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Volumn 19, Issue 6, 1999, Pages 4465-4479

Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN B; LEPTOMYCIN B; PROTEIN; PROTEIN 14 3 3; PROTEIN CDC25C; PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 0032974109     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.6.4465     Document Type: Article
Times cited : (244)

References (66)
  • 1
    • 0026562544 scopus 로고
    • DNA repair mutants defining G2 checkpoint pathways in Schizosaccharomyces pombe
    • Al-Khodairy, F., and A. M. Carr. 1992. DNA repair mutants defining G2 checkpoint pathways in Schizosaccharomyces pombe. EMBO J. 11:1343-1350.
    • (1992) EMBO J. , vol.11 , pp. 1343-1350
    • Al-Khodairy, F.1    Carr, A.M.2
  • 3
    • 0029031231 scopus 로고
    • The wee1 protein kinase regulates T14 phosphorylation of fission yeast cdc2
    • Den Haese, G. J., N. Walworth, A. M. Carr, and K. L. Gould. 1995. The wee1 protein kinase regulates T14 phosphorylation of fission yeast cdc2. Mol. Biol. Cell 6:371-385.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 371-385
    • Den Haese, G.J.1    Walworth, N.2    Carr, A.M.3    Gould, K.L.4
  • 4
    • 0025938467 scopus 로고
    • The cdc25 protein contains an intrinsic phosphatase activity
    • Dunphy, W. G., and A. Kumagai. 1991. The cdc25 protein contains an intrinsic phosphatase activity. Cell 67:189-196.
    • (1991) Cell , vol.67 , pp. 189-196
    • Dunphy, W.G.1    Kumagai, A.2
  • 5
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., G. K. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 6
    • 0024004720 scopus 로고
    • Purification of a RAS-responsive adenyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method
    • Field, J., J. I. Nikawa, D. Broek, B. MacDonald, L. Rodgers, I. A. Wilson, R. A. Lerner, and M. Wigler. 1988. Purification of a RAS-responsive adenyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method. Mol. Cell. Biol. 8:2159-2165.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2159-2165
    • Field, J.1    Nikawa, J.I.2    Broek, D.3    MacDonald, B.4    Rodgers, L.5    Wilson, I.A.6    Lerner, R.A.7    Wigler, M.8
  • 7
    • 0344384724 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U., J. Huber, W. C. Boelens, I. W. Mattaj, and R. Luhrmann. 1995. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 90:1051-1060.
    • (1995) Cell , vol.90 , pp. 1051-1060
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 9
    • 0030768948 scopus 로고    scopus 로고
    • Cdc25 mitotic inducer targeted by Chk1 DNA damage checkpoint kinase
    • Furnari, B., N. Rhind, and P. Russell. 1997. Cdc25 mitotic inducer targeted by Chk1 DNA damage checkpoint kinase. Science 277:1495-1497.
    • (1997) Science , vol.277 , pp. 1495-1497
    • Furnari, B.1    Rhind, N.2    Russell, P.3
  • 10
    • 0029937532 scopus 로고    scopus 로고
    • Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells
    • Gabrielli, B. G., C. P. C. DeSouza, I. D. Tonks, J. M. Clark, N. K. Hayward, and K. A. O. Ellem. 1996. Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells. J. Cell Sci. 109:1081-1093.
    • (1996) J. Cell Sci. , vol.109 , pp. 1081-1093
    • Gabrielli, B.G.1    Desouza, C.P.C.2    Tonks, I.D.3    Clark, J.M.4    Hayward, N.K.5    Ellem, K.A.O.6
  • 12
    • 0026709066 scopus 로고
    • Cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells
    • Girard, F., U. Strausfeld, J.-C. Cavadore, P. Russell, A. Fernandez, and N. J. C. Lamb. 1992. cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells. J. Cell Biol. 118:785-794.
    • (1992) J. Cell Biol. , vol.118 , pp. 785-794
    • Girard, F.1    Strausfeld, U.2    Cavadore, J.-C.3    Russell, P.4    Fernandez, A.5    Lamb, N.J.C.6
  • 13
  • 15
    • 0030022993 scopus 로고    scopus 로고
    • In vivo regulation of the early embryonic cell cycle in Xenopus
    • Hartley, R. S., R. E. Rempel, and J. L. Maller. 1996. In vivo regulation of the early embryonic cell cycle in Xenopus. Dev. Biol. 173:408-419.
    • (1996) Dev. Biol. , vol.173 , pp. 408-419
    • Hartley, R.S.1    Rempel, R.E.2    Maller, J.L.3
  • 16
    • 0027244234 scopus 로고
    • Human Wee1 maintains mitotic timing by protecting the nucleus from cytoplasmically activated cdc2 kinase
    • Heald, R., M. McLoughlin, and F. McKeon. 1993. Human Wee1 maintains mitotic timing by protecting the nucleus from cytoplasmically activated cdc2 kinase. Cell 74:463-474.
    • (1993) Cell , vol.74 , pp. 463-474
    • Heald, R.1    McLoughlin, M.2    McKeon, F.3
  • 17
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • Hendzel, M. J., Y. Wei, M. A. Mancini, A. V. Hooser, T. Ranalli, B. R. Brinkley, D. P. Bazett-Jones, and C. D. Allis. 1997. Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106:348-360.
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1    Wei, Y.2    Mancini, M.A.3    Hooser, A.V.4    Ranalli, T.5    Brinkley, B.R.6    Bazett-Jones, D.P.7    Allis, C.D.8
  • 19
    • 0027509501 scopus 로고
    • Phosphorylation and activation of human cdc25C by cdc2-cyclin B and its involvement in the self amplification of MPF at mitosis
    • Hoffmann, I., P. R. Clarke, M. J. Marcote, E. Karsenti, and G. Draetta. 1993. Phosphorylation and activation of human cdc25C by cdc2-cyclin B and its involvement in the self amplification of MPF at mitosis. EMBO J. 12:53-63.
    • (1993) EMBO J. , vol.12 , pp. 53-63
    • Hoffmann, I.1    Clarke, P.R.2    Marcote, M.J.3    Karsenti, E.4    Draetta, G.5
  • 20
    • 0028022034 scopus 로고
    • Activation of the phosphatase activity of human cdc25a by a cdk2-cyclin e dependent phosphorylation at the G1/S transition
    • Hoffmann, I., G. Draetta, and E. Karsenti. 1994. Activation of the phosphatase activity of human cdc25A by a cdk2-cyclin E dependent phosphorylation at the G1/S transition. EMBO J. 13:4302-4310.
    • (1994) EMBO J. , vol.13 , pp. 4302-4310
    • Hoffmann, I.1    Draetta, G.2    Karsenti, E.3
  • 22
    • 0027746003 scopus 로고
    • Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase
    • Izumi, T., and J. L. Maller. 1993. Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase. Mol. Biol. Cell 4:1337-1350.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1337-1350
    • Izumi, T.1    Maller, J.L.2
  • 23
    • 0029039470 scopus 로고
    • Phosphorylation and activation of the Xenopus cdc25 phosphatase in the absence of cdc2 and cdk2 kinase activity
    • Izumi, T., and J. L. Maller. 1995. Phosphorylation and activation of the Xenopus cdc25 phosphatase in the absence of cdc2 and cdk2 kinase activity. Mol. Biol. Cell 6:215-226.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 215-226
    • Izumi, T.1    Maller, J.L.2
  • 24
    • 0027075988 scopus 로고
    • Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase regulate its activity
    • Izumi, T., D. H. Walker, and J. L. Maller. 1992. Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase regulate its activity. Mol. Biol. Cell 3:927-939.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 927-939
    • Izumi, T.1    Walker, D.H.2    Maller, J.L.3
  • 25
    • 0031749011 scopus 로고    scopus 로고
    • Nuclear localization of cyclin B1 controls mitotic entry after DNA damage
    • Jin, P., S. Hardy, and D. O. Morgan. 1998. Nuclear localization of cyclin B1 controls mitotic entry after DNA damage. J. Cell Biol. 141:875-885.
    • (1998) J. Cell Biol. , vol.141 , pp. 875-885
    • Jin, P.1    Hardy, S.2    Morgan, D.O.3
  • 27
    • 0025980359 scopus 로고
    • The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system
    • Kumagai, A., and W. G. Dunphy. 1991. The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell 64:903-914.
    • (1991) Cell , vol.64 , pp. 903-914
    • Kumagai, A.1    Dunphy, W.G.2
  • 28
    • 0029821131 scopus 로고    scopus 로고
    • Purification and molecular cloning of P1x1, a cdc25-regulatory kinase from Xenopus egg extracts
    • Kumagai, A., and W. G. Dunphy. 1996. Purification and molecular cloning of P1x1, a cdc25-regulatory kinase from Xenopus egg extracts. Science 273: 1377-1380.
    • (1996) Science , vol.273 , pp. 1377-1380
    • Kumagai, A.1    Dunphy, W.G.2
  • 29
    • 0026719599 scopus 로고
    • Regulation of the cdc25 protein during the cell cycle in xenopus extracts
    • Kumagai, A., and W. G. Dunphy. 1992. Regulation of the cdc25 protein during the cell cycle in xenopus extracts. Cell 70:139-151.
    • (1992) Cell , vol.70 , pp. 139-151
    • Kumagai, A.1    Dunphy, W.G.2
  • 30
    • 0032555924 scopus 로고    scopus 로고
    • The Xenopus Chk1 protein kinase mediates a caffeine-sensitive pathway of checkpoint control in cell-free extracts
    • Kumagai, A., Z. Guo, K. H. Emami, S. X. Wang, and W. G. Dunphy. 1998. The Xenopus Chk1 protein kinase mediates a caffeine-sensitive pathway of checkpoint control in cell-free extracts. J. Cell Biol. 142:1559-1569.
    • (1998) J. Cell Biol. , vol.142 , pp. 1559-1569
    • Kumagai, A.1    Guo, Z.2    Emami, K.H.3    Wang, S.X.4    Dunphy, W.G.5
  • 31
    • 0031906844 scopus 로고    scopus 로고
    • 14-3-3 proteins act as negative regulators of the mitotic inducer cdc25 in Xenopus egg extracts
    • Kumagai, A., P. S. Yakowec, and W. G. Dunphy. 1998. 14-3-3 proteins act as negative regulators of the mitotic inducer cdc25 in Xenopus egg extracts. Mol. Biol. Cell 9:345-354.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 345-354
    • Kumagai, A.1    Yakowec, P.S.2    Dunphy, W.G.3
  • 34
    • 0023261635 scopus 로고
    • The retinoblastoma susceptibility gene encodes a nuclear phosphoprotein associated with DNa binding activity
    • Lee, W.-H., J.-Y. Shew, F. D. Hong, T. W. Sery, L. A. Donoso, L.-J. Young, R. Bookstein, and E. Y.-H. P. Lee. 1987. The retinoblastoma susceptibility gene encodes a nuclear phosphoprotein associated with DNA binding activity. Nature 329:642-645.
    • (1987) Nature , vol.329 , pp. 642-645
    • Lee, W.-H.1    Shew, J.-Y.2    Hong, F.D.3    Sery, T.W.4    Donoso, L.A.5    Young, L.-J.6    Bookstein, R.7    Lee, E.Y.-H.P.8
  • 35
    • 0031028382 scopus 로고    scopus 로고
    • Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation
    • Li, J., A. N. Meyer, and D. J. Donoghue. 1997. Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation. Proc. Natl. Acad. Sci. USA 94:502-507.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 502-507
    • Li, J.1    Meyer, A.N.2    Donoghue, D.J.3
  • 36
    • 0031053117 scopus 로고    scopus 로고
    • The human Myt1 kinase preferentially phosphorylates Cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex
    • Liu, F., J. J. Stanton, Z. Wu, and H. Piwnica-Worms. 1997. The human Myt1 kinase preferentially phosphorylates Cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex. Mol. Cell. Biol. 17:571-583.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 571-583
    • Liu, F.1    Stanton, J.J.2    Wu, Z.3    Piwnica-Worms, H.4
  • 37
    • 0033552943 scopus 로고    scopus 로고
    • Nuclear localization of Cdc25 is regulated by DNa damage and a 14-3-3 protein
    • Lopez-Girona, A., B. Furnari, O. Mondesert, and P. Russell. 1999. Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein. Nature 397:172-175.
    • (1999) Nature , vol.397 , pp. 172-175
    • Lopez-Girona, A.1    Furnari, B.2    Mondesert, O.3    Russell, P.4
  • 38
    • 0032484084 scopus 로고    scopus 로고
    • Linkage of ATM to cell cycle regulation by the chk2 protein kinase
    • Matsuoka, S., M. Huang, and S. J. Elledge. 1998. Linkage of ATM to cell cycle regulation by the chk2 protein kinase. Science 282:1893-1897.
    • (1998) Science , vol.282 , pp. 1893-1897
    • Matsuoka, S.1    Huang, M.2    Elledge, S.J.3
  • 41
    • 0025810049 scopus 로고
    • G1/S phosphorylation of the retinoblastoma protein is associated with an altered affinity for the nuclear compartment
    • Mittnacht, S., and R. A. Weinberg. 1991. G1/S phosphorylation of the retinoblastoma protein is associated with an altered affinity for the nuclear compartment. Cell 65:381-393.
    • (1991) Cell , vol.65 , pp. 381-393
    • Mittnacht, S.1    Weinberg, R.A.2
  • 42
    • 0028783413 scopus 로고
    • Myt1: A membrane-associated inhibitory kinase that phosphorylates cdc2 on both threonine-14 and tyrosine-15
    • Mueller, P. A., T. R. Coleman, A. Kumagai, and W. G. Dunphy. 1995. Myt1: a membrane-associated inhibitory kinase that phosphorylates cdc2 on both threonine-14 and tyrosine-15. Science 270:85-90.
    • (1995) Science , vol.270 , pp. 85-90
    • Mueller, P.A.1    Coleman, T.R.2    Kumagai, A.3    Dunphy, W.G.4
  • 43
    • 0021767899 scopus 로고
    • Use of peptide tagging to detect proteins expressed from cloned genes: Deletion mapping functions of Drosophila hsp70
    • Munro, S., and H. R. B. Pelham. 1984. Use of peptide tagging to detect proteins expressed from cloned genes: deletion mapping functions of Drosophila hsp70. EMBO J. 3:3087-3093.
    • (1984) EMBO J. , vol.3 , pp. 3087-3093
    • Munro, S.1    Pelham, H.R.B.2
  • 44
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by 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 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
  • 45
    • 0031470835 scopus 로고    scopus 로고
    • Checkpoint pathways come of age
    • Nurse, P. 1998. Checkpoint pathways come of age. Cell 91:865-867.
    • (1998) Cell , vol.91 , pp. 865-867
    • Nurse, P.1
  • 46
    • 0027938207 scopus 로고
    • Ordering S phase and M phase in the cell cycle
    • Nurse, P. 1994. Ordering S phase and M phase in the cell cycle. Cell 79:547-550.
    • (1994) Cell , vol.79 , pp. 547-550
    • Nurse, P.1
  • 47
    • 0028149892 scopus 로고
    • Purification of a serine kinase that associates with and phosphorylates human cdc25C on serine 216
    • Ogg, S., B. Gabrielli, and H. Piwnica-Worms. 1994. Purification of a serine kinase that associates with and phosphorylates human cdc25C on serine 216. J. Biol. Chem. 269:30461-30469.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30461-30469
    • Ogg, S.1    Gabrielli, B.2    Piwnica-Worms, H.3
  • 48
    • 0026616796 scopus 로고
    • Inactivation of the p34cdc2-cyclin B complex by the human wee1 tyrosine kinase
    • Parker, L. L., and H. Piwnica-Worms. 1992. Inactivation of the p34cdc2-cyclin B complex by the human wee1 tyrosine kinase. Science 257:1955-1957.
    • (1992) Science , vol.257 , pp. 1955-1957
    • Parker, L.L.1    Piwnica-Worms, H.2
  • 49
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of cdc25C on serine-216
    • Peng, C.-Y., P. R. Graves, R. S. Thoma, Z. Wu, A. S. Shaw, and H. Piwnica-Worms. 1997. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of cdc25C on serine-216. Science 277:1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.-Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 51
    • 0027933911 scopus 로고
    • The differential localization of human cyclins a and B is due to a cyloplasmic retention signal in cyclin B
    • Pines, J., and T. Hunter. 1994. The differential localization of human cyclins A and B is due to a cyloplasmic retention signal in cyclin B. EMBO J. 13:3772-3781.
    • (1994) EMBO J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 52
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to cdk regulation through cdc25
    • Sanchez, Y., C. Wong, R. S. Thoma, R. Richman, Z. Wu, H. Piwnica-Worms, and S. J. Elledge. 1997. Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to cdk regulation through cdc25. Science 277:1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.S.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.J.7
  • 53
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber, E., P. Matthias, M. M. Muller, and W. Schaffner. 1989. Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res. 17:6419.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 55
    • 85038169640 scopus 로고    scopus 로고
    • Unpublished data
    • Sellers, W. R. 1998. Unpublished data.
    • (1998)
    • Sellers, W.R.1
  • 58
    • 0029989279 scopus 로고    scopus 로고
    • Simian virus 40 large T antigen alters the phosphorylation state of the RB-related proteins p130 and p107
    • Stubdal, H., J. Zalvide, and J. A. DeCaprio. 1996. Simian virus 40 large T antigen alters the phosphorylation state of the RB-related proteins p130 and p107. J. Virol. 70:2781-2788.
    • (1996) J. Virol. , vol.70 , pp. 2781-2788
    • Stubdal, H.1    Zalvide, J.2    Decaprio, J.A.3
  • 59
    • 0032525308 scopus 로고    scopus 로고
    • Nuclear export of cyclin B1 and its possible role in the DNA damage-induced G2 checkpoint
    • Toyoshima, F., T. Moriguchi, A. Wada, M. Fukuda, and E. Nishida. 1998. Nuclear export of cyclin B1 and its possible role in the DNA damage-induced G2 checkpoint. EMBO J. 17:2728-2735.
    • (1998) EMBO J. , vol.17 , pp. 2728-2735
    • Toyoshima, F.1    Moriguchi, T.2    Wada, A.3    Fukuda, M.4    Nishida, E.5
  • 60
    • 0027208148 scopus 로고
    • Fission yeast chk1 protein kinase links the rad checkpoint pathway to cdc2
    • Walworth, N., S. Davey, and D. Beach. 1993. Fission yeast chk1 protein kinase links the rad checkpoint pathway to cdc2. Nature 363:368-371.
    • (1993) Nature , vol.363 , pp. 368-371
    • Walworth, N.1    Davey, S.2    Beach, D.3
  • 61
    • 0029664616 scopus 로고    scopus 로고
    • Rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint
    • Walworth, N. C., and R. Bernards. 1996. Rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint. Science 271: 353-356.
    • (1996) Science , vol.271 , pp. 353-356
    • Walworth, N.C.1    Bernards, R.2
  • 63
    • 0032528001 scopus 로고    scopus 로고
    • Control of cyclin B1 localization through regulated binding of the nuclear export factor, CRM1
    • Yang, J., E. S. G. Bardes, J. D. Moore, J. Brennan, M. Powers, and S. Kombluth. 1998. Control of cyclin B1 localization through regulated binding of the nuclear export factor, CRM1. Genes Dev. 12:2131-2143.
    • (1998) Genes Dev. , vol.12 , pp. 2131-2143
    • Yang, J.1    Bardes, E.S.G.2    Moore, J.D.3    Brennan, J.4    Powers, M.5    Kombluth, S.6
  • 64
    • 0031935825 scopus 로고    scopus 로고
    • The J domain of simian virus 40 large T antigen is required to functionally inactivate RB family proteins
    • Zalvide, J., H. Stubdal, and J. A. DeCaprio. 1998. The J domain of simian virus 40 large T antigen is required to functionally inactivate RB family proteins. Mol. Cell. Biol. 18:1408-1415.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1408-1415
    • Zalvide, J.1    Stubdal, H.2    Decaprio, J.A.3
  • 65
    • 0032190082 scopus 로고    scopus 로고
    • Replication checkpoint requires phosphorylation of the phosphatase cdc25 by Cds1 or Chk1
    • Zeng, Y., K. C. Forbes, Z. Wu, S. Moreno, H. Piwnica-Worms, and T. Enoch. 1998. Replication checkpoint requires phosphorylation of the phosphatase cdc25 by Cds1 or Chk1. Nature 395:507-510.
    • (1998) Nature , vol.395 , pp. 507-510
    • Zeng, Y.1    Forbes, K.C.2    Wu, Z.3    Moreno, S.4    Piwnica-Worms, H.5    Enoch, T.6
  • 66
    • 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-XL
    • 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-XL. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.