Chem. 270:1995;10777-10783.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10777-10783
    • Kazanietz, M.G.1    Lewin, N.E.2    Bruns, J.D.3    Blumberg, P.M.4
  • 35
    • 0034717940 scopus 로고    scopus 로고
    • Fatty acid import into mitochondria
    • Kerner J., Hoppel C. Fatty acid import into mitochondria. Biochim. Biophys. Acta. 1486:2000;1-17.
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 1-17
    • Kerner, J.1    Hoppel, C.2
  • 36
    • 0033581954 scopus 로고    scopus 로고
    • Increased protein kinase C delta in mammary tumor cells: Relationship to transformtion and metastatic progression
    • Kiley S.C., Clark K.J., Duddy S.K., Welch D.R., Jaken S. Increased protein kinase C delta in mammary tumor cells: relationship to transformtion and metastatic progression. Oncogene. 18:1999;6748-6757.
    • (1999) Oncogene , vol.18 , pp. 6748-6757
    • Kiley, S.C.1    Clark, K.J.2    Duddy, S.K.3    Welch, D.R.4    Jaken, S.5
  • 37
    • 0033168515 scopus 로고    scopus 로고
    • Protein kinase C delta involvement in mammary tumor cell metastasis
    • Kiley S.C., Clark K.J., Goodnough M., Welch D.R., Jaken S. Protein kinase C delta involvement in mammary tumor cell metastasis. Cancer Res. 59:1999;3230-3238.
    • (1999) Cancer Res. , vol.59 , pp. 3230-3238
    • Kiley, S.C.1    Clark, K.J.2    Goodnough, M.3    Welch, D.R.4    Jaken, S.5
  • 38
    • 0021111512 scopus 로고
    • Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease
    • Kishimoto A., Kajikawa N., Shiota M., Nishizuka Y. Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease. J. Biol. Chem. 258:1983;1156-1164.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1156-1164
    • Kishimoto, A.1    Kajikawa, N.2    Shiota, M.3    Nishizuka, Y.4
  • 40
    • 0020698115 scopus 로고
    • 2+, phospholipid-dependent protein kinase associated with plasma membrane
    • 2+, phospholipid-dependent protein kinase associated with plasma membrane. Nature. 301:1983;621-623.
    • (1983) Nature , vol.301 , pp. 621-623
    • Kraft, A.S.1    Anderson, W.B.2
  • 41
    • 0034634651 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C delta on distinct tyrosine residues regulates specific cellular functions
    • Kronfeld I., Kazimirsky G., Lorenzo P.S., Garfield S.H., Blumberg P.M., Brodie C. Phosphorylation of protein kinase C delta on distinct tyrosine residues regulates specific cellular functions. J. Biol. Chem. 275:2000;35491-35498.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35491-35498
    • Kronfeld, I.1    Kazimirsky, G.2    Lorenzo, P.S.3    Garfield, S.H.4    Blumberg, P.M.5    Brodie, C.6
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good J.A., Ziegler W.H., Parekh D.B., Alessi D.R., Cohen P., Parker P.J. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science. 281:1998;2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 45
    • 0031786125 scopus 로고    scopus 로고
    • The sevenfold way of PKC regulation
    • Liu W.S., Heckman C.A. The sevenfold way of PKC regulation. Cell Signal. 10:1998;529-542.
    • (1998) Cell Signal , vol.10 , pp. 529-542
    • Liu, W.S.1    Heckman, C.A.2
  • 48
    • 0023003536 scopus 로고
    • The involvement of calpain in the activation of protein kinase C in neutrophils stimulated by phorbol myristic acid
    • Melloni E., Pontremoli S., Michetti M., Sacco O., Sparatore B., Horecker B.L. The involvement of calpain in the activation of protein kinase C in neutrophils stimulated by phorbol myristic acid. J. Biol. Chem. 261:1986;4101-4105.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4101-4105
    • Melloni, E.1    Pontremoli, S.2    Michetti, M.3    Sacco, O.4    Sparatore, B.5    Horecker, B.L.6
  • 50
    • 0025908315 scopus 로고
    • Identification of intracellular receptor proteins for activated protein kinase C
    • Mochly-Rosen D., Khaner H., Lopez J. Identification of intracellular receptor proteins for activated protein kinase C. Proc. Natl. Acad. Sci. U.S.A. 88:1991;3997-4000.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3997-4000
    • Mochly-Rosen, D.1    Khaner, H.2    Lopez, J.3
  • 51
    • 0025917246 scopus 로고
    • Intracellular receptors for activated protein kinase C: Identification of a binding site for the enzyme
    • Mochly-Rosen D., Khaner H., Lopez J., Smith B.L. Intracellular receptors for activated protein kinase C: identification of a binding site for the enzyme. J. Biol. Chem. 266:1991;14866-14868.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14866-14868
    • Mochly-Rosen, D.1    Khaner, H.2    Lopez, J.3    Smith, B.L.4
  • 52
    • 0029003788 scopus 로고
    • PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid
    • Muller G., Ayoub M., Storz P., Rennecke J., Fabbro D., Pfizenmaier K. PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid. EMBO J. 14:1995;1961-1969.
    • (1995) EMBO J. , vol.14 , pp. 1961-1969
    • Muller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 54
    • 0023600266 scopus 로고
    • Modulation by palmitoylcarnitine of protein kinase C activation
    • Nakadate T., Blumberg P.M. Modulation by palmitoylcarnitine of protein kinase C activation. Cancer Res. 47:1987;6537-6542.
    • (1987) Cancer Res. , vol.47 , pp. 6537-6542
    • Nakadate, T.1    Blumberg, P.M.2
  • 55
    • 0027535742 scopus 로고
    • Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi H., Brewer K.A., Exton J.H. Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 268:1993;13-16.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 57
    • 0031456381 scopus 로고    scopus 로고
    • Effect of palmitoylcarnitine on the cellular differentiation, proliferation and protein kinase C activity in neuroblastoma NB-2a cells
    • Nałȩcz K.A., Mroczkowska J.E., Berent U., Nałȩcz M.J. Effect of palmitoylcarnitine on the cellular differentiation, proliferation and protein kinase C activity in neuroblastoma NB-2a cells. Acta Neurobiol. Exp. 57:1997;263-274.
    • (1997) Acta Neurobiol. Exp. , vol.57 , pp. 263-274
    • Nałȩcz, K.A.1    Mroczkowska, J.E.2    Berent, U.3    Nałȩcz, M.J.4
  • 58
    • 0002999518 scopus 로고
    • Extraction, partial purification, and reconstitution of a mixture of carriers from the inner mitochondrial membrane
    • Azzi, A. Masotii, L., Vecli, A. (Eds.), Springer, Berlin
    • Nałȩcz, M.J., Nałȩcz, K.A., Azzi, A., 1986. Extraction, partial purification, and reconstitution of a mixture of carriers from the inner mitochondrial membrane. In: Azzi, A. Masotii, L., Vecli, A. (Eds.), Membrane Proteins: Isolation and Characterization, Springer, Berlin, pp. 67-75.
    • (1986) Membrane Proteins: Isolation and Characterization , pp. 67-75
    • Nałȩcz, M.J.1    Nałȩcz, K.A.2    Azzi, A.3
  • 59
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton A.C. Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270:1995;28495-28498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 60
    • 0032555778 scopus 로고    scopus 로고
    • Protein kinase C: A paradigm for regulation of protein function by two membrane-targeting modules
    • Newton A.C., Johnson J.E. Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim. Biophys. Acta. 1376:1998;155-172.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 155-172
    • Newton, A.C.1    Johnson, J.E.2
  • 62
    • 0027999633 scopus 로고
    • Requirement for negative charge on "activation loop" of protein kinase C
    • Orr J.W., Newton A.C. Requirement for negative charge on "activation loop" of protein kinase C. J. Biol. Chem. 269:1994;27715-27718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27715-27718
    • Orr, J.W.1    Newton, A.C.2
  • 63
    • 0033520995 scopus 로고    scopus 로고
    • Mammalian TOR controls one of two kinase pathways acting upon nPKCdelta and nPKCepsilon
    • Parekh D., Ziegler W., Yonezawa K., Hara K., Parker P.J. Mammalian TOR controls one of two kinase pathways acting upon nPKCdelta and nPKCepsilon. J. Biol. Chem. 274:1999;34758-34764.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34758-34764
    • Parekh, D.1    Ziegler, W.2    Yonezawa, K.3    Hara, K.4    Parker, P.J.5
  • 64
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh D.B., Ziegler W., Parker P.J. Multiple pathways control protein kinase C phosphorylation. EMBO J. 19:2000;496-503.
    • (2000) EMBO J. , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 65
    • 0033966463 scopus 로고    scopus 로고
    • The carnitine acyltransferases: Modulators of acyl-CoA-dependent reactions
    • Ramsay R.R. The carnitine acyltransferases: modulators of acyl-CoA-dependent reactions. Biochem. Soc. Trans. 28:2000s;182-186.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 182-186
    • Ramsay, R.R.1
  • 66
    • 0033505786 scopus 로고    scopus 로고
    • The role of the carnitine system in peroxisomal fatty acid oxidation
    • Ramsay R.R. The role of the carnitine system in peroxisomal fatty acid oxidation. Am. J. Med. Sci. 318:1999;28-35.
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 28-35
    • Ramsay, R.R.1
  • 68
    • 0026808818 scopus 로고
    • Potencies of protein kinase C inhibitors are dependent on the activators used to stimulate the enzyme
    • Robinson P.J. Potencies of protein kinase C inhibitors are dependent on the activators used to stimulate the enzyme. Biochem. Pharmacol. 44:1992;1325-1334.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1325-1334
    • Robinson, P.J.1
  • 69
    • 0032849088 scopus 로고    scopus 로고
    • New insights into the regulation of protein kinase C and novel phorbol ester receptors
    • Ron D., Kazanietz M.G. New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J. 13:1999;1658-1676.
    • (1999) FASEB J. , vol.13 , pp. 1658-1676
    • Ron, D.1    Kazanietz, M.G.2
  • 70
    • 0029891788 scopus 로고    scopus 로고
    • Differential growth regulation by all-trans retinoic acid is determined by protein kinase C alpha in human pancreatic carcinoma cells
    • Rosewicz S., Brembeck F., Kaiser A., Marschall Z.V., Riecken E.O. Differential growth regulation by all-trans retinoic acid is determined by protein kinase C alpha in human pancreatic carcinoma cells. Endocrinology. 137:1996;3340-3347.
    • (1996) Endocrinology , vol.137 , pp. 3340-3347
    • Rosewicz, S.1    Brembeck, F.2    Kaiser, A.3    Marschall, Z.V.4    Riecken, E.O.5
  • 71
    • 0026502424 scopus 로고
    • Purification and characterization of protein kinase C epsilon from rabbit brain
    • Saido T.C., Mizuno K., Konno Y., Osada S., Ohno S., Suzuki K. Purification and characterization of protein kinase C epsilon from rabbit brain. Biochemistry. 31:1992;482-490.
    • (1992) Biochemistry , vol.31 , pp. 482-490
    • Saido, T.C.1    Mizuno, K.2    Konno, Y.3    Osada, S.4    Ohno, S.5    Suzuki, K.6
  • 73
    • 0027431089 scopus 로고
    • Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells
    • Selbie L.A., Schmitz-Peiffer C., Sheng Y., Biden T.J. Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells. J. Biol. Chem. 268:1993;24296-24302.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24296-24302
    • Selbie, L.A.1    Schmitz-Peiffer, C.2    Sheng, Y.3    Biden, T.J.4
  • 74
    • 0019444439 scopus 로고
    • Axonally transported proteins associated with axon growth in rabbit central and peripheral nervous systems
    • Skene J.H., Willard M. Axonally transported proteins associated with axon growth in rabbit central and peripheral nervous systems. J. Cell Biol. 89:1981;96-103.
    • (1981) J. Cell Biol. , vol.89 , pp. 96-103
    • Skene, J.H.1    Willard, M.2
  • 75
    • 0019829507 scopus 로고
    • Changes in axonally transported proteins during axon regeneration in toad retinal ganglion cells
    • Skene J.H., Willard M. Changes in axonally transported proteins during axon regeneration in toad retinal ganglion cells. J. Cell Biol. 89:1981;86-95.
    • (1981) J. Cell Biol. , vol.89 , pp. 86-95
    • Skene, J.H.1    Willard, M.2
  • 77
    • 0017745032 scopus 로고
    • Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. I. Purification and characterization of an active enzyme from bovine cerebellum
    • Takai Y., Kishimoto A., Inoue M., Nishizuka Y. Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. I. Purification and characterization of an active enzyme from bovine cerebellum. J. Biol. Chem. 252:1977;7603-7609.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7603-7609
    • Takai, Y.1    Kishimoto, A.2    Inoue, M.3    Nishizuka, Y.4
  • 78
    • 0018800888 scopus 로고
    • Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids
    • Takai Y., Kishimoto A., Iwasa Y., Kawahara Y., Mori T., Nishizuka Y. Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids. J. Biol. Chem. 254:1979;3692-3695.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3692-3695
    • Takai, Y.1    Kishimoto, A.2    Iwasa, Y.3    Kawahara, Y.4    Mori, T.5    Nishizuka, Y.6
  • 79
    • 0030707562 scopus 로고    scopus 로고
    • TOR signalling and control of cell growth
    • Thomas G., Hall M.N. TOR signalling and control of cell growth. Curr. Opin. Cell Biol. 9:1997;782-787.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 782-787
    • Thomas, G.1    Hall, M.N.2
  • 84
    • 0034950742 scopus 로고    scopus 로고
    • Structure-function relationships of the liver and muscle isoforms of carnitine palmitoyltransferase I
    • Zammit V.A., Price N.T., Fraser F., Jackson V.N. Structure-function relationships of the liver and muscle isoforms of carnitine palmitoyltransferase I. Biochem. Soc. Trans. 29:2001;287-292.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 287-292
    • Zammit, V.A.1    Price, N.T.2    Fraser, F.3    Jackson, V.N.4
  • 85
    • 0028979464 scopus 로고
    • Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester
    • Zhang G., Kazanietz M.G., Blumberg P.M., Hurley J.H. Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester. Cell. 81:1995;917-924.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 86
    • 0018056906 scopus 로고
    • ACTH-induced inhibition of endogenous rat brain protein phosphorylation in vitro: Structure activity
    • Zwiers H., Wiegant V.M., Schotman P., Gispen W.H. ACTH-induced inhibition of endogenous rat brain protein phosphorylation in vitro: structure activity. Neurochem. Res. 3:1978;455-463.
    • (1978) Neurochem. Res. , vol.3 , pp. 455-463
    • Zwiers, H.1    Wiegant, V.M.2    Schotman, P.3    Gispen, W.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.