메뉴 건너뛰기




Volumn 18, Issue 6, 1999, Pages 1660-1672

A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking

Author keywords

MDM2; Neuroblastoma; Nuclear export; p53; Tetramerization

Indexed keywords

DIMER; LEPTOMYCIN B; LEUCINE; MONOMER; MUTANT PROTEIN; PROTEIN MDM2; PROTEIN P53; REGULATOR PROTEIN; TETRAMER;

EID: 0033559256     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.6.1660     Document Type: Article
Times cited : (618)

References (89)
  • 1
    • 0032576768 scopus 로고    scopus 로고
    • ES cells do not activate p53-dependent stress responses and undergo p53-independent apoptosis in response to DNA damage
    • Aladjem, M.I., Spike, B.T., Rodewald, L.W., Hope, T.J., Klemm, M., Jaenisch, R. and Wahl, G.M. (1998) ES cells do not activate p53-dependent stress responses and undergo p53-independent apoptosis in response to DNA damage. Curr. Biol., 8, 145-155.
    • (1998) Curr. Biol. , vol.8 , pp. 145-155
    • Aladjem, M.I.1    Spike, B.T.2    Rodewald, L.W.3    Hope, T.J.4    Klemm, M.5    Jaenisch, R.6    Wahl, G.M.7
  • 2
    • 0032509524 scopus 로고    scopus 로고
    • The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP
    • Askjaer, P., Jensen, T.H., Nilsson, J., Englmeier, L. and Kjems, J. (1998) The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP. J. Biol. Chem., 273, 33414-33422.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33414-33422
    • Askjaer, P.1    Jensen, T.H.2    Nilsson, J.3    Englmeier, L.4    Kjems, J.5
  • 3
    • 0030778227 scopus 로고    scopus 로고
    • Nuclear export signal of IκBα interferes with the Rev-dependent posttranscriptional regulation of human immunodeficiency virus type I
    • Bachelerie, F., Rodriguez, M.S., Dargemont, C., Rousset, D., Thomas, D., Virelizier, J.L. and Arenzana-Seisdedos, F. (1997) Nuclear export signal of IκBα interferes with the Rev-dependent posttranscriptional regulation of human immunodeficiency virus type I. J. Cell Sci., 110, 2883-2893.
    • (1997) J. Cell Sci. , vol.110 , pp. 2883-2893
    • Bachelerie, F.1    Rodriguez, M.S.2    Dargemont, C.3    Rousset, D.4    Thomas, D.5    Virelizier, J.L.6    Arenzana-Seisdedos, F.7
  • 4
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D. and Anderson, W.F. (1988) A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph., 6, 219-220.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-220
    • Bacon, D.1    Anderson, W.F.2
  • 6
    • 0029894726 scopus 로고    scopus 로고
    • Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay
    • Bogerd, H.P., Fridell, R.A., Benson, R.E., Hua, J. and Cullen, B.R. (1996) Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay. Mol. Cell. Biol., 16, 4207-4214.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4207-4214
    • Bogerd, H.P.1    Fridell, R.A.2    Benson, R.E.3    Hua, J.4    Cullen, B.R.5
  • 7
    • 0028978774 scopus 로고
    • P53 gene mutations. P53 protein accumulation and compartmentalization in colorectal adenocarcinoma
    • Bosari, S., Viale, G., Roncalli, M., Graziani, D., Borsani, G., Lee, A.K. and Coggi, G. (1995) p53 gene mutations. p53 protein accumulation and compartmentalization in colorectal adenocarcinoma. Am. J. Pathol. 147, 790-798.
    • (1995) Am. J. Pathol. , vol.147 , pp. 790-798
    • Bosari, S.1    Viale, G.2    Roncalli, M.3    Graziani, D.4    Borsani, G.5    Lee, A.K.6    Coggi, G.7
  • 9
    • 0032478331 scopus 로고    scopus 로고
    • Stabilization and activation of p53 are regulated independently by different phosphorylation events
    • Chernov, M.V., Ramana, C.V., Adler, V.V. and Stark, G.R. (1998) Stabilization and activation of p53 are regulated independently by different phosphorylation events. Proc. Natl Acad. Sci. USA, 95, 2284-2289.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2284-2289
    • Chernov, M.V.1    Ramana, C.V.2    Adler, V.V.3    Stark, G.R.4
  • 10
    • 0031973018 scopus 로고    scopus 로고
    • MYC abrogates p53-mediated cell cycle arrest in N (phosphonacetyl)-L-aspartate-treated cells, permitting CAD gene amplification
    • Chemova, O.B., Chernov, M.V., Ishizaka, Y., Agarwal, M.L. and Stark, G.R. (1998) MYC abrogates p53-mediated cell cycle arrest in N (phosphonacetyl)-L-aspartate-treated cells, permitting CAD gene amplification. Mol. Cell. Biol., 18, 536-545.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 536-545
    • Chemova, O.B.1    Chernov, M.V.2    Ishizaka, Y.3    Agarwal, M.L.4    Stark, G.R.5
  • 12
    • 0028131554 scopus 로고
    • Transcriptional activation by p53 correlates with suppression of growth but not transformation
    • Crook, T., Marston, N.J., Sara, E.A. and Vousden, K.H. (1994) Transcriptional activation by p53 correlates with suppression of growth but not transformation. Cell. 79, 817-827.
    • (1994) Cell. , vol.79 , pp. 817-827
    • Crook, T.1    Marston, N.J.2    Sara, E.A.3    Vousden, K.H.4
  • 13
    • 0029827769 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of nuclear p53 traffic occurs in one subclass of human tumor cells and in untransformed cells
    • David-Pfeuty, T., Chakrani, F., Ory, K. and Nouvian-Dooghe, Y. (1996) Cell cycle-dependent regulation of nuclear p53 traffic occurs in one subclass of human tumor cells and in untransformed cells. Cell Growth Differ., 7, 1211-1225.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1211-1225
    • David-Pfeuty, T.1    Chakrani, F.2    Ory, K.3    Nouvian-Dooghe, Y.4
  • 15
    • 0029130169 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., Huber, J., Boelens, W.C., Mattaj, I.W. and Luhrmann, R. (1995) The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell, 82, 475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 16
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M. and Mattaj, I.W. (1997) CRM1 is an export receptor for leucine-rich nuclear export signals. Cell, 90, 1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 17
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman, D.A. and Levine, A.J. (1998) Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol. Cell. Biol., 18, 7288-7293.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 18
    • 0027522365 scopus 로고
    • The p53 protein is an unusually shaped tetramer that binds directly to DNA
    • published erratum appears in Proc: Natl Acad. Sci. USA 1993, 90, 5878
    • Friedman, P.N., Chen, X., Bargonetti, J. and Prives, C. (1993) The p53 protein is an unusually shaped tetramer that binds directly to DNA [published erratum appears in Proc: Natl Acad. Sci. USA 1993, 90, 5878]. Proc. Natl Acad. Sci. USA, 90, 3319-3323.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3319-3323
    • Friedman, P.N.1    Chen, X.2    Bargonetti, J.3    Prives, C.4
  • 19
    • 0027500246 scopus 로고
    • Induction of nuclear accumulation of the tumor-suppressor protein p53 by DNA-damaging agents
    • published erratum appears in Oncogene 1993, 8, 2605
    • Fritsche, M., Haessler, C. and Brandner, G. (1993) Induction of nuclear accumulation of the tumor-suppressor protein p53 by DNA-damaging agents [published erratum appears in Oncogene 1993, 8, 2605]. Oncogene, 8, 307-318.
    • (1993) Oncogene , vol.8 , pp. 307-318
    • Fritsche, M.1    Haessler, C.2    Brandner, G.3
  • 20
    • 0029121296 scopus 로고
    • Nuclear export signals and the fast track to the cytoplasm
    • Gerace, L. (1995) Nuclear export signals and the fast track to the cytoplasm. Cell, 82, 341-344.
    • (1995) Cell , vol.82 , pp. 341-344
    • Gerace, L.1
  • 21
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich, D. and Mattaj, I.W. (1996) Nucleocytoplasmic transport. Science, 271, 1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 22
    • 0027953380 scopus 로고
    • Analysis of p53 quaternary structure in relation to sequence-specific DNA binding
    • Hainaut, P., Hall, A. and Milner, J. (1994) Analysis of p53 quaternary structure in relation to sequence-specific DNA binding. Oncogene, 9, 299-303.
    • (1994) Oncogene , vol.9 , pp. 299-303
    • Hainaut, P.1    Hall, A.2    Milner, J.3
  • 23
    • 0027521114 scopus 로고
    • Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants
    • Halazonetis, T.D. and Kandil, A.N. (1993) Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants. EMBO J., 12, 5057-5064.
    • (1993) EMBO J. , vol.12 , pp. 5057-5064
    • Halazonetis, T.D.1    Kandil, A.N.2
  • 24
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., Maya, R., Kazaz, A. and Oren, M. (1997) Mdm2 promotes the rapid degradation of p53. Nature, 387, 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 27
    • 0028519273 scopus 로고
    • Allosteric activation of latent p53 tetramers
    • Hupp, T.R. and Lane, D.P. (1994) Allosteric activation of latent p53 tetramers. Curr. Biol., 4, 865-875.
    • (1994) Curr. Biol. , vol.4 , pp. 865-875
    • Hupp, T.R.1    Lane, D.P.2
  • 28
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp, T.R., Meek, D.W., Midgley, C.A. and Lane, D.P. (1992) Regulation of the specific DNA binding function of p53. Cell, 71, 875-886.
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 30
    • 0028952841 scopus 로고
    • Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 Å
    • Jeffrey, P.D., Gorina, S. and Pavletich, N.P. (1995) Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 Å. Science. 267, 1498-1502.
    • (1995) Science , vol.267 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 31
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones, S.N., Roe, A.E., Donehower, L.A. and Bradley, A. (1995) Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature, 378, 206-208.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 32
    • 0030812331 scopus 로고    scopus 로고
    • Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers
    • Kaghad, M. et al. (1997) Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers. Cell, 90, 809-819.
    • (1997) Cell , vol.90 , pp. 809-819
    • Kaghad, M.1
  • 35
    • 0029783724 scopus 로고    scopus 로고
    • Characterization of the nuclear export signal of human T-cell lymphotropic virus type 1 Rex reveals that nuclear export is mediated by position-variable hydrophobic interactions
    • Kim, F.J., Beeche, A.A., Hunter, J.J., Chin, D.J. and Hope,T.J. (1996) Characterization of the nuclear export signal of human T-cell lymphotropic virus type 1 Rex reveals that nuclear export is mediated by position-variable hydrophobic interactions. Mol. Cell. Biol., 16, 5147-5155.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5147-5155
    • Kim, F.J.1    Beeche, A.A.2    Hunter, J.J.3    Chin, D.J.4
  • 36
    • 0032474750 scopus 로고    scopus 로고
    • Cytoplasmic retention of mutant tsp53 is dependent on an intermediate filament protein (vimentin) scaffold
    • Klotzsche, O., Etzrodt, D., Hohenberg, H., Bohn. W. and Deppert, W. (1998) Cytoplasmic retention of mutant tsp53 is dependent on an intermediate filament protein (vimentin) scaffold. Oncogene, 16, 3423-3434.
    • (1998) Oncogene , vol.16 , pp. 3423-3434
    • Klotzsche, O.1    Etzrodt, D.2    Hohenberg, H.3    Bohn, W.4    Deppert, W.5
  • 37
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko, L.J. and Prives, C. (1996) p53: puzzle and paradigm. Genes Dev., 10, 1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 38
    • 0030722533 scopus 로고    scopus 로고
    • Intracellular localization of p53 tumor suppressor protein in γ-irradiated cells is cell cycle regulated and determined by the nucleus
    • Komarova, E.A., Zelnick, C.R., Chin, D., Zeremski, M., Gleiberman, A.S., Bacus, S.S. and Gudkov, A.V. (1997) Intracellular localization of p53 tumor suppressor protein in γ-irradiated cells is cell cycle regulated and determined by the nucleus. Cancer Res., 57, 5217-5220.
    • (1997) Cancer Res. , vol.57 , pp. 5217-5220
    • Komarova, E.A.1    Zelnick, C.R.2    Chin, D.3    Zeremski, M.4    Gleiberman, A.S.5    Bacus, S.S.6    Gudkov, A.V.7
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 40
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat, M.H., Jones, S.N. and Vousden, K.H. (1997) Regulation of p53 stability by Mdm2. Nature, 387, 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 41
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie, P.H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A.J. and Pavletich, N.P. (1996) Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science, 274, 948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 42
    • 84970061891 scopus 로고
    • Solution structure of the tetrameric minimum transforming domain of p53
    • published erratum appears in Nature Struct. Biol. 1995, 2, 81
    • Lee, W., Harvey, T.S., Yin, Y., Yau, P., Litchfield, D. and Arrowsmith, C.H. (1994) Solution structure of the tetrameric minimum transforming domain of p53 [published erratum appears in Nature Struct. Biol. 1995, 2, 81]. Nature Struct. Biol., 1, 877-890.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 877-890
    • Lee, W.1    Harvey, T.S.2    Yin, Y.3    Yau, P.4    Litchfield, D.5    Arrowsmith, C.H.6
  • 43
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • Levine, A.J. (1997) p53, the cellular gatekeeper for growth and division. Cell, 88, 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 44
    • 0032584666 scopus 로고    scopus 로고
    • Cooperation of a single lysine mutation and a C-terminal domain in the cytoplasmic sequestration of the p53 protein
    • Liang, S.H., Hong, D. and Clarke, M.F. (1998) Cooperation of a single lysine mutation and a C-terminal domain in the cytoplasmic sequestration of the p53 protein. J. Biol. Chem., 273, 19817-19821.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19817-19821
    • Liang, S.H.1    Hong, D.2    Clarke, M.F.3
  • 45
    • 0028303752 scopus 로고
    • Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 EIB 55-kD protein
    • Lin, J., Chen, J., Elenbaas, B. and Levine, A.J. (1994) Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 EIB 55-kD protein. Genes Dev., 8, 1235-1246.
    • (1994) Genes Dev. , vol.8 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3    Levine, A.J.4
  • 47
    • 0032490875 scopus 로고    scopus 로고
    • Characterization of p53 oligomerization domain mutations isolated from Li-Fraumeni and Li-Fraumeni-like family members
    • Lomax, M.E., Barnes, D.M., Hupp, T.R., Picksley, S.M. and Camplejohn, R.S. (1998) Characterization of p53 oligomerization domain mutations isolated from Li-Fraumeni and Li-Fraumeni-like family members. Oncogene, 17, 643-649.
    • (1998) Oncogene , vol.17 , pp. 643-649
    • Lomax, M.E.1    Barnes, D.M.2    Hupp, T.R.3    Picksley, S.M.4    Camplejohn, R.S.5
  • 48
    • 8044222151 scopus 로고    scopus 로고
    • Novel patterns of p53 abnormality in breast cancer from Taiwan: Experience from a low-incidence area
    • Lou, M.A. et al. (1997) Novel patterns of p53 abnormality in breast cancer from Taiwan: experience from a low-incidence area. Br. J. Cancer, 75, 746-751.
    • (1997) Br. J. Cancer , vol.75 , pp. 746-751
    • Lou, M.A.1
  • 49
    • 0032568633 scopus 로고    scopus 로고
    • Ultraviolet radiation, but not gamma radiation or etoposide-induced DNA damage, results in the phosphorylation of the murine p53 protein at serine-389
    • Lu, H., Taya, Y., Ikeda, M. and Levine, A.J. (1998) Ultraviolet radiation, but not gamma radiation or etoposide-induced DNA damage, results in the phosphorylation of the murine p53 protein at serine-389. Proc. Natl Acad. Sci. USA. 95, 6399-6402.
    • (1998) Proc. Natl Acad. Sci. USA. , vol.95 , pp. 6399-6402
    • Lu, H.1    Taya, Y.2    Ikeda, M.3    Levine, A.J.4
  • 51
    • 0032525133 scopus 로고    scopus 로고
    • Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain
    • Mateu, M.G. and Fersht, A.R. (1998) Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain. EMBO J., 17, 2748-2758.
    • (1998) EMBO J. , vol.17 , pp. 2748-2758
    • Mateu, M.G.1    Fersht, A.R.2
  • 52
    • 0032526426 scopus 로고    scopus 로고
    • How p53 binds DNA as a tetramer
    • McLure, K.G. and Lee, P.W. (1998) How p53 binds DNA as a tetramer. EMBO J., 17, 3342-3350.
    • (1998) EMBO J. , vol.17 , pp. 3342-3350
    • McLure, K.G.1    Lee, P.W.2
  • 53
    • 0030935858 scopus 로고    scopus 로고
    • The tumor suppressor p53 is subject to both nuclear import and export and both are fast, energy-dependent and lectin-inhibited
    • Middeler, G., Zerf, K., Jenovai, S., Thulig, A., Tschodrich-Rotter, M., Kubitscheck, U. and Peters, R. (1997) The tumor suppressor p53 is subject to both nuclear import and export and both are fast, energy-dependent and lectin-inhibited. Oncogene, 14, 1407-1417.
    • (1997) Oncogene , vol.14 , pp. 1407-1417
    • Middeler, G.1    Zerf, K.2    Jenovai, S.3    Thulig, A.4    Tschodrich-Rotter, M.5    Kubitscheck, U.6    Peters, R.7
  • 54
    • 0026694826 scopus 로고
    • Two distinct mechanisms alter p53 in breast cancer: Mutation and nuclear exclusion
    • Moll, U.M., Riou, G. and Levine, A.J. (1992) Two distinct mechanisms alter p53 in breast cancer: mutation and nuclear exclusion. Proc. Natl Acad. Sci. USA. 89, 7262-7266.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7262-7266
    • Moll, U.M.1    Riou, G.2    Levine, A.J.3
  • 55
    • 0029049828 scopus 로고
    • Wild-type p53 protein undergoes cytoplasmic sequestration in undifferentiated neuroblastomas but not in differentiated tumors
    • Moll, U.M., LaQuaglia, M., Benard, J. and Riou, G. (1995) Wild-type p53 protein undergoes cytoplasmic sequestration in undifferentiated neuroblastomas but not in differentiated tumors. Proc. Natl Acad. Sci. USA, 92, 4407-4411.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4407-4411
    • Moll, U.M.1    LaQuaglia, M.2    Benard, J.3    Riou, G.4
  • 58
    • 0016718010 scopus 로고
    • Mouse-human heterokaryon analysis with a 33258 Hoechst-Giemsa technique
    • Moser, F.G., Dorman, B.P. and Ruddle, F.H. (1975) Mouse-human heterokaryon analysis with a 33258 Hoechst-Giemsa technique. J. Cell Biol., 66, 676-680.
    • (1975) J. Cell Biol. , vol.66 , pp. 676-680
    • Moser, F.G.1    Dorman, B.P.2    Ruddle, F.H.3
  • 59
    • 0030782642 scopus 로고    scopus 로고
    • A fluorescent p53GFP fusion protein facilitates its detection in mammalian cells while retaining the properties of wild-type p53
    • Norris, P.S. and Haas, M. (1997) A fluorescent p53GFP fusion protein facilitates its detection in mammalian cells while retaining the properties of wild-type p53. Oncogene, 15, 2241-2247.
    • (1997) Oncogene , vol.15 , pp. 2241-2247
    • Norris, P.S.1    Haas, M.2
  • 61
    • 0031852337 scopus 로고    scopus 로고
    • Cloning and functional analysis of human p51, which structurally and functionally resembles p53
    • Osada, M. et al (1998) Cloning and functional analysis of human p51, which structurally and functionally resembles p53. Nature Med., 4, 839-843.
    • (1998) Nature Med. , vol.4 , pp. 839-843
    • Osada, M.1
  • 62
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., Bachelerie, F. and Dargemont, C. (1997) Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science. 278, 141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 63
    • 0030448760 scopus 로고    scopus 로고
    • Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus hy a C-terminal peptide
    • Ostermeyer, A.G., Runko, E., Winkfield, B., Ahn, B. and Moll, U.M. (1996) Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus hy a C-terminal peptide. Proc: Natl Acad. Sci. USA, 93, 15190-15194.
    • (1996) Proc: Natl Acad. Sci. USA , vol.93 , pp. 15190-15194
    • Ostermeyer, A.G.1    Runko, E.2    Winkfield, B.3    Ahn, B.4    Moll, U.M.5
  • 64
    • 0031893222 scopus 로고    scopus 로고
    • Gene amplification in a p53-deficient cell line requires cell cycle progression under conditions that generate DNA breakage
    • Paulson, T.G., Almasan, A., Brody, L.L. and Wahl, G.M. (1998) Gene amplification in a p53-deficient cell line requires cell cycle progression under conditions that generate DNA breakage. Mol. Cell. Biol., 18, 3089-3100.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3089-3100
    • Paulson, T.G.1    Almasan, A.2    Brody, L.L.3    Wahl, G.M.4
  • 67
    • 0029132301 scopus 로고
    • Cdk2 kinase phosphorylates serine 315 of human p53 in vitro
    • Price, B.D., Hughes-Davies, L. and Park, S.J. (1995) Cdk2 kinase phosphorylates serine 315 of human p53 in vitro. Oncogene, 11, 73-80.
    • (1995) Oncogene , vol.11 , pp. 73-80
    • Price, B.D.1    Hughes-Davies, L.2    Park, S.J.3
  • 68
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth, J., Dobbelstein, M., Freedman, D.A., Shenk, T. and Levine, A.J. (1998) Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J., 17, 554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 69
    • 0030790778 scopus 로고    scopus 로고
    • Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53
    • Sakaguchi, K., Sakamoto, H., Lewis, M.S., Anderson, C.W., Erickson, J.W., Appella, E. and Xie, D. (1997) Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53. Biochemistry, 36, 10117-10124.
    • (1997) Biochemistry , vol.36 , pp. 10117-10124
    • Sakaguchi, K.1    Sakamoto, H.2    Lewis, M.S.3    Anderson, C.W.4    Erickson, J.W.5    Appella, E.6    Xie, D.7
  • 70
    • 0030779121 scopus 로고    scopus 로고
    • Nuclear exclusion of wild-type p_53 in immortalized human retinoblastoma cells
    • Schlamp, C.L., Poulsen, G.L. Nork, T.M. and Nickells, R.W. (1997) Nuclear exclusion of wild-type p_53 in immortalized human retinoblastoma cells. J. Natl Cancer Inst., 89, 1530-1536.
    • (1997) J. Natl Cancer Inst. , vol.89 , pp. 1530-1536
    • Schlamp, C.L.1    Poulsen, G.L.2    Nork, T.M.3    Nickells, R.W.4
  • 71
    • 0025203803 scopus 로고
    • Subcellular distribution of the p53 protein during the cell cycle of Balb/c 3T3 cells
    • Shaulsky, G., Ben-Ze'ev, A. and Rotter, V. (1990a) Subcellular distribution of the p53 protein during the cell cycle of Balb/c 3T3 cells. Oncogene, 5, 1707-1711.
    • (1990) Oncogene , vol.5 , pp. 1707-1711
    • Shaulsky, G.1    Ben-Ze'ev, A.2    Rotter, V.3
  • 72
    • 0025201181 scopus 로고
    • Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis
    • Shaulsky, G., Goldfinger, N., Ben-Ze'ev, A. and Rotter, V. (1990b) Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis. Mol. Cell. Biol., 10, 6565-6577.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6565-6577
    • Shaulsky, G.1    Goldfinger, N.2    Ben-Ze'ev, A.3    Rotter, V.4
  • 73
    • 0032191393 scopus 로고    scopus 로고
    • Tumor surveillance via the ARF-p53 pathway
    • Sherr, C.J. (1998) Tumor surveillance via the ARF-p53 pathway. Genes Dev., 12, 2984-2991.
    • (1998) Genes Dev. , vol.12 , pp. 2984-2991
    • Sherr, C.J.1
  • 74
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S.Y., Ikeda, M., Taya, Y. and Prives, C. (1997) DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell, 91, 325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 75
    • 0030564943 scopus 로고    scopus 로고
    • Structural aspects of the p53 protein in relation to gene evolution: A second look
    • Soussi, T. and May, P. (1996) Structural aspects of the p53 protein in relation to gene evolution: a second look. J. Mol. Biol., 260, 623-637.
    • (1996) J. Mol. Biol. , vol.260 , pp. 623-637
    • Soussi, T.1    May, P.2
  • 77
  • 80
    • 0030886673 scopus 로고    scopus 로고
    • Nuclear export receptors: From importin to exportin
    • Ullman, K.S., Powers, M.A. and Forbes, D.J. (1997) Nuclear export receptors: from importin to exportin. Cell, 90, 967-970.
    • (1997) Cell , vol.90 , pp. 967-970
    • Ullman, K.S.1    Powers, M.A.2    Forbes, D.J.3
  • 81
    • 0029955185 scopus 로고    scopus 로고
    • A previously undescribed mutation within the tetramerisation domain of TP53 in a family with Li-Fraumeni syndrome
    • Varley, J.M. et al. (1996) A previously undescribed mutation within the tetramerisation domain of TP53 in a family with Li-Fraumeni syndrome. Oncogene, 12, 2437-2442.
    • (1996) Oncogene , vol.12 , pp. 2437-2442
    • Varley, J.M.1
  • 82
    • 0031003783 scopus 로고    scopus 로고
    • Maintaining genetic stability through TP53 mediated checkpoint control
    • Wahl, G.M., Linke, S.P., Paulson, T.G. and Huang, L.C. (1997) Maintaining genetic stability through TP53 mediated checkpoint control. Cancer Surv., 29, 183-219.
    • (1997) Cancer Surv. , vol.29 , pp. 183-219
    • Wahl, G.M.1    Linke, S.P.2    Paulson, T.G.3    Huang, L.C.4
  • 84
    • 0028888020 scopus 로고
    • The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding
    • Waterman, J.L., Shenk, J.L. and Halazonetis, T.D. (1995) The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding. EMBO J., 14, 512-519.
    • (1995) EMBO J. , vol.14 , pp. 512-519
    • Waterman, J.L.1    Shenk, J.L.2    Halazonetis, T.D.3
  • 85
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., Meinkoth, J.L., Tsien, R.Y. and Taylor, S.S. (1995) Identification of a signal for rapid export of proteins from the nucleus. Cell, 82, 463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 86
    • 0031079648 scopus 로고    scopus 로고
    • Leptomycin B is an inhibitor of nuclear export: Inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA
    • Wolff, B., Sanglier, J.J. and Wang, Y. (1997) Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem. Biol., 4, 139-147.
    • (1997) Chem. Biol. , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 87
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu, X., Bayle, J.H., Olson, D. and Levine, A.J. (1993) The p53-mdm-2 autoregulatory feedback loop. Genes Dev., 7, 1126-1132.
    • (1993) Genes Dev. , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 88
    • 0032528001 scopus 로고    scopus 로고
    • Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1
    • Yang, J., Bardes, E.S.G., Moore, J.D., Brennan, J., Powers, M.A. and Kornbluth, S. (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.A.5    Kornbluth, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.