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Volumn 18, Issue 7, 1998, Pages 3947-3955

14-3-3 facilitates Ras-dependent Raf-1 activation in vitro and in vivo

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0031862578     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.7.3947     Document Type: Article
Times cited : (118)

References (58)
  • 1
    • 0029943160 scopus 로고    scopus 로고
    • The activity of D-raf in torso signal transduction is altered by serine substitution, N-terminal deletion, and membrane targeting
    • Baek, K. H., J. R. Fabian, F. Sprenger, D. K. Morrison, and L. Ambrosio. 1996. The activity of D-raf in torso signal transduction is altered by serine substitution, N-terminal deletion, and membrane targeting. Dev. Biol. 175: 191-204
    • (1996) Dev. Biol. , vol.175 , pp. 191-204
    • Baek, K.H.1    Fabian, J.R.2    Sprenger, F.3    Morrison, D.K.4    Ambrosio, L.5
  • 3
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah, B. J., A. Khokhlatchev, M. H. Cobb, and E. J. Goldsmith. 1997. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90:859-869.
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 4
    • 0028057469 scopus 로고
    • Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells
    • Carroll, M. P., and W. S. May. 1994. Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells. J. Biol. Chem. 269:1249-1256.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1249-1256
    • Carroll, M.P.1    May, W.S.2
  • 5
    • 0030999664 scopus 로고    scopus 로고
    • 14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila
    • Chang, H. C., and G. M. Rubin. 1997. 14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila. Genes Dev. 11:1132-1139.
    • (1997) Genes Dev. , vol.11 , pp. 1132-1139
    • Chang, H.C.1    Rubin, G.M.2
  • 8
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • Fabian, J. R., I. O. Daar, and D. K. Morrison. 1993. Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol. Cell. Biol. 13:7170-7179.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 9
    • 0027184473 scopus 로고
    • Requirement for Raf and MAP kinase function during the meiotic maturation of Xenopus oocytes
    • Fabian, J. R., D. K. Morrison, and I. O. Daar. 1993. Requirement for Raf and MAP kinase function during the meiotic maturation of Xenopus oocytes. J. Cell Biol. 122:645-652.
    • (1993) J. Cell Biol. , vol.122 , pp. 645-652
    • Fabian, J.R.1    Morrison, D.K.2    Daar, I.O.3
  • 10
    • 0028341334 scopus 로고
    • A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function
    • Fabian, J. R., A. B. Vojtek, J. A. Cooper, and D. K. Morrison. 1994. A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function. Proc. Natl. Acad. Sci. USA 91:5982-5986.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5982-5986
    • Fabian, J.R.1    Vojtek, A.B.2    Cooper, J.A.3    Morrison, D.K.4
  • 12
    • 0029807304 scopus 로고    scopus 로고
    • Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
    • Farrar, M. A., I. Alberol, and R. M. Perlmutter. 1996. Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization. Nature 383:178-181.
    • (1996) Nature , vol.383 , pp. 178-181
    • Farrar, M.A.1    Alberol, I.2    Perlmutter, R.M.3
  • 13
    • 0031020427 scopus 로고    scopus 로고
    • Sequential modification of serines 621 and 624 in the Raf-1 carboxyl terminus produces alterations in its electrophoretic mobility
    • Ferrier A. F., M. Lee, W. B. Anderson, G. Benvenuto, D. K. Morrison, D. R. Lowy, and J. E. DeClue. 1997. Sequential modification of serines 621 and 624 in the Raf-1 carboxyl terminus produces alterations in its electrophoretic mobility. J. Biol. Chem. 272:2136-2142.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2136-2142
    • Ferrier, A.F.1    Lee, M.2    Anderson, W.B.3    Benvenuto, G.4    Morrison, D.K.5    Lowy, D.R.6    DeClue, J.E.7
  • 14
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed, E., M. Symons, S. G. Macdonald, F. McCormick, and R. Ruggieri. 1994. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265:1713-1716.
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    Macdonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 16
    • 0028073963 scopus 로고
    • Identification of discrete segments of human Raf-1 kinase critical for high affinity binding to Ha-Ras
    • Ghosh S., and R. M. Bell. 1994. Identification of discrete segments of human Raf-1 kinase critical for high affinity binding to Ha-Ras. J. Biol. Chem. 269:30785-30788.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30785-30788
    • Ghosh, S.1    Bell, R.M.2
  • 17
    • 0029935339 scopus 로고    scopus 로고
    • Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells
    • Ghosh, S., J. C. Strum, V. A. Sciorra, L. Daniel, and R. M. Bell. 1996. Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells. J. Biol. Chem. 271:8472-8480.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8472-8480
    • Ghosh, S.1    Strum, J.C.2    Sciorra, V.A.3    Daniel, L.4    Bell, R.M.5
  • 18
    • 0028083893 scopus 로고
    • The cysteine-rich region of Raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras
    • Ghosh, S., W. Q. Xie, A. F. Quest, G. M. Mabrouk, J. C. Strum, and R. M. Bell. 1994. The cysteine-rich region of Raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras. J. Biol. Chem. 269:10000-10007.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10000-10007
    • Ghosh, S.1    Xie, W.Q.2    Quest, A.F.3    Mabrouk, G.M.4    Strum, J.C.5    Bell, R.M.6
  • 19
    • 0027232261 scopus 로고
    • A novel role for RhoGDI as inhibitor of GAP proteins
    • Hancock, J. F., and A. Hall. 1993. A novel role for RhoGDI as inhibitor of GAP proteins. EMBO J. 12:1915-1921.
    • (1993) EMBO J. , vol.12 , pp. 1915-1921
    • Hancock, J.F.1    Hall, A.2
  • 20
    • 0029587739 scopus 로고
    • Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras
    • Hu, C. D., K. Kariya, M. Tamada, K. Akasaka, M. Shirouzu, S. Yokoyama, and T. Kataoka. 1995. Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras. J. Biol. Chem. 270:30274-30277.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30274-30277
    • Hu, C.D.1    Kariya, K.2    Tamada, M.3    Akasaka, K.4    Shirouzu, M.5    Yokoyama, S.6    Kataoka, T.7
  • 22
    • 0028051904 scopus 로고
    • Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase
    • Irie, K., Y. Gotoh, B. M. Yashar, B. Errede, E. Nishida, and K. Matsumoto. 1994. Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 265:1716-1719.
    • (1994) Science , vol.265 , pp. 1716-1719
    • Irie, K.1    Gotoh, Y.2    Yashar, B.M.3    Errede, B.4    Nishida, E.5    Matsumoto, K.6
  • 23
    • 0030029343 scopus 로고    scopus 로고
    • Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation
    • Jelinek, T., P. Dent, T. W. Sturgill, and M. J. Weber. 1996. Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation. Mol. Cell. Biol. 16:1027-1034.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1027-1034
    • Jelinek, T.1    Dent, P.2    Sturgill, T.W.3    Weber, M.J.4
  • 24
    • 0030953744 scopus 로고    scopus 로고
    • Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development
    • Kockel, L., G. Vorbruggen, H. Jackle, M. Mlodzik, and D. Bohmann. 1997. Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development. Genes Dev. 11:1140-1147.
    • (1997) Genes Dev. , vol.11 , pp. 1140-1147
    • Kockel, L.1    Vorbruggen, G.2    Jackle, H.3    Mlodzik, M.4    Bohmann, D.5
  • 25
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers, S. J., H. F. Paterson, and C. J. Marshall. 1994. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 369:411-414.
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 27
    • 0031024585 scopus 로고    scopus 로고
    • An intact zinc finger is required for optimal binding to processed Ras and for Ras-dependent Raf activation in situ
    • Luo, Z., B. Diaz, M. Marshall, and J. Avruch. 1997. An intact zinc finger is required for optimal binding to processed Ras and for Ras-dependent Raf activation in situ. Mol. Cell. Biol. 17:46-53.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 46-53
    • Luo, Z.1    Diaz, B.2    Marshall, M.3    Avruch, J.4
  • 28
    • 0029811985 scopus 로고    scopus 로고
    • Oligomerization activates c-Raf-1 through a Ras-dependent mechanism
    • Luo, Z., G. Tzivion, P. J. Belshaw, D. Vavvas, M. Marshall, and J. Avruch. 1996. Oligomerization activates c-Raf-1 through a Ras-dependent mechanism. Nature 383:181-185.
    • (1996) Nature , vol.383 , pp. 181-185
    • Luo, Z.1    Tzivion, G.2    Belshaw, P.J.3    Vavvas, D.4    Marshall, M.5    Avruch, J.6
  • 29
    • 0028842660 scopus 로고
    • Identification of the 14.3.3 zeta domains important for self-association and Raf binding
    • Luo, Z. J., X. F. Zhang, U. Rapp, and J. Avruch. 1995. Identification of the 14.3.3 zeta domains important for self-association and Raf binding. J. Biol. Chem. 270:23681-23687.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23681-23687
    • Luo, Z.J.1    Zhang, X.F.2    Rapp, U.3    Avruch, J.4
  • 30
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais, R., Y. Light, H. F. Paterson, and C. J. Marshall. 1995. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14:3136-3145.
    • (1995) EMBO J. , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Marshall, C.J.4
  • 31
    • 0031041171 scopus 로고    scopus 로고
    • Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic ras and tyrosine kinases
    • Marais, R., Y. Light, H. F. Paterson, C. S. Mason, and C. J. Marshall. 1997. Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic ras and tyrosine kinases. J. Biol. Chem. 272:4378-4383.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4378-4383
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Mason, C.S.4    Marshall, C.J.5
  • 32
    • 0029855237 scopus 로고    scopus 로고
    • Control of the ERK MAP kinase cascade by Ras and Raf
    • Marais, R., and C. J. Marshall. 1996. Control of the ERK MAP kinase cascade by Ras and Raf. Cancer Surv. 27:101-125.
    • (1996) Cancer Surv. , vol.27 , pp. 101-125
    • Marais, R.1    Marshall, C.J.2
  • 33
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 34
  • 36
    • 0029071689 scopus 로고
    • 14-3-3 is not essential for Raf-1 function: Identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner
    • Michaud, N. R., J. R. Fabian, K. D. Mathes, and D. K. Morrison. 1995. 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner. Mol. Cell. Biol. 15:3390-3397.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3390-3397
    • Michaud, N.R.1    Fabian, J.R.2    Mathes, K.D.3    Morrison, D.K.4
  • 37
    • 0030890762 scopus 로고    scopus 로고
    • Physical association with ras enhances activation of membrane-bound raf (RafCAAX)
    • Mineo, C., R. G. Anderson, and M. A. White. 1997. Physical association with ras enhances activation of membrane-bound raf (RafCAAX). J. Biol. Chem. 272:10345-10348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10345-10348
    • Mineo, C.1    Anderson, R.G.2    White, M.A.3
  • 40
    • 0027168907 scopus 로고
    • Identification of the major phosphorylation sites of the Raf-1 kinase
    • Morrison, D. K., G. Heidecker, U. R. Rapp, and T. D. Copeland. 1993. Identification of the major phosphorylation sites of the Raf-1 kinase. J. Biol. Chem. 268:17309-17316.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17309-17316
    • Morrison, D.K.1    Heidecker, G.2    Rapp, U.R.3    Copeland, T.D.4
  • 41
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., J. W. Tanner, P. M. Allen, and A. S. Shaw. 1996. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84:889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 42
    • 0345813949 scopus 로고    scopus 로고
    • Inhibition of Raf/MAPK signaling in Xenopus oocyte extracts by Raf-1-specific peptides
    • Radziwill, G., U. Steinhusen, A. Aitken, and K. Moelling. 1996. Inhibition of Raf/MAPK signaling in Xenopus oocyte extracts by Raf-1-specific peptides. Biochem. Biophys. Res. Commun. 227:20-26.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 20-26
    • Radziwill, G.1    Steinhusen, U.2    Aitken, A.3    Moelling, K.4
  • 44
    • 0030853961 scopus 로고    scopus 로고
    • Negative regulation of Raf activity by binding of 14-3-3 to the amino terminus of Raf in vivo
    • Rommel, C., G. Radziwill, K. Moelling, and E. Hafen. 1997. Negative regulation of Raf activity by binding of 14-3-3 to the amino terminus of Raf in vivo. Mech. Dev. 64:95-104.
    • (1997) Mech. Dev. , vol.64 , pp. 95-104
    • Rommel, C.1    Radziwill, G.2    Moelling, K.3    Hafen, E.4
  • 45
    • 0030854042 scopus 로고    scopus 로고
    • Activity of plasma membrane recruited Raf-1 is regulated by Ras via the Raf zinc finger
    • Roy, S., A. Lane, J. Yan, R. McPherson, and J. F. Hancock. 1997. Activity of plasma membrane recruited Raf-1 is regulated by Ras via the Raf zinc finger. J. Biol. Chem. 272:20139-20145.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20139-20145
    • Roy, S.1    Lane, A.2    Yan, J.3    McPherson, R.4    Hancock, J.F.5
  • 46
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe, D., S. G. Macdonald, K. Cadwallader, M. Symons, and J. F. Hancock. 1994. Activation of Raf as a result of recruitment to the plasma membrane. Science 264:1463-1467.
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallader, K.3    Symons, M.4    Hancock, J.F.5
  • 47
    • 0030919893 scopus 로고    scopus 로고
    • Activation of c-Raf-1 by Ras and Src through different mechanisms: Activation in vivo and in vitro
    • Stokoe, D., and F. McCormick. 1997. Activation of c-Raf-1 by Ras and Src through different mechanisms: activation in vivo and in vitro. EMBO J. 16:2384-2396.
    • (1997) EMBO J. , vol.16 , pp. 2384-2396
    • Stokoe, D.1    McCormick, F.2
  • 48
    • 0029113212 scopus 로고
    • Lack of evidence for the activation of the Ras/Raf mitogenic pathway by 14-3-3 proteins in mammalian cells
    • Suen, K. L., X. R. Bustelo, and M. Barbacid. 1995. Lack of evidence for the activation of the Ras/Raf mitogenic pathway by 14-3-3 proteins in mammalian cells. Oncogene 11:825-831.
    • (1995) Oncogene , vol.11 , pp. 825-831
    • Suen, K.L.1    Bustelo, X.R.2    Barbacid, M.3
  • 49
    • 0029850713 scopus 로고    scopus 로고
    • KSR modulates signal propagation within the MAPK cascade
    • Therrien, M., N. R. Michaud, G. M. Rubin, and D. K. Morrison. 1996. KSR modulates signal propagation within the MAPK cascade. Genes Dev. 10: 2684-2695.
    • (1996) Genes Dev. , vol.10 , pp. 2684-2695
    • Therrien, M.1    Michaud, N.R.2    Rubin, G.M.3    Morrison, D.K.4
  • 50
    • 0027527919 scopus 로고
    • Specific association of activated MAP kinase kinase kinase (Raf) with the plasma membranes of ras-transformed retinal cells
    • Traverse, S., P. Cohen, H. Paterson, C. Marshall, U. Rapp, and R. J. Grand. 1993. Specific association of activated MAP kinase kinase kinase (Raf) with the plasma membranes of ras-transformed retinal cells. Oncogene 8:3175-3181.
    • (1993) Oncogene , vol.8 , pp. 3175-3181
    • Traverse, S.1    Cohen, P.2    Paterson, H.3    Marshall, C.4    Rapp, U.5    Grand, R.J.6
  • 51
    • 0029789967 scopus 로고    scopus 로고
    • Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf
    • Ueda, Y., S. Hirai, S. Osada, A. Suzuki, K. Mizuno, and S. Ohno. 1996. Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf. J. Biol. Chem. 271:23512-23519.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23512-23519
    • Ueda, Y.1    Hirai, S.2    Osada, S.3    Suzuki, A.4    Mizuno, K.5    Ohno, S.6
  • 52
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 53
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne, P. H., P. R. Viciana, and J. Downward. 1993. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 364:352-355.
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Viciana, P.R.2    Downward, J.3
  • 54
    • 0028227245 scopus 로고
    • The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex
    • Wartmann, M., and R. J. Davis. 1994. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269:6695-6701.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6695-6701
    • Wartmann, M.1    Davis, R.J.2
  • 55
    • 0031054797 scopus 로고    scopus 로고
    • Negative modulation of membrane localization of the Raf-1 protein kinase by hyperphosphorylation
    • Wartmann, M., P. Hofer, P. Turowski, A. R. Saltiel, and N. E. Hynes. 1997. Negative modulation of membrane localization of the Raf-1 protein kinase by hyperphosphorylation. J. Biol. Chem. 272:3915-3923.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3915-3923
    • Wartmann, M.1    Hofer, P.2    Turowski, P.3    Saltiel, A.R.4    Hynes, N.E.5
  • 56
    • 0028838235 scopus 로고
    • Phosphorylation of Raf by ceramide-activated protein kinase
    • Yao, B., Y. Zhang, S. Delikat, S. Mathias, S. Basu, and R. Kolesnick. 1995. Phosphorylation of Raf by ceramide-activated protein kinase. Nature 378: 307-310.
    • (1995) Nature , vol.378 , pp. 307-310
    • Yao, B.1    Zhang, Y.2    Delikat, S.3    Mathias, S.4    Basu, S.5    Kolesnick, R.6
  • 57
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha, J., H. Harada, E. Yang, J. Jockel, and S. J. Korsmeyer. 1996. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87:619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5


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