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Volumn 409, Issue 1, 2008, Pages 95-106

Phorbol ester and hydrogen peroxide synergistically induce the interaction of diacylglycerol kinase γ with the Src homology 2 and C1 domains of β2-chimaerin

Author keywords

GTPase activating protein; Phorbol myristate acetate (PMA); Rac; Src homology 2 domain (SH2 domain); Translocation; Zinc finger structures

Indexed keywords

GTPASE-ACTIVATING PROTEIN; PHORBOL MYRISTATE ACETATE (PMA); PHOSPHOTYROSINE; PROTEIN-PROTEIN INTERACTION; TRANSLOCATION; ZINC-FINGER STRUCTURES;

EID: 38149086943     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070848     Document Type: Article
Times cited : (8)

References (52)
  • 2
    • 33144458615 scopus 로고    scopus 로고
    • Signaling roles of diacylglycerol kinases
    • Topham, M. K. (2006) Signaling roles of diacylglycerol kinases. J. Cell. Biochem. 97, 474-484
    • (2006) J. Cell. Biochem , vol.97 , pp. 474-484
    • Topham, M.K.1
  • 3
    • 0033749209 scopus 로고    scopus 로고
    • Properties and functions of diacylglycerol kinases
    • van Blitterswijk, W. J. and Houssa, B. (2000) Properties and functions of diacylglycerol kinases. Cell. Signalling 12, 595-605
    • (2000) Cell. Signalling , vol.12 , pp. 595-605
    • van Blitterswijk, W.J.1    Houssa, B.2
  • 4
    • 0032775007 scopus 로고    scopus 로고
    • Regulation of phospholipase D
    • Exton, J. H. (1999)Regulation of phospholipase D. Biochim. Biophys. Acta 1439, 121-133
    • (1999) Biochim. Biophys. Acta , vol.1439 , pp. 121-133
    • Exton, J.H.1
  • 6
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y. (1992) Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science. 258, 607-614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 7
    • 0036209077 scopus 로고    scopus 로고
    • Novel "nonkinase" phorbol ester receptors: The C1 domain connection
    • Kazanietz, M. G. (2002) Novel "nonkinase" phorbol ester receptors: the C1 domain connection. Mol. Pharmacol. 61, 759-767
    • (2002) Mol. Pharmacol , vol.61 , pp. 759-767
    • Kazanietz, M.G.1
  • 8
    • 0027258578 scopus 로고
    • A novel functional target for tumor-promoting phorbol esters and lysophosphatidic acid. The p21rac-GTPase activating protein n-chimaerin
    • Ahmed, S., Lee, J., Kozma, R., Best, A., Monfries, C. and Lim, L. (1993) A novel functional target for tumor-promoting phorbol esters and lysophosphatidic acid. The p21rac-GTPase activating protein n-chimaerin. J. Biol. Chem. 268, 10709-10712
    • (1993) J. Biol. Chem , vol.268 , pp. 10709-10712
    • Ahmed, S.1    Lee, J.2    Kozma, R.3    Best, A.4    Monfries, C.5    Lim, L.6
  • 9
    • 0142169536 scopus 로고    scopus 로고
    • Characterization of the Rac-GAP (Rac-GTPase-activating protein) activity of β2-chimaerin, a 'non-protein kinase C' phorbol ester receptor
    • Caloca, M. J., Wang, H. and Kazanietz, M. G. (2003) Characterization of the Rac-GAP (Rac-GTPase-activating protein) activity of β2-chimaerin, a 'non-protein kinase C' phorbol ester receptor. Biochem. J. 375, 313-321
    • (2003) Biochem. J , vol.375 , pp. 313-321
    • Caloca, M.J.1    Wang, H.2    Kazanietz, M.G.3
  • 10
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science. 279, 509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 11
    • 0032437666 scopus 로고    scopus 로고
    • Signaling to the actin cytoskeleton
    • Schmidt, A. and Hall, M. N. (1998) Signaling to the actin cytoskeleton. Annu. Rev. Cell Dev. Biol. 14, 305-338
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 305-338
    • Schmidt, A.1    Hall, M.N.2
  • 13
    • 33646788066 scopus 로고    scopus 로고
    • Phospholipase Cγ/diacylglycerol-dependent activation of β2-chimaerin restricts EGF-induced Rac signaling
    • Wang, H., Yang, C., Leskow, F. C., Sun, J., Canagarajah, B., Hurley, J. H. and Kazanietz, M. G. (2006) Phospholipase Cγ/diacylglycerol-dependent activation of β2-chimaerin restricts EGF-induced Rac signaling. EMBO J. 25, 2062-2074
    • (2006) EMBO J , vol.25 , pp. 2062-2074
    • Wang, H.1    Yang, C.2    Leskow, F.C.3    Sun, J.4    Canagarajah, B.5    Hurley, J.H.6    Kazanietz, M.G.7
  • 14
    • 0027282112 scopus 로고
    • 2-Chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testes
    • 2-Chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testes. Mol. Cell. Biol. 13, 4986-4998
    • (1993) Mol. Cell. Biol , vol.13 , pp. 4986-4998
    • Hall, C.1    Sin, W.C.2    Teo, M.3    Michael, G.J.4    Smith, P.5    Dong, J.M.6    Lim, H.H.7    Manser, E.8    Spurr, N.K.9    Jones, T.A.10    Lim, L.11
  • 15
    • 0027456496 scopus 로고
    • Germ cell β-chimaerin, a new GTPase-activating protein for p21rac, is specifically expressed during the acrosomal assembly stage in rat testis
    • Leung, T., How, B. E., Manser, E. and Lim, L. (1993) Germ cell β-chimaerin, a new GTPase-activating protein for p21rac, is specifically expressed during the acrosomal assembly stage in rat testis. J. Biol. Chem. 268, 3813-3816
    • (1993) J. Biol. Chem , vol.268 , pp. 3813-3816
    • Leung, T.1    How, B.E.2    Manser, E.3    Lim, L.4
  • 16
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • Boggon, T. J. and Eck, M. J. (2004) Structure and regulation of Src family kinases. Oncogene. 23, 7918-7927
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 17
    • 3142616908 scopus 로고    scopus 로고
    • Diacylglycerol kinase γ serves as an upstream suppressor of Rad and lamellipodium formation
    • Tsushima, S., Kai, M., Yamada, K., Imai, S., Houkin, K., Kanoh, H. and Sakane, F. (2004) Diacylglycerol kinase γ serves as an upstream suppressor of Rad and lamellipodium formation. J. Biol. Chem. 279, 28603-28613
    • (2004) J. Biol. Chem , vol.279 , pp. 28603-28613
    • Tsushima, S.1    Kai, M.2    Yamada, K.3    Imai, S.4    Houkin, K.5    Kanoh, H.6    Sakane, F.7
  • 18
    • 33846444740 scopus 로고    scopus 로고
    • Diacylglycerol kinase γ interacts with and activates β2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor
    • Yasuda, S., Kai, M., Imai, S., Kanoh, H. and Sakane, F. (2007) Diacylglycerol kinase γ interacts with and activates β2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor. FEBS Lett. 581, 551-557
    • (2007) FEBS Lett , vol.581 , pp. 551-557
    • Yasuda, S.1    Kai, M.2    Imai, S.3    Kanoh, H.4    Sakane, F.5
  • 19
    • 0028275895 scopus 로고
    • Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells
    • Kai, M., Sakane, F., Imai, S., Wada, I. and Kanoh, H. (1994) Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells. J. Biol. Chem. 269, 18492-18498
    • (1994) J. Biol. Chem , vol.269 , pp. 18492-18498
    • Kai, M.1    Sakane, F.2    Imai, S.3    Wada, I.4    Kanoh, H.5
  • 21
  • 23
    • 5644276320 scopus 로고    scopus 로고
    • α2-Chimaerin, cyclin-dependent kinase 5/p35, and its target collapsin response mediator protein-2 are essential components in semaphorin 3A-induced growth-cone collapse
    • Brown, M., Jacobs, T., Eickholt, B., Ferrari, G., Teo, M., Monfries, C., Qi, R. Z., Leung, T., Lim, L. and Hall, C. (2004) α2-Chimaerin, cyclin-dependent kinase 5/p35, and its target collapsin response mediator protein-2 are essential components in semaphorin 3A-induced growth-cone collapse. J. Neurosci. 24, 8994-9004
    • (2004) J. Neurosci , vol.24 , pp. 8994-9004
    • Brown, M.1    Jacobs, T.2    Eickholt, B.3    Ferrari, G.4    Teo, M.5    Monfries, C.6    Qi, R.Z.7    Leung, T.8    Lim, L.9    Hall, C.10
  • 24
    • 0035878075 scopus 로고    scopus 로고
    • α2-Chimaerin, a Cdc42/Rac1 regulator, is selectively expressed in the rat embryonic nervous system and is involved in neurogenesis in N1E-115 neuroblastoma cells
    • Hall, C., Michael, G. J., Cann, N., Ferrari, G., Teo, M., Jacobs, T., Monfries, C. and Lim, L. (2001) α2-Chimaerin, a Cdc42/Rac1 regulator, is selectively expressed in the rat embryonic nervous system and is involved in neurogenesis in N1E-115 neuroblastoma cells. J. Neurosci. 21, 5191-5202
    • (2001) J. Neurosci , vol.21 , pp. 5191-5202
    • Hall, C.1    Michael, G.J.2    Cann, N.3    Ferrari, G.4    Teo, M.5    Jacobs, T.6    Monfries, C.7    Lim, L.8
  • 25
    • 33644546374 scopus 로고    scopus 로고
    • Uncoupling of the base excision and nucleotide incision repair pathways reveals their respective biological roles
    • Ishchenko, A. A., Deprez, E., Maksimenko, A., Brochon, J. C., Taue, P. and Saparbaev, M. K. (2006) Uncoupling of the base excision and nucleotide incision repair pathways reveals their respective biological roles. Proc. Natl. Acad. Sci. U.S.A. 103, 2564-2569
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 2564-2569
    • Ishchenko, A.A.1    Deprez, E.2    Maksimenko, A.3    Brochon, J.C.4    Taue, P.5    Saparbaev, M.K.6
  • 26
    • 0034637434 scopus 로고    scopus 로고
    • Subtype-specific translocation of diacylglycerol kinase α and γ and its correlation with protein kinase C.J
    • Shirai, Y., Segawa, S., Kuriyama, M., Goto, K., Sakai, N. and Saito, N. (2000) Subtype-specific translocation of diacylglycerol kinase α and γ and its correlation with protein kinase C.J. Biol. Chem. 275, 24760-24766.
    • (2000) 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
  • 27
    • 0035947687 scopus 로고    scopus 로고
    • Phorbol esters and related analogs regulate the subcellular localization of β2-chimaerin, a non-protein kinase C phorbol ester receptor
    • Caloca, M. J., Wang, H., Delemos, A., Wang, S. and Kazanietz, M. G. (2001) Phorbol esters and related analogs regulate the subcellular localization of β2-chimaerin, a non-protein kinase C phorbol ester receptor. J. Biol. Chem. 276, 18303-18312
    • (2001) J. Biol. Chem , vol.276 , pp. 18303-18312
    • Caloca, M.J.1    Wang, H.2    Delemos, A.3    Wang, S.4    Kazanietz, M.G.5
  • 28
    • 28844495301 scopus 로고    scopus 로고
    • Identification and characterization of a novel human type II diacylglycerol kinase, DGKκ
    • Imai, S., Kai, M., Yasuda, S., Kanoh, H. and Sakane, F. (2005) Identification and characterization of a novel human type II diacylglycerol kinase, DGKκ. J. Biol. Chem. 280, 39870-39881
    • (2005) J. Biol. Chem , vol.280 , pp. 39870-39881
    • Imai, S.1    Kai, M.2    Yasuda, S.3    Kanoh, H.4    Sakane, F.5
  • 29
    • 0141445975 scopus 로고    scopus 로고
    • Identification and characterization of two splice variants of human diacylglycerol kinase η
    • Murakami, T., Sakane, F. Imai, S. I., Houkin, K. and Kanoh, H. (2003) Identification and characterization of two splice variants of human diacylglycerol kinase η. J. Biol. Chem. 278, 34364-34372
    • (2003) J. Biol. Chem , vol.278 , pp. 34364-34372
    • Murakami, T.1    Sakane, F.2    Imai, S.I.3    Houkin, K.4    Kanoh, H.5
  • 30
    • 34548506571 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of β2-chimaerin by Src-family kinase negatively regulates its Rac-specific GAP activity
    • Kai, M., Yasuda, S., Imai, S., Kanoh, H. and Sakane, F. (2007) Tyrosine phosphorylation of β2-chimaerin by Src-family kinase negatively regulates its Rac-specific GAP activity. Biochim. Biophys. Acta 1773, 1407-1415
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1407-1415
    • Kai, M.1    Yasuda, S.2    Imai, S.3    Kanoh, H.4    Sakane, F.5
  • 31
    • 0028180706 scopus 로고
    • Cerebellar β2-chimaerin, a GTPase-activating protein for p21 ras-related rac is specifically expressed in granule cells and has a unigue N-terminal SH2 domain
    • Leung, T., How, B. E., Manser, E. and Lim, L. (1994) Cerebellar β2-chimaerin, a GTPase-activating protein for p21 ras-related rac is specifically expressed in granule cells and has a unigue N-terminal SH2 domain. J. Biol. Chem. 269, 12888-12892
    • (1994) J. Biol. Chem , vol.269 , pp. 12888-12892
    • Leung, T.1    How, B.E.2    Manser, E.3    Lim, L.4
  • 32
    • 0026672312 scopus 로고
    • Developmental regulation and neuronal expression of the mRNA of rat n-chimaerin, a p21rac GAP:cDNA sequence
    • Lim, H. H., Michael, G. J., Smith, P., Lim, L. and Hall, C. (1992) Developmental regulation and neuronal expression of the mRNA of rat n-chimaerin, a p21rac GAP:cDNA sequence. Biochem. J. 287, 415-422
    • (1992) Biochem. J , vol.287 , pp. 415-422
    • Lim, H.H.1    Michael, G.J.2    Smith, P.3    Lim, L.4    Hall, C.5
  • 33
    • 0029133178 scopus 로고
    • Identification and characterization of human β2-chimaerin: Association with malignant transformation in astrocytoma
    • Yuan, S., Miller, D. W., Barnett, G. H., Hahn, J. F. and Williams, B. R. (1995) Identification and characterization of human β2-chimaerin: association with malignant transformation in astrocytoma. Cancer Res. 55, 3456-3461
    • (1995) Cancer Res , vol.55 , pp. 3456-3461
    • Yuan, S.1    Miller, D.W.2    Barnett, G.H.3    Hahn, J.F.4    Williams, B.R.5
  • 34
    • 0037413711 scopus 로고    scopus 로고
    • Protein kinase D mediates a stress-induced NF-κB activation and survival pathway
    • Storz, P. and Toker, A. (2003) Protein kinase D mediates a stress-induced NF-κB activation and survival pathway. EMBO J. 22, 109-120
    • (2003) EMBO J , vol.22 , pp. 109-120
    • Storz, P.1    Toker, A.2
  • 35
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • Korichneva, I., Hoyos, B., Chua, R., Levi, E. and Hammerling, U. (2002) Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen. J. Biol. Chem. 277, 44327-44331
    • (2002) J. Biol. Chem , vol.277 , pp. 44327-44331
    • Korichneva, I.1    Hoyos, B.2    Chua, R.3    Levi, E.4    Hammerling, U.5
  • 36
    • 0034604723 scopus 로고    scopus 로고
    • Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content
    • Knapp, L. T. and Klann, E. (2000) Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content. J. Biol. Chem. 275, 24136-24145
    • (2000) J. Biol. Chem , vol.275 , pp. 24136-24145
    • Knapp, L.T.1    Klann, E.2
  • 37
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D. and Kuriyan, J. (1993) Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell. 72, 779-790
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 38
    • 33846331650 scopus 로고    scopus 로고
    • Oxidative stress and cancer: Have we moved forward?
    • Halliwell, B. (2007) Oxidative stress and cancer: have we moved forward? Biochem. J. 401, 1-11
    • (2007) Biochem. J , vol.401 , pp. 1-11
    • Halliwell, B.1
  • 39
    • 0026094301 scopus 로고
    • Tumor necrosis factor induces rapid production of 1′,2′- diacylglycerol by a phosphatidylcholine-specific phospholipase C
    • Schutze, S., Berkovic, D., Tomsing, O., Unger, C. and Kronke, M. (1991) Tumor necrosis factor induces rapid production of 1′,2′- diacylglycerol by a phosphatidylcholine-specific phospholipase C. J. Exp. Med. 174, 975-988
    • (1991) J. Exp. Med , vol.174 , pp. 975-988
    • Schutze, S.1    Berkovic, D.2    Tomsing, O.3    Unger, C.4    Kronke, M.5
  • 40
    • 0030801591 scopus 로고    scopus 로고
    • Involvement of diacylglycerol production in activation of nuclear factor κB by a CD14-mediated lipopolysaccharide stimulus
    • Yamamoto, H., Hanada, K. and Nishijima, M. (1997) Involvement of diacylglycerol production in activation of nuclear factor κB by a CD14-mediated lipopolysaccharide stimulus. Biochem. J. 325, 223-228
    • (1997) Biochem. J , vol.325 , pp. 223-228
    • Yamamoto, H.1    Hanada, K.2    Nishijima, M.3
  • 41
    • 0033597338 scopus 로고    scopus 로고
    • Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions
    • Topham, M. K. and 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
  • 42
    • 0035976766 scopus 로고    scopus 로고
    • Diacylglycerol kinase γ is one of the specific receptors of tumor-promoting phorbol esters
    • Shindo, M., Irie, K., Ohigashi, H., Kuriyama, M. and Saito, N. (2001) Diacylglycerol kinase γ is one of the specific receptors of tumor-promoting phorbol esters. Biochem. Biophys. Res. Commun. 289, 451-456.
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 451-456
    • Shindo, M.1    Irie, K.2    Ohigashi, H.3    Kuriyama, M.4    Saito, N.5
  • 43
    • 0029792364 scopus 로고    scopus 로고
    • The C-terminal part of diacylglycerol kinase α lacking zinc fingers serves as a catalytic domain
    • Sakane, F., Kai, M., Wada, I., Imai, S. and Kanoh, H. (1996) The C-terminal part of diacylglycerol kinase α lacking zinc fingers serves as a catalytic domain. Biochem. J. 318, 583-590
    • (1996) Biochem. J , vol.318 , pp. 583-590
    • Sakane, F.1    Kai, M.2    Wada, I.3    Imai, S.4    Kanoh, H.5
  • 44
    • 0037040248 scopus 로고    scopus 로고
    • Chimaerins, novel non-protein kinase C phorbol ester receptors, associate with Tmp21-I (p23): Evidence for a novel anchoring mechanism involving the chimaerin C1 domain
    • Wang, H. and Kazanietz, M. G. (2002) Chimaerins, novel non-protein kinase C phorbol ester receptors, associate with Tmp21-I (p23): evidence for a novel anchoring mechanism involving the chimaerin C1 domain. J. Biol. Chem. 277, 4541-4550
    • (2002) J. Biol. Chem , vol.277 , pp. 4541-4550
    • Wang, H.1    Kazanietz, M.G.2
  • 45
    • 33750211862 scopus 로고    scopus 로고
    • PSD-95 is a negative regulator of the tyrosine kinase Src in the NMDA receptor complex
    • Kalia, L. V., Pitcher, G. M., Pelkey, K. A. and Salter, M. W. (2006) PSD-95 is a negative regulator of the tyrosine kinase Src in the NMDA receptor complex. EMBO J. 25, 4971-4982
    • (2006) EMBO J , vol.25 , pp. 4971-4982
    • Kalia, L.V.1    Pitcher, G.M.2    Pelkey, K.A.3    Salter, M.W.4
  • 46
    • 33846010146 scopus 로고    scopus 로고
    • The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1
    • Liao, Y. C., Si, L., Devere White, R. W. and Lo, S. H. (2007) The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1. J. Cell Biol. 176, 43-49
    • (2007) J. Cell Biol , vol.176 , pp. 43-49
    • Liao, Y.C.1    Si, L.2    Devere White, R.W.3    Lo, S.H.4
  • 47
    • 0037451177 scopus 로고    scopus 로고
    • Association of diacylglycerol kinase ζ with protein kinase C α: Spatial regulation of diacylglycerol signaling
    • Luo, B., Prescott, S. M. and Topham, M. K. (2003) Association of diacylglycerol kinase ζ with protein kinase C α: spatial regulation of diacylglycerol signaling. J. Cell Biol. 160, 929-937
    • (2003) J. Cell Biol , vol.160 , pp. 929-937
    • Luo, B.1    Prescott, S.M.2    Topham, M.K.3
  • 48
    • 0035911971 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ regulates Ras activation by a novel mechanism
    • Topham, M. K. and Prescott, S. M. (2001) Diacylglycerol kinase ζ regulates Ras activation by a novel mechanism. J. Cell Biol. 152, 1135-1144.
    • (2001) J. Cell Biol , vol.152 , pp. 1135-1144
    • Topham, M.K.1    Prescott, S.M.2
  • 50
    • 0033546314 scopus 로고    scopus 로고
    • Interleukin-2 causes an increase in saturated/monounsaturated phosphatidic acid derived from 1,2-diacylglycerol and 1-O-alkyl-2- acylglycerol
    • Jones, D. R., Pettitt, T. R., Sanjuan, M. A., Merida, I. and Wakelam, M. J. (1999) Interleukin-2 causes an increase in saturated/monounsaturated phosphatidic acid derived from 1,2-diacylglycerol and 1-O-alkyl-2- acylglycerol. J. Biol. Chem. 274, 16846-16852
    • (1999) J. Biol. Chem , vol.274 , pp. 16846-16852
    • Jones, D.R.1    Pettitt, T.R.2    Sanjuan, M.A.3    Merida, I.4    Wakelam, M.J.5
  • 51
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I. C., Tekle, E., Chock, P. B. and Rhee, S. G. (1997) Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272, 217-221
    • (1997) J. Biol. Chem , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 52
    • 0023927798 scopus 로고
    • Kinetic analysis of 1,2-diacylglycerol mass levels in cultured fibroblasts. Comparison of stimulation by α-thrombin and epidermal growth factor
    • Wright, T. M., Rangan, L. A., Shin, H. S. and Raben, D. M. (1988) Kinetic analysis of 1,2-diacylglycerol mass levels in cultured fibroblasts. Comparison of stimulation by α-thrombin and epidermal growth factor. J. Biol. Chem. 263, 9374-9380
    • (1988) J. Biol. Chem , vol.263 , pp. 9374-9380
    • Wright, T.M.1    Rangan, L.A.2    Shin, H.S.3    Raben, D.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.