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Volumn 289, Issue 25, 2014, Pages 17812-17829

Conserved modular domains team up to latch-open active protein kinase Cα

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EID: 84903462238     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.534750     Document Type: Article
Times cited : (21)

References (64)
  • 3
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • DOI 10.1126/science.1083653
    • Pawson, T., and Nash, P. (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452 (Pubitemid 36444318)
    • (2003) Science , vol.300 , Issue.5618 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 4
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: The role of modular interactions in the evolution and wiring of cell signaling circuits
    • DOI 10.1146/annurev.biochem.75.103004.142710
    • Bhattacharyya, R. P., Reményi, A., Yeh, B. J., and Lim, W. A. (2006) Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu. Rev. Biochem. 75, 655-680 (Pubitemid 44118047)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 5
    • 84862221167 scopus 로고    scopus 로고
    • SMART7: Recent updates to the protein domain annotation resource
    • Letunic, I., Doerks, T., and Bork, P. (2012)SMART7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40, D302-D305
    • (2012) Nucleic Acids Res. , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 6
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg, S. F. (2008) Structural basis of protein kinase C isoform function. Physiol. Rev. 88, 1341-1378
    • (2008) Physiol. Rev. , vol.88 , pp. 1341-1378
    • Steinberg, S.F.1
  • 7
    • 34547907805 scopus 로고    scopus 로고
    • Expanding mTOR signaling
    • DOI 10.1038/cr.2007.64, PII CR200764
    • Yang, Q., and Guan, K. L. (2007) Expanding mTOR signaling. Cell Res. 17, 666-681 (Pubitemid 47255937)
    • (2007) Cell Research , vol.17 , Issue.8 , pp. 666-681
    • Yang, Q.1    Guan, K.-L.2
  • 8
    • 77957068247 scopus 로고    scopus 로고
    • Structure and function of regulator of G protein signaling homology domains
    • Tesmer, J. J. (2009) Structure and function of regulator of G protein signaling homology domains. Prog. Mol. Biol. Transl. Sci. 86, 75-113
    • (2009) Prog. Mol. Biol. Transl. Sci. , vol.86 , pp. 75-113
    • Tesmer, J.J.1
  • 9
    • 84876000745 scopus 로고    scopus 로고
    • Visualizing and manipulating focal adhesion kinase regulation in live cells
    • Ritt, M., Guan, J. L., and Sivaramakrishnan, S. (2013) Visualizing and manipulating focal adhesion kinase regulation in live cells. J. Biol. Chem. 288, 8875-8886
    • (2013) J. Biol. Chem. , vol.288 , pp. 8875-8886
    • Ritt, M.1    Guan, J.L.2    Sivaramakrishnan, S.3
  • 10
    • 84855513111 scopus 로고    scopus 로고
    • Systematic control of protein interaction using a modular ER/K α-helix linker
    • Sivaramakrishnan, S., and Spudich, J. A. (2011) Systematic control of protein interaction using a modular ER/K α-helix linker. Proc. Natl. Acad. Sci. U.S.A. 108, 20467-20472
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 20467-20472
    • Sivaramakrishnan, S.1    Spudich, J.A.2
  • 12
    • 35349021416 scopus 로고    scopus 로고
    • Identification of acidic amino acid residues in the protein kinase Cα V5 domain that contribute to its insensitivity to diacylglycerol
    • DOI 10.1074/jbc.M702248200
    • Stensman, H., and Larsson, C. (2007) Identification of acidic amino acid residues in the protein kinase C α V5 domain that contribute to its insensitivity to diacylglycerol. J. Biol. Chem. 282, 28627-28638 (Pubitemid 47606060)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.39 , pp. 28627-28638
    • Stensman, H.1    Larsson, C.2
  • 13
    • 84899011868 scopus 로고    scopus 로고
    • Single-molecule studies reveal a hidden key step in the activation mechanism of membrane-bound protein kinase Cα
    • Ziemba, B. P., Li, J., Landgraf, K. E., Knight, J. D., Voth, G. A., and Falke, J. J. (2014) Single-molecule studies reveal a hidden key step in the activation mechanism of membrane-bound protein kinase Cα. Biochemistry 53, 1697-1713
    • (2014) Biochemistry , vol.53 , pp. 1697-1713
    • Ziemba, B.P.1    Li, J.2    Landgraf, K.E.3    Knight, J.D.4    Voth, G.A.5    Falke, J.J.6
  • 15
  • 16
    • 72249096074 scopus 로고    scopus 로고
    • Combining single-molecule optical trapping and small-angle x-ray scattering measurements to compute the persistence length of a protein ER/K α-helix
    • Sivaramakrishnan, S., Sung, J., Ali, M., Doniach, S., Flyvbjerg, H., and Spudich, J. A. (2009) Combining single-molecule optical trapping and small-angle x-ray scattering measurements to compute the persistence length of a protein ER/K α-helix. Biophys. J. 97, 2993-2999
    • (2009) Biophys. J. , vol.97 , pp. 2993-2999
    • Sivaramakrishnan, S.1    Sung, J.2    Ali, M.3    Doniach, S.4    Flyvbjerg, H.5    Spudich, J.A.6
  • 17
    • 84879054442 scopus 로고    scopus 로고
    • Detection of G protein-selective G proteincoupled receptor (GPCR) conformations in live cells
    • Malik, R. U., Ritt, M., DeVree, B. T., Neubig, R. R., Sunahara, R. K., and Sivaramakrishnan, S. (2013) Detection of G protein-selective G proteincoupled receptor (GPCR) conformations in live cells. J. Biol. Chem. 288, 17167-17178
    • (2013) J. Biol. Chem. , vol.288 , pp. 17167-17178
    • Malik, R.U.1    Ritt, M.2    DeVree, B.T.3    Neubig, R.R.4    Sunahara, R.K.5    Sivaramakrishnan, S.6
  • 18
    • 78650942010 scopus 로고    scopus 로고
    • Crystal structure and allosteric activation of protein kinase CßII
    • Leonard, T. A., Ró¿zycki, B., Saidi, L. F., Hummer, G., and Hurley, J. H. (2011) Crystal structure and allosteric activation of protein kinase CßII. Cell 144, 55-66
    • (2011) Cell , vol.144 , pp. 55-66
    • Leonard, T.A.1    Rózycki, B.2    Saidi, L.F.3    Hummer, G.4    Hurley, J.H.5
  • 19
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • DOI 10.1083/jcb.200302125
    • Violin, J. D., Zhang, J., Tsien, R. Y., and Newton, A. C. (2003) A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. J. Cell Biol. 161, 899-909 (Pubitemid 36718423)
    • (2003) Journal of Cell Biology , vol.161 , Issue.5 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 20
    • 0033554389 scopus 로고    scopus 로고
    • Calcium and phosphatidylserine stimulate the self-association of conventional protein kinase C isoforms
    • Huang, S. M., Leventhal, P. S., Wiepz, G. J., and Bertics, P. J. (1999) Calcium and phosphatidylserine stimulate the self-association of conventional protein kinase C isoforms. Biochemistry 38, 12020-12027
    • (1999) Biochemistry , vol.38 , pp. 12020-12027
    • Huang, S.M.1    Leventhal, P.S.2    Wiepz, G.J.3    Bertics, P.J.4
  • 21
    • 1542652306 scopus 로고    scopus 로고
    • Measuring the binding of protein kinase C to sucrose-loaded vesicles
    • Giorgione, J., and Newton, A. C. (2003) Measuring the binding of protein kinase C to sucrose-loaded vesicles. Methods Mol. Biol. 233, 105-113
    • (2003) Methods Mol. Biol. , vol.233 , pp. 105-113
    • Giorgione, J.1    Newton, A.C.2
  • 22
    • 0041845195 scopus 로고    scopus 로고
    • Inhibition of protein kinase C catalytic activity by additional regions within the human protein kinase Cα-regulatory domain lying outside of the pseudosubstrate sequence
    • DOI 10.1042/BJ20030011
    • Kirwan, A. F., Bibby, A. C., Mvilongo, T., Riedel, H., Burke, T., Millis, S. Z., and Parissenti, A. M. (2003) Inhibition of protein kinaseCcatalytic activity by additional regions within the human protein kinase Cα-regulatory domain lying outside of the pseudosubstrate sequence. Biochem. J. 373, 571-581 (Pubitemid 36897859)
    • (2003) Biochemical Journal , vol.373 , Issue.2 , pp. 571-581
    • Kirwan, A.F.1    Bibby, A.C.2    Mvilongo, T.3    Riedel, H.4    Burke, T.5    Millis, S.Z.6    Parissenti, A.M.7
  • 23
    • 14844285356 scopus 로고    scopus 로고
    • Analysis by fluorescence resonance energy transfer of the interaction between ligands and protein kinase Cδ in the intact cell
    • DOI 10.1074/jbc.M413896200
    • Braun, D. C., Garfield, S. H., and Blumberg, P. M. (2005) Analysis by fluorescence resonance energy transfer of the interaction between ligands and protein kinase Cδ in the intact cell. J. Biol. Chem. 280, 8164-8171 (Pubitemid 40349717)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 8164-8171
    • Braun, D.C.1    Garfield, S.H.2    Blumberg, P.M.3
  • 24
    • 0017170344 scopus 로고
    • Fluorescence studies on the interaction of the tumor promoter phorbol myristate acetate and related compounds with rat liver plasma membranes
    • van Duuren, B. L., Banerjee, S., and Witz, G. (1976) Fluorescence studies on the interaction of the tumor promoter phorbol myristate acetate and related compounds with rat liver plasma membranes. Chem. Biol. Interact. 15, 233-246
    • (1976) Chem. Biol. Interact. , vol.15 , pp. 233-246
    • Van Duuren, B.L.1    Banerjee, S.2    Witz, G.3
  • 25
    • 0029904712 scopus 로고    scopus 로고
    • Formation of membrane domains during the activation of protein kinase C
    • DOI 10.1021/bi9610008
    • Yang, L., and Glaser, M. (1996) Formation of membrane domains during the activation of protein kinase C. Biochemistry 35, 13966-13974 (Pubitemid 26374468)
    • (1996) Biochemistry , vol.35 , Issue.44 , pp. 13966-13974
    • Yang, L.1    Glaser, M.2
  • 26
    • 84862000521 scopus 로고    scopus 로고
    • Regulation of protein kinase C-related protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain
    • Bauer, A. F., Sonzogni, S., Meyer, L., Zeuzem, S., Piiper, A., Biondi, R. M., and Neimanis, S. (2012) Regulation of protein kinase C-related protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain. J. Biol. Chem. 287, 20590-20602
    • (2012) J. Biol. Chem. , vol.287 , pp. 20590-20602
    • Bauer, A.F.1    Sonzogni, S.2    Meyer, L.3    Zeuzem, S.4    Piiper, A.5    Biondi, R.M.6    Neimanis, S.7
  • 27
    • 0023654062 scopus 로고
    • Domain structure and phosphorylation of protein kinase C
    • Mochly-Rosen, D., and Koshland, D. E., Jr. (1987) Domain structure and phosphorylation of protein kinase C. J. Biol. Chem. 262, 2291-2297
    • (1987) J. Biol. Chem. , vol.262 , pp. 2291-2297
    • Mochly-Rosen, D.1    Koshland Jr., D.E.2
  • 28
    • 0023920459 scopus 로고
    • Activation of protein kinase C by short chain phosphatidylcholines
    • Walker, J. M., and Sando, J. J. (1988) Activation of protein kinase C by short chain phosphatidylcholines. J. Biol. Chem. 263, 4537-4540
    • (1988) J. Biol. Chem. , vol.263 , pp. 4537-4540
    • Walker, J.M.1    Sando, J.J.2
  • 29
    • 0025004286 scopus 로고
    • Autophosphorylation of protein kinase C at three separated regions of its primary sequence
    • Flint, A. J., Paladini, R. D., and Koshland, D. E., Jr. (1990) Autophosphorylation of protein kinase C at three separated regions of its primary sequence. Science 249, 408-411 (Pubitemid 20248867)
    • (1990) Science , vol.249 , Issue.4967 , pp. 408-411
    • Flint, A.J.1    Paladini, R.D.2    Koshland Jr., D.E.3
  • 30
    • 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
  • 32
    • 0033815252 scopus 로고    scopus 로고
    • Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives
    • Ni, Q., Shaffer, J., and Adams, J. A. (2000) Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives. Protein Sci. 9, 1818-1827
    • (2000) Protein Sci. , vol.9 , pp. 1818-1827
    • Ni, Q.1    Shaffer, J.2    Adams, J.A.3
  • 33
    • 45549084379 scopus 로고    scopus 로고
    • Kinetic mechanism of fully activated S6K1 protein kinase
    • Keshwani, M. M., and Harris, T. K. (2008) Kinetic mechanism of fully activated S6K1 protein kinase. J. Biol. Chem. 283, 11972-11980
    • (2008) J. Biol. Chem. , vol.283 , pp. 11972-11980
    • Keshwani, M.M.1    Harris, T.K.2
  • 34
    • 0034161251 scopus 로고    scopus 로고
    • Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
    • Biondi, R. M., Cheung, P. C., Casamayor, A., Deak, M., Currie, R. A., and Alessi, D. R. (2000) Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA. EMBO J. 19, 979-988 (Pubitemid 30119823)
    • (2000) EMBO Journal , vol.19 , Issue.5 , pp. 979-988
    • Biondi, R.M.1    Cheung, P.C.F.2    Casamayor, A.3    Deak, M.4    Currie, R.A.5    Alessi, D.R.6
  • 36
    • 0037444771 scopus 로고    scopus 로고
    • 2+ and diacylglycerol
    • DOI 10.1042/BJ20021420
    • Raghunath, A., Ling, M., and Larsson, C. (2003) The catalytic domain limits the translocation of protein kinase C α in response to increases in Ca2+ and diacylglycerol. Biochem. J. 370, 901-912 (Pubitemid 36399082)
    • (2003) Biochemical Journal , vol.370 , Issue.3 , pp. 901-912
    • Raghunath, A.1    Ling, M.2    Larsson, C.3
  • 37
    • 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 (Pubitemid 28370527)
    • (1998) Journal of Cell Science , vol.111 , Issue.13 , pp. 1823-1830
    • Schmalz, D.1    Hucho, F.2    Buchner, K.3
  • 38
    • 0020326790 scopus 로고
    • Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters
    • Castagna, M., Takai, Y., Kaibuchi, K., Sano, K., Kikkawa, U., and Nishizuka, Y. (1982) Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters. J. Biol. Chem. 257, 7847-7851 (Pubitemid 12043279)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.13 , pp. 7847-7851
    • Castagna, M.1    Takai, Y.2    Kaibuchi, K.3
  • 39
    • 0024428410 scopus 로고
    • Lysophosphatidate-induced cell proliferation: Identification and dissection of signaling pathways mediated by G proteins
    • DOI 10.1016/0092-8674(89)90868-4
    • van Corven, E. J., Groenink, A., Jalink, K., Eichholtz, T., and Moolenaar, W. H. (1989) Lysophosphatidate-induced cell proliferation: identification and dissection of signaling pathways mediated by G proteins. Cell 59, 45-54 (Pubitemid 19248557)
    • (1989) Cell , vol.59 , Issue.1 , pp. 45-54
    • Van Corven, E.J.1    Groenink, A.2    Jalink, K.3    Eichholtz, T.4    Moolenaar, W.H.5
  • 40
    • 77953036199 scopus 로고    scopus 로고
    • Diversity of lysophosphatidic acid receptor-mediated intracellular calcium signaling in early cortical neurogenesis
    • Dubin, A. E., Herr, D. R., and Chun, J. (2010) Diversity of lysophosphatidic acid receptor-mediated intracellular calcium signaling in early cortical neurogenesis. J. Neurosci. 30, 7300-7309
    • (2010) J. Neurosci. , vol.30 , pp. 7300-7309
    • Dubin, A.E.1    Herr, D.R.2    Chun, J.3
  • 42
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubstrate prototope in its regulatory domain
    • House, C., and Kemp, B. E. (1987) Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science 238, 1726-1728 (Pubitemid 18046276)
    • (1987) Science , vol.238 , Issue.4834 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 44
    • 33644937697 scopus 로고    scopus 로고
    • Scanning mutagenesis studies reveal multiple distinct regions within the human protein kinase C α regulatory domain important for phorbol ester-dependent activation of the enzyme
    • Guo, B., Reed, K., and Parissenti, A. M. (2006) Scanning mutagenesis studies reveal multiple distinct regions within the human protein kinase C α regulatory domain important for phorbol ester-dependent activation of the enzyme. J. Mol. Biol. 357, 820-832
    • (2006) J. Mol. Biol. , vol.357 , pp. 820-832
    • Guo, B.1    Reed, K.2    Parissenti, A.M.3
  • 45
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state
    • DOI 10.1074/jbc.272.6.3544
    • Bornancin, F., and Parker, P. J. (1997) Phosphorylation of protein kinase Cα on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state. J. Biol. Chem. 272, 3544-3549 (Pubitemid 27066857)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 46
    • 4644326204 scopus 로고    scopus 로고
    • Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Cα in response to diacylglycerol
    • DOI 10.1074/jbc.M405560200
    • Stensman, H., Raghunath, A., and Larsson, C. (2004) Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Cα in response to diacylglycerol. J. Biol. Chem. 279, 40576-40583 (Pubitemid 39287649)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40576-40583
    • Stensman, H.1    Raghunath, A.2    Larsson, C.3
  • 48
    • 33751570046 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human protein kinase C β II complexed with a bisindolylmaleimide inhibitor
    • DOI 10.1021/bi061128h
    • Grodsky, N., Li, Y., Bouzida, D., Love, R., Jensen, J., Nodes, B., Nonomiya, J., and Grant, S. (2006) Structure of the catalytic domain of human protein kinase C βII complexed with a bisindolylmaleimide inhibitor. Biochemistry 45, 13970-13981 (Pubitemid 44846186)
    • (2006) Biochemistry , vol.45 , Issue.47 , pp. 13970-13981
    • Grodsky, N.1    Li, Y.2    Bouzida, D.3    Love, R.4    Jensen, J.5    Nodes, B.6    Nonomiya, J.7    Grant, S.8
  • 49
    • 0034616296 scopus 로고    scopus 로고
    • Dual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol
    • DOI 10.1074/jbc.275.14.10697
    • Dutil, E. M., and Newton, A. C. (2000) Dual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol. J. Biol. Chem. 275, 10697-10701 (Pubitemid 30202138)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10697-10701
    • Dutil, E.M.1    Newton, A.C.2
  • 50
    • 34248591612 scopus 로고    scopus 로고
    • Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
    • DOI 10.1038/sj.onc.1210422, PII 1210422
    • Roberts, P. J., and Der, C. J. (2007) Targeting the Raf-MEK-ERK mitogenactivated protein kinase cascade for the treatment of cancer. Oncogene 26, 3291-3310 (Pubitemid 46763022)
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3291-3310
    • Roberts, P.J.1    Der, C.J.2
  • 51
    • 67349125149 scopus 로고    scopus 로고
    • PKC maturation is promoted by nucleotide pocket occupation independently of intrinsic kinase activity
    • Cameron, A. J., Escribano, C., Saurin, A. T., Kostelecky, B., and Parker, P. J. (2009) PKC maturation is promoted by nucleotide pocket occupation independently of intrinsic kinase activity. Nat. Struct. Mol. Biol. 16, 624-630
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 624-630
    • Cameron, A.J.1    Escribano, C.2    Saurin, A.T.3    Kostelecky, B.4    Parker, P.J.5
  • 52
    • 80052801123 scopus 로고    scopus 로고
    • Protein kinase Cα as a heart failure therapeutic target
    • Liu, Q., and Molkentin, J. D. (2011) Protein kinase Cα as a heart failure therapeutic target. J. Mol. Cell. Cardiol 51, 474-478
    • (2011) J. Mol. Cell. Cardiol , vol.51 , pp. 474-478
    • Liu, Q.1    Molkentin, J.D.2
  • 53
    • 33846528583 scopus 로고    scopus 로고
    • PKC signaling deficits: A mechanistic hypothesis for the origins of Alzheimer's disease
    • DOI 10.1016/j.tips.2006.12.002, PII S0165614706002859
    • Alkon, D. L., Sun, M. K., and Nelson, T. J. (2007) PKC signaling deficits: a mechanistic hypothesis for the origins of Alzheimer's disease. Trends Pharmacol. Sci. 28, 51-60 (Pubitemid 46161834)
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.2 , pp. 51-60
    • Alkon, D.L.1    Sun, M.-K.2    Nelson, T.J.3
  • 54
    • 77952468064 scopus 로고    scopus 로고
    • Activation of protein kinaseCisoforms and its impact on diabetic complications
    • Geraldes, P., and King, G. L. (2010) Activation of protein kinaseCisoforms and its impact on diabetic complications. Circ. Res. 106, 1319-1331
    • (2010) Circ. Res. , vol.106 , pp. 1319-1331
    • Geraldes, P.1    King, G.L.2
  • 56
    • 34250757608 scopus 로고    scopus 로고
    • Insight into intra- and inter-molecular interactions of PKC: Design of specific modulators of kinase function
    • DOI 10.1016/j.phrs.2007.04.014, PII S1043661807000941
    • Kheifets, V., and Mochly-Rosen, D. (2007) Insight into intra- and intermolecular interactions of PKC: design of specific modulators of kinase function. Pharmacol. Res. 55, 467-476 (Pubitemid 46962313)
    • (2007) Pharmacological Research , vol.55 , Issue.6 , pp. 467-476
    • Kheifets, V.1    Mochly-Rosen, D.2
  • 57
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • DOI 10.1016/S0092-8674(00)81763-8
    • Oancea, E., and Meyer, T. (1998) Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 95, 307-318 (Pubitemid 28507320)
    • (1998) Cell , vol.95 , Issue.3 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 59
    • 0024457676 scopus 로고
    • The mechanism of protein kinase C activation
    • Huang, K. P. (1989) The mechanism of protein kinase C activation. Trends Neurosci. 12, 425-432
    • (1989) Trends Neurosci. , vol.12 , pp. 425-432
    • Huang, K.P.1
  • 61
    • 10644234702 scopus 로고    scopus 로고
    • New insights into the structure-function relationships of Rho-associated kinase: A thermodynamic and hydrodynamic study of the dimer-to-monomer transition and its kinetic implications
    • DOI 10.1042/BJ20040344
    • Doran, J. D., Liu, X., Taslimi, P., Saadat, A., and Fox, T. (2004) New insights into the structure-function relationships of Rho-associated kinase: a thermodynamic and hydrodynamic study of the dimer-to-monomer transition and its kinetic implications. Biochem. J. 384, 255-262 (Pubitemid 39656237)
    • (2004) Biochemical Journal , vol.384 , Issue.2 , pp. 255-262
    • Doran, J.D.1    Liu, X.2    Taslimi, P.3    Saadat, A.4    Fox, T.5
  • 64
    • 33644837834 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil
    • Yamaguchi, H., Kasa, M., Amano, M., Kaibuchi, K., and Hakoshima, T. (2006) Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil. Structure 14, 589-600
    • (2006) Structure , vol.14 , pp. 589-600
    • Yamaguchi, H.1    Kasa, M.2    Amano, M.3    Kaibuchi, K.4    Hakoshima, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.