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Volumn 10, Issue 3, 2005, Pages 225-239

Phosphorylation of PKC activation loop plays an important role in receptor-mediated translocation of PKC

Author keywords

[No Author keywords available]

Indexed keywords

3 PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; ADENOSINE TRIPHOSPHATE; ALANINE; CALCIUM ION; DIACYLGLYCEROL; GREEN FLUORESCENT PROTEIN; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN KINASE C DELTA; PROTEIN KINASE C GAMMA; PURINE P2Y RECEPTOR; THREONINE; UNCLASSIFIED DRUG;

EID: 15844395343     PISSN: 13569597     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2005.00830.x     Document Type: Article
Times cited : (30)

References (49)
  • 1
    • 85047681190 scopus 로고    scopus 로고
    • Discovery of PDK1, one of the missing links in insulin signal transduction. Colworth Medal Lecture
    • Alessi, D.R. (2001) Discovery of PDK1, one of the missing links in insulin signal transduction. Colworth Medal Lecture. Biochem. Soc. Trans. 29, 1-14.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 1-14
    • Alessi, D.R.1
  • 2
    • 0037799269 scopus 로고    scopus 로고
    • Protein kinase C isoform-specific differences in the spatial-temporal regulation and decoding of metabotropic glutamate receptor1a-stimulated second messenger responses
    • Babwah, A.V., Dale, L.B. & Ferguson, S.S. (2003) Protein kinase C isoform-specific differences in the spatial-temporal regulation and decoding of metabotropic glutamate receptor1a-stimulated second messenger responses. J. Biol. Chem. 278, 5419-5426.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5419-5426
    • Babwah, A.V.1    Dale, L.B.2    Ferguson, S.S.3
  • 3
    • 0034634443 scopus 로고    scopus 로고
    • Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms
    • Balendran, A., Hare, G.R., Kieloch, A., Williams, M.R. & Alessi, D.R. (2000) Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms. FEBS Lett. 484, 217-223.
    • (2000) FEBS Lett. , vol.484 , pp. 217-223
    • Balendran, A.1    Hare, G.R.2    Kieloch, A.3    Williams, M.R.4    Alessi, D.R.5
  • 4
    • 0033565608 scopus 로고    scopus 로고
    • The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation
    • Behn-Krappa, A. & Newton, A.C. (1999) The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation. Curr. Biol. 9, 728-737.
    • (1999) Curr. Biol. , vol.9 , pp. 728-737
    • Behn-Krappa, A.1    Newton, A.C.2
  • 5
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state
    • Bornancin, F. & Parker, P.J. (1997) Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state. J. Biol. Chem. 272, 3544-3549.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 6
    • 0028108027 scopus 로고
    • Threonine-497 is a critical site for permissive activation of protein kinase C alpha
    • Cazaubon, S., Bornancin, F. & Parker, P.J. (1994) Threonine-497 is a critical site for permissive activation of protein kinase C alpha. Biochem. J. 301, 443-448.
    • (1994) Biochem. J. , vol.301 , pp. 443-448
    • Cazaubon, S.1    Bornancin, F.2    Parker, P.J.3
  • 8
    • 0035943029 scopus 로고    scopus 로고
    • Control of astrocyte Ca(2+) oscillations and waves by oscillating translocation and activation of protein kinase C
    • Codazzi, F., Teruel, M.N. & Meyer, T. (2001) Control of astrocyte Ca(2+) oscillations and waves by oscillating translocation and activation of protein kinase C. Curr. Biol. 11, 1089-1097.
    • (2001) Curr. Biol. , vol.11 , pp. 1089-1097
    • Codazzi, F.1    Teruel, M.N.2    Meyer, T.3
  • 10
    • 0028062105 scopus 로고
    • In vivo regulation of protein kinase C by transphosphorylation followed by autophosphorylation
    • Dutil, E.M., Keranen, L.M., DePaoli-Roach, A.A. & Newton, A.C. (1994) In vivo regulation of protein kinase C by transphosphorylation followed by autophosphorylation. J. Biol. Chem. 269, 29359-29362.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29359-29362
    • Dutil, E.M.1    Keranen, L.M.2    DePaoli-Roach, A.A.3    Newton, A.C.4
  • 11
    • 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. (1998) Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1). Curr. Biol. 8, 1366-1375.
    • (1998) Curr. Biol. , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 12
    • 0033525860 scopus 로고    scopus 로고
    • Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C betaII
    • Edwards, A.S., Faux, M.C., Scott, J.D. & Newton, A.C. (1999) Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C betaII. J. Biol. Chem. 274, 6461-6468.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6461-6468
    • Edwards, A.S.1    Faux, M.C.2    Scott, J.D.3    Newton, A.C.4
  • 13
    • 0032500506 scopus 로고    scopus 로고
    • An essential role for autophosphorylation in the dissociation of activated protein kinase C from the plasma membrane
    • Feng, X. & Hannun, Y.A. (1998) An essential role for autophosphorylation in the dissociation of activated protein kinase C from the plasma membrane. J. Biol. Chem. 273, 26870-26874.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26870-26874
    • Feng, X.1    Hannun, Y.A.2
  • 14
    • 0032562752 scopus 로고    scopus 로고
    • Visualization of dynamic trafficking of a protein kinase C betaII/green fluorescent protein conjugate reveals differences in G protein-coupled receptor activation and desensitization
    • Feng, X., Zhang, J., Barak, L.S., Meyer, T., Caron, M.G. & Hannun, Y.A. (1998) Visualization of dynamic trafficking of a protein kinase C betaII/green fluorescent protein conjugate reveals differences in G protein-coupled receptor activation and desensitization. J. Biol. Chem. 273, 10755-10762.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10755-10762
    • Feng, X.1    Zhang, J.2    Barak, L.S.3    Meyer, T.4    Caron, M.G.5    Hannun, Y.A.6
  • 15
    • 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. (2000) Regulation of receptor-mediated protein kinase C membrane trafficking by autophosphorylation. J. Biol. Chem. 275 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
  • 16
    • 0035380478 scopus 로고    scopus 로고
    • The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1
    • Gao, T., Toker, A. & Newton, A.C. (2001) The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1. J. Biol. Chem. 276, 19588-19596.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19588-19596
    • Gao, T.1    Toker, A.2    Newton, A.C.3
  • 17
    • 0029761426 scopus 로고    scopus 로고
    • Replacement of Ser657 of protein kinase C-alpha by alanine leads to premature down regulation after phorbol-ester-induced translocation to the membrane
    • Gysin, S. & Imber, R. (1996) Replacement of Ser657 of protein kinase C-alpha by alanine leads to premature down regulation after phorbol-ester-induced translocation to the membrane. Eur. J. Biochem. 240, 747-750.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 747-750
    • Gysin, S.1    Imber, R.2
  • 18
    • 0030762437 scopus 로고    scopus 로고
    • The potential for isoenzyme-selective modulation of protein kinase C
    • Hofmann, J. (1997) The potential for isoenzyme-selective modulation of protein kinase C. FASEB J. 11, 649-669.
    • (1997) FASEB J. , vol.11 , pp. 649-669
    • Hofmann, J.1
  • 19
    • 0027501409 scopus 로고
    • Increases in intracellular calcium via activation of an endogenous P2-purinoceptor in cultured CHO-K1 cells
    • Iredale, P.A. & Hill, S.J. (1993) Increases in intracellular calcium via activation of an endogenous P2-purinoceptor in cultured CHO-K1 cells. Br. J. Pharmacol. 110, 1305-1310.
    • (1993) Br. J. Pharmacol. , vol.110 , pp. 1305-1310
    • Iredale, P.A.1    Hill, S.J.2
  • 20
    • 0034602168 scopus 로고    scopus 로고
    • A domain with homology to neuronal calcium sensors is required for calcium-dependent activation of diacylglycerol kinase alpha
    • Jiang, Y., Qian, W., Hawes, J.W. & Walsh, J.P. (2000) A domain with homology to neuronal calcium sensors is required for calcium-dependent activation of diacylglycerol kinase alpha. J. Biol. Chem. 275, 34092-34099.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34092-34099
    • Jiang, Y.1    Qian, W.2    Hawes, J.W.3    Walsh, J.P.4
  • 21
    • 0035131424 scopus 로고    scopus 로고
    • Subtype-specific translocation of the delta subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells
    • Kajimoto, T., Ohmori, S., Shirai, Y., Sakai, N. & Saito, N. (2001) Subtype-specific translocation of the delta subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells. Mol. Cell. Biol. 21, 1769-1783.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1769-1783
    • Kajimoto, T.1    Ohmori, S.2    Shirai, Y.3    Sakai, N.4    Saito, N.5
  • 22
    • 0036560847 scopus 로고    scopus 로고
    • Diacylglycerol kinases: Emerging downstream regulators in cell signalling systems
    • Kanoh, H., Yamada, K. & Sakane, F. (2002) Diacylglycerol kinases: Emerging downstream regulators in cell signalling systems. J. Biochem. (Tokyo) 131, 629-633.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 629-633
    • Kanoh, H.1    Yamada, K.2    Sakane, F.3
  • 23
    • 0037124093 scopus 로고    scopus 로고
    • Importance of C1B domain for lipid messenger-induced targeting of protein kinase C
    • Kashiwagi, K., Shirai, Y., Kuriyama, M., Sakai, N. & Saito, N. (2002) Importance of C1B domain for lipid messenger-induced targeting of protein kinase C. J. Biol. Chem. 277, 18037-18045.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18037-18045
    • Kashiwagi, K.1    Shirai, Y.2    Kuriyama, M.3    Sakai, N.4    Saito, N.5
  • 24
    • 0030611049 scopus 로고    scopus 로고
    • 2+ differentially regulates conventional protein kinase Cs' membrane interaction and activation
    • 2+ 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
  • 25
    • 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. (1998) Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 281, 2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 26
    • 0037081849 scopus 로고    scopus 로고
    • Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction
    • Liu, Y., Graham, C., Li, A., Fisher, R.J. & Shaw, S. (2002) Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction. Biochem. J. 361, 255-265.
    • (2002) Biochem. J. , vol.361 , pp. 255-265
    • Liu, Y.1    Graham, C.2    Li, A.3    Fisher, R.J.4    Shaw, S.5
  • 27
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • Newton, A.C. (2003) Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm. Biochem. J. 370 361-371.
    • (2003) Biochem. J. , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 28
    • 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
  • 29
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka, Y. (1988) The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334, 661-665.
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 30
    • 0031865214 scopus 로고    scopus 로고
    • Three distinct mechanisms for translocation and activation of the delta subspecies of protein kinase C
    • Ohmori, S., Shirai, Y., Sakai, N., et al. (1998) Three distinct mechanisms for translocation and activation of the delta subspecies of protein kinase C. Mol. Cell. Biol. 18, 5263-5271.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5263-5271
    • Ohmori, S.1    Shirai, Y.2    Sakai, N.3
  • 31
    • 0034713935 scopus 로고    scopus 로고
    • Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate
    • Ohmori, S., Sakai, N., Shirai, Y., et al. (2000) Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate. J. Biol. Chem. 275, 26449-26457.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26449-26457
    • Ohmori, S.1    Sakai, N.2    Shirai, Y.3
  • 32
    • 0023891959 scopus 로고
    • Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat brain protein kinase C
    • Ono, Y., Fujii, T., Igarashi, K., Kikkawa, U., Ogita, K. & Nishizuka, Y. (1988) Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat brain protein kinase C. Nucleic Acids Res. 16 5199-5200.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5199-5200
    • Ono, Y.1    Fujii, T.2    Igarashi, K.3    Kikkawa, U.4    Ogita, K.5    Nishizuka, Y.6
  • 33
    • 0027999633 scopus 로고
    • Requirement for negative charge on 'activation loop' of protein kinase C
    • Orr, J.W. & Newton, A.C. (1994) Requirement for negative charge on 'activation loop' of protein kinase C. J. Biol. Chem. 269, 27715-27718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27715-27718
    • Orr, J.W.1    Newton, A.C.2
  • 34
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh, D.B., Ziegler, W. & Parker, P.J. (2000) Multiple pathways control protein kinase C phosphorylation. EMBO J. 19 496-503.
    • (2000) EMBO J. , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 35
    • 0031466995 scopus 로고    scopus 로고
    • Direct visualization of the translocation of the gamma-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein
    • Sakai, N., Sasaki, K., Ikegaki, N., Shirai, Y. Ono, Y.& Saito, N. (1997) Direct visualization of the translocation of the gamma-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein. J. Cell Biol. 139, 1465-1476.
    • (1997) J. Cell Biol. , vol.139 , pp. 1465-1476
    • Sakai, N.1    Sasaki, K.2    Ikegaki, N.3    Shirai, Y.4    Ono, Y.5    Saito, N.6
  • 36
    • 0026320268 scopus 로고
    • The regulatory role of EF-hand motifs of pig 80K diacylglycerol kinase as assessed using truncation and deletion mutants
    • Sakane, E., Imai, S., Yamada, K. & Kanoh, H. (1991) The regulatory role of EF-hand motifs of pig 80K diacylglycerol kinase as assessed using truncation and deletion mutants. Biochem. Biophys. Res. Commun. 181, 1015-1021.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 1015-1021
    • Sakane, E.1    Imai, S.2    Yamada, K.3    Kanoh, H.4
  • 37
    • 0032547808 scopus 로고    scopus 로고
    • Distinct effects of fatty acids on translocation of gamma- and epsilon-subspecies of protein kinase C
    • Shirai, Y., Kashiwagi, K., Yagi, K., Sakai, N. & Saito, N. (1998a) Distinct effects of fatty acids on translocation of gamma- and epsilon-subspecies of protein kinase C. J. Cell Biol. 143, 511-521.
    • (1998) J. Cell Biol. , vol.143 , pp. 511-521
    • Shirai, Y.1    Kashiwagi, K.2    Yagi, K.3    Sakai, N.4    Saito, N.5
  • 38
    • 0032435504 scopus 로고    scopus 로고
    • Subspecies-specific targeting mechanism of protein kinase C
    • Shirai, Y., Sakai, N. & Saito, N. (1998b) Subspecies-specific targeting mechanism of protein kinase C. Jpn. J. Pharmacol. 78 411-417.
    • (1998) Jpn. J. Pharmacol. , vol.78 , pp. 411-417
    • Shirai, Y.1    Sakai, N.2    Saito, N.3
  • 39
    • 0034054688 scopus 로고    scopus 로고
    • Phospholipase A (2) and its products are involved in the purinergic receptor-mediated translocation of protein kinase C in CHO-K1 cells
    • Shirai, Y., Kashiwagi, K., Sakai, N. & Saito, N. (2000a) Phospholipase A (2) and its products are involved in the purinergic receptor-mediated translocation of protein kinase C in CHO-K1 cells. J. Cell Sci. 113, 1335-1343.
    • (2000) J. Cell Sci. , vol.113 , pp. 1335-1343
    • Shirai, Y.1    Kashiwagi, K.2    Sakai, N.3    Saito, N.4
  • 40
    • 0034637434 scopus 로고    scopus 로고
    • Subtype-specific translocation of diacylglycerol kinase alpha and gamma and its correlation with protein kinase C
    • Shirai, Y., Segawa, S., Kuriyama, M., Goto, K., Sakai, N. & Saito, N. (2000b) Subtype-specific translocation of diacylglycerol kinase alpha and gamma and its correlation with protein kinase C. J. Biol. Chem. 275, 24760-24766.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24760-24766
    • Shirai, Y.1    Segawa, S.2    Kuriyama, M.3    Goto, K.4    Sakai, N.5    Saito, N.6
  • 41
    • 0035976977 scopus 로고    scopus 로고
    • The phosphoinositide-dependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase
    • Sonnenburg, E.D., Gao, T. & Newton, A.C. (2001) The phosphoinositide-dependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase. J. Biol. Chem. 276, 45289-45297.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45289-45297
    • Sonnenburg, E.D.1    Gao, T.2    Newton, A.C.3
  • 42
    • 0030894024 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase Cdelta (PKCdelta) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCdelta and an alanine 505 mutant in bacteria in a functional form
    • Stempka, L., Girod, A., Muller, H.J., et al. (1997) Phosphorylation of protein kinase Cdelta (PKCdelta) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCdelta and an alanine 505 mutant in bacteria in a functional form. J. Biol. Chem. 272, 6805-6811.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6805-6811
    • Stempka, L.1    Girod, A.2    Muller, H.J.3
  • 43
    • 0344141205 scopus 로고    scopus 로고
    • Requirements of protein kinase cdelta for catalytic function. Role of glutamic acid 500 and autophosphorylation on serine 643
    • Stempka, L., Schnolzer, M., Radke, S., Rincke, G., Marks, F. & Gschwendt, M. (1999) Requirements of protein kinase cdelta for catalytic function. Role of glutamic acid 500 and autophosphorylation on serine 643. J. Biol. Chem. 274, 8886-8892.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8886-8892
    • Stempka, L.1    Schnolzer, M.2    Radke, S.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6
  • 44
    • 0034644523 scopus 로고    scopus 로고
    • Cellular signaling: Pivoting around PDK-1
    • Toker, A. & Newton, A.C. (2000) Cellular signaling: Pivoting around PDK-1. Cell 103, 185-188.
    • (2000) Cell , vol.103 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 45
    • 0033597338 scopus 로고    scopus 로고
    • Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions
    • Topham, M.K. & Prescott, S.M. (1999) Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions. J. Biol. Chem. 274, 11447-11450.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11447-11450
    • Topham, M.K.1    Prescott, S.M.2
  • 47
    • 0033601367 scopus 로고    scopus 로고
    • Differential localization of protein kinase C delta by phorbol esters and related compounds using a fusion protein with green fluorescent protein
    • Wang, Q.J., Bhattacharyya, D., Garfield, S., Nacro, K., Marquez, V.E. & Blumberg, P.M. (1999) Differential localization of protein kinase C delta by phorbol esters and related compounds using a fusion protein with green fluorescent protein. J. Biol. Chem. 274, 37233-37239.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37233-37239
    • Wang, Q.J.1    Bhattacharyya, D.2    Garfield, S.3    Nacro, K.4    Marquez, V.E.5    Blumberg, P.M.6
  • 48
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner, M.P., Costa, G.L., Schoettlin, W., Cline, J., Mathur, E. & Bauer, J.C. (1994) Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151, 119-123.
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 49


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