메뉴 건너뛰기




Volumn 253, Issue 2, 1999, Pages 315-324

Accumulating active p53 in the nucleus by inhibition of nuclear export: A novel strategy to promote the p53 tumor suppressor function

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; PROTEIN P53;

EID: 0343938848     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4672     Document Type: Review
Times cited : (56)

References (104)
  • 1
    • 0028049474 scopus 로고
    • Regulation of mdm2 expression by p53: Alternative promoters produce transcripts with nonidentical translation potential
    • Barak Y., Gottlieb E., Juven-Gershon T., Oren M. Regulation of mdm2 expression by p53: Alternative promoters produce transcripts with nonidentical translation potential. Genes Dev. 8:1994;1739-1749.
    • (1994) Genes Dev. , vol.8 , pp. 1739-1749
    • Barak, Y.1    Gottlieb, E.2    Juven-Gershon, T.3    Oren, M.4
  • 2
    • 0032984992 scopus 로고    scopus 로고
    • Mechanisms of p53-mediated apoptosis
    • Bates S., Vousden K. H. Mechanisms of p53-mediated apoptosis. Cell. Mol. Life Sci. 55:1999;28-37.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 28-37
    • Bates, S.1    Vousden, K.H.2
  • 4
    • 0031282325 scopus 로고    scopus 로고
    • Peptide aptamers that disrupt the interaction between mdm2 and p53 in vivo activate p53 dependent transcription and inhibit p53 degradation
    • Bottger A., Bottger V., Sparks A., Liu W-L., Howard S. F., Lane D. Peptide aptamers that disrupt the interaction between mdm2 and p53 in vivo activate p53 dependent transcription and inhibit p53 degradation. Curr. Biol. 7:1997b;860-869.
    • (1997) Curr. Biol. , vol.7 , pp. 860-869
    • Bottger, A.1    Bottger, V.2    Sparks, A.3    Liu, W.-L.4    Howard, S.F.5    Lane, D.6
  • 5
    • 0028070989 scopus 로고
    • P53-dependent apoptosis in the absence of transcriptional activation of p53-target genes
    • Caelles C., Helmberg A., Karin M. p53-dependent apoptosis in the absence of transcriptional activation of p53-target genes. Nature. 370:1994;220-223.
    • (1994) Nature , vol.370 , pp. 220-223
    • Caelles, C.1    Helmberg, A.2    Karin, M.3
  • 6
    • 0030783156 scopus 로고    scopus 로고
    • The search for physiological substrates of MAP and SAP kinases in mammalian cells
    • Cohen P. The search for physiological substrates of MAP and SAP kinases in mammalian cells. Trends Cell. Biol. 7:1997;353-361.
    • (1997) Trends Cell. Biol. , vol.7 , pp. 353-361
    • Cohen, P.1
  • 8
    • 0032975130 scopus 로고    scopus 로고
    • Ubiquitous induction of p53 in tumour cells by antisense inhibition of MDM2 expression
    • Chen L., Lu W., Agrawal S., Zhou W., Zhang R., Chen J. Ubiquitous induction of p53 in tumour cells by antisense inhibition of MDM2 expression. Mol. Med. 5:1999;21-34.
    • (1999) Mol. Med. , vol.5 , pp. 21-34
    • Chen, L.1    Lu, W.2    Agrawal, S.3    Zhou, W.4    Zhang, R.5    Chen, J.6
  • 9
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and the 26S proteasomes
    • Coux O., Tanaka K., Goldberg A. L. Structure and functions of the 20S and the 26S proteasomes. Annu. Rev. Biochem. 65:1996;801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 10
    • 0032546326 scopus 로고    scopus 로고
    • A transforming p53 mutant, which binds DNA, transactivates and induces apoptosis reveals a nuclear:cytoplasmic shuttling defect
    • Crook T., Parker G. A., Rozycka M., Crossland S., Allday M. J. A transforming p53 mutant, which binds DNA, transactivates and induces apoptosis reveals a nuclear:cytoplasmic shuttling defect. Oncogene. 16:1998;1429-1441.
    • (1998) Oncogene , vol.16 , pp. 1429-1441
    • Crook, T.1    Parker, G.A.2    Rozycka, M.3    Crossland, S.4    Allday, M.J.5
  • 11
    • 0024431720 scopus 로고
    • Nuclear and nucleolar sequences of c-erb-A, c-myb, N-myc, p53. HSP70, and HIV tat proteins
    • Dang C. V., Lee W. M. Nuclear and nucleolar sequences of c-erb-A, c-myb, N-myc, p53. HSP70, and HIV tat proteins. J. Biol. Chem. 264:1989;18019-18023.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18019-18023
    • Dang, C.V.1    Lee, W.M.2
  • 12
    • 0029827769 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of nuclear p53 traffic occurs in one subclass of human tumour cells and in untransformed cells
    • David-Pfeuty T., Chakrani F., Ory K., Nouvian-Dooghe Y. Cell cycle-dependent regulation of nuclear p53 traffic occurs in one subclass of human tumour cells and in untransformed cells. Cell Growth Differ. 7:1996;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
  • 13
    • 0028220204 scopus 로고
    • P53-dependent inhibition of cyclin-dependent kinase activities in human fibroblasts during radiation-induced G1 arrest
    • Dulic V., Kaufmann W. K., Wilson S. J., Tlsty T. D., Lees E., Harper J. W., Elledge S. J., Reed S. I. p53-dependent inhibition of cyclin-dependent kinase activities in human fibroblasts during radiation-induced G1 arrest. Cell. 76:1994;1013-1023.
    • (1994) Cell , vol.76 , pp. 1013-1023
    • Dulic, V.1    Kaufmann, W.K.2    Wilson, S.J.3    Tlsty, T.D.4    Lees, E.5    Harper, J.W.6    Elledge, S.J.7    Reed, S.I.8
  • 15
    • 0032526988 scopus 로고    scopus 로고
    • Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation
    • Engel K., Kotlyarov A., Gaestel M. Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. EMBO J. 17:1998;3363-3371.
    • (1998) EMBO J. , vol.17 , pp. 3363-3371
    • Engel, K.1    Kotlyarov, A.2    Gaestel, M.3
  • 16
    • 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., Lührmann R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell. 82:1995;475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührmann, R.5
  • 18
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., Ohno M., Yoshida M., Mattaj I. W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 90:1997;1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 19
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman D. A., Levine A. J. Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol. Cell. Biol. 18:1998;7288-7293.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 21
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda M., Asano S., Nakamura T., Adachi M., Yoshida M., Yanagida M., Nishida E. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature. 390:1997;308-311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 22
    • 0029786994 scopus 로고    scopus 로고
    • Cytoplasmic localisation of mitogen-activated protein kinase directed by its NH2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal
    • Fukuda M., Gotoh I., Gotoh Y., Nishida E. Cytoplasmic localisation of mitogen-activated protein kinase directed by its NH2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal. J. Biol. Chem. 271:1996;20024-20028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20024-20028
    • Fukuda, M.1    Gotoh, I.2    Gotoh, Y.3    Nishida, E.4
  • 23
    • 0025975701 scopus 로고
    • Protein-synthes is required to anchor a mutant p53 protein which is temperature-sensitive for nuclear transport
    • Gannon J. V., Lane D. P. Protein-synthes is required to anchor a mutant p53 protein which is temperature-sensitive for nuclear transport. Nature. 349:1991;802-806.
    • (1991) Nature , vol.349 , pp. 802-806
    • Gannon, J.V.1    Lane, D.P.2
  • 26
    • 0027496935 scopus 로고
    • The p21 cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper J. W., Adami G. R., Wei N., Keyomarsi K., Elledge S. The p21 cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell. 75:1993;805-816.
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.5
  • 27
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. Mdm2 promotes the rapid degradation of p53. Nature. 387:1997;296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 28
    • 0028999429 scopus 로고
    • P53-mediated apoptosis in HeLa cells can be overcome by excess pRB
    • Haupt Y., Rowan S., Oren M. p53-mediated apoptosis in HeLa cells can be overcome by excess pRB. Oncogene. 10:1995;1563-1571.
    • (1995) Oncogene , vol.10 , pp. 1563-1571
    • Haupt, Y.1    Rowan, S.2    Oren, M.3
  • 31
    • 0033521621 scopus 로고    scopus 로고
    • ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 tumour suppressor p53
    • ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 tumour suppressor p53. EMBO J. 18:1999;22-27.
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 33
    • 0029028352 scopus 로고
    • Mutational analysis of the carboxy-terminal portion of p53 using both yeast and mammalian cell assays in vivo
    • Ishioka C., Englert C., Winge P., Yan Y. X., Engelstein M., Friend S. H. Mutational analysis of the carboxy-terminal portion of p53 using both yeast and mammalian cell assays in vivo. Oncogene. 10:1995;1485-1492.
    • (1995) Oncogene , vol.10 , pp. 1485-1492
    • Ishioka, C.1    Englert, C.2    Winge, P.3    Yan, Y.X.4    Engelstein, M.5    Friend, S.H.6
  • 34
    • 0027501841 scopus 로고
    • Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene
    • Juven T., Barak Y., Zauberman A., George D. L., Oren M. Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene. Oncogene. 8:1993;3411-3416.
    • (1993) Oncogene , vol.8 , pp. 3411-3416
    • Juven, T.1    Barak, Y.2    Zauberman, A.3    George, D.L.4    Oren, M.5
  • 35
    • 0032443366 scopus 로고    scopus 로고
    • Determination of cell fate by c-Abl activation in response to DNA damage
    • Kharbanda S., Yuan Z. M., Weichselbaum R., Kufe D. Determination of cell fate by c-Abl activation in response to DNA damage. Oncogene. 17:1998;3309-3318.
    • (1998) Oncogene , vol.17 , pp. 3309-3318
    • Kharbanda, S.1    Yuan, Z.M.2    Weichselbaum, R.3    Kufe, D.4
  • 36
    • 0029972806 scopus 로고    scopus 로고
    • P53: Puzzle and paradigm
    • Ko L. J., Prives C. p53: Puzzle and paradigm. Genes Dev. 10:1996;1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 37
    • 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., Gudkov A. V. Intracellular localization of p53 tumor suppressor protein in γ-irradiated cells is cell cycle regulated and determined by the nucleus. Cancer Res. 57:1997;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
  • 38
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat M. H., Jones S. N., Vousden K. H. Regulation of p53 stability by Mdm2. Nature. 387:1997;299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 39
    • 0033591412 scopus 로고    scopus 로고
    • A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1
    • Kudo N., Taoka H., Toda T., Yoshida M., Horinouchi S. A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1. J. Biol. Chem. 274:1999;15151-15158.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15151-15158
    • Kudo, N.1    Taoka, H.2    Toda, T.3    Yoshida, M.4    Horinouchi, S.5
  • 41
    • 0030701840 scopus 로고    scopus 로고
    • Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins
    • Kudo N., Khochbin S., Nishi K., Kitano K., Yanagida M., Horinouchi S. Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J. Biol. Chem. 272:1997;29742-29751.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29742-29751
    • Kudo, N.1    Khochbin, S.2    Nishi, K.3    Kitano, K.4    Yanagida, M.5    Horinouchi, S.6
  • 43
    • 0033134794 scopus 로고    scopus 로고
    • Binding of 14-3-3 proteins and nuclear export control the intracellular localisation of the mitotic inducer Cdc25
    • Kumagai A., Dunphy W. G. Binding of 14-3-3 proteins and nuclear export control the intracellular localisation of the mitotic inducer Cdc25. Genes and Dev. 13:1999;1067-1072.
    • (1999) Genes and Dev. , vol.13 , pp. 1067-1072
    • Kumagai, A.1    Dunphy, W.G.2
  • 44
    • 0038298110 scopus 로고    scopus 로고
    • An inhibitor of nuclear export activates the p53 response and induces the localisation of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs
    • Laín S., Midgley C., Sparks A., Lane B., Lane D. P. An inhibitor of nuclear export activates the p53 response and induces the localisation of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs. Exp. Cell. Res. 248:1999;457-472.
    • (1999) Exp. Cell. Res. , vol.248 , pp. 457-472
    • Laín, S.1    Midgley, C.2    Sparks, A.3    Lane, B.4    Lane, D.P.5
  • 45
    • 17144460505 scopus 로고    scopus 로고
    • Awakening angels
    • Lane D. P. Awakening angels. Nature. 394:1998;616-617.
    • (1998) Nature , vol.394 , pp. 616-617
    • Lane, D.P.1
  • 47
    • 0030941458 scopus 로고    scopus 로고
    • The cellular gatekeeper for growth and division
    • Levine A. The cellular gatekeeper for growth and division. Cell. 88:1997;323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.1
  • 48
    • 0033602407 scopus 로고    scopus 로고
    • The nuclear import of p53 is determined by the presence of a basic domain and its relative position to the nuclear localization signal
    • Liang S. H., Clarke M. F. The nuclear import of p53 is determined by the presence of a basic domain and its relative position to the nuclear localization signal. Oncogene. 18:1999;2163-2166.
    • (1999) Oncogene , vol.18 , pp. 2163-2166
    • Liang, S.H.1    Clarke, M.F.2
  • 49
    • 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., Clarke M. F. Cooperation of a single lysine mutation and a C-terminal domain in the cytoplasmic sequestration of the p53 protein. J. Biol. Chem. 273:1998;19817-19821.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19817-19821
    • Liang, S.H.1    Hong, D.2    Clarke, M.F.3
  • 50
    • 0032190629 scopus 로고    scopus 로고
    • Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling
    • Lin A. W., Barradas M., Stone J. C., van Aelst L., Serrano M., Lowe S. W. Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling. Genes Dev. 12:1998;3008-3019.
    • (1998) Genes Dev. , vol.12 , pp. 3008-3019
    • Lin, A.W.1    Barradas, M.2    Stone, J.C.3    Van Aelst, L.4    Serrano, M.5    Lowe, S.W.6
  • 51
    • 0033523015 scopus 로고    scopus 로고
    • Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2
    • Maki C. G. Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2. J. Biol. Chem. 274:1999;16531-16535.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16531-16535
    • Maki, C.G.1
  • 52
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic export: The soluble phase
    • Mattaj I. W., Englmeier L. Nucleocytoplasmic export: The soluble phase. Annu. Rev. Biochem. 67:1998;265-306.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 53
    • 0030935858 scopus 로고    scopus 로고
    • The tumor suppressor p53 is subject both to nuclear import and export, and both are fast, energy-dependent and lectin-inhibited
    • Middeler G., Zerf K., Jenovai S., Thulig A., Tschordrich-Rotter M., Kubitscheck U., Peters R. The tumor suppressor p53 is subject both to nuclear import and export, and both are fast, energy-dependent and lectin-inhibited. Oncogene. 14:1997;1407-1417.
    • (1997) Oncogene , vol.14 , pp. 1407-1417
    • Middeler, G.1    Zerf, K.2    Jenovai, S.3    Thulig, A.4    Tschordrich-Rotter, M.5    Kubitscheck, U.6    Peters, R.7
  • 54
    • 0030825813 scopus 로고    scopus 로고
    • P53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding
    • Midgley C. A., Lane D. P. p53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding. Oncogene. 15:1997;1179-1189.
    • (1997) Oncogene , vol.15 , pp. 1179-1189
    • Midgley, C.A.1    Lane, D.P.2
  • 55
    • 0342871691 scopus 로고    scopus 로고
    • Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, translation, and the cellular stress response
    • Mimnaugh E. G., Chen H. Y., Davie J. R., Celis J. E., Neckers L. Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, translation, and the cellular stress response. Biochemistry. 36:1997;14418-14429.
    • (1997) Biochemistry , vol.36 , pp. 14418-14429
    • Mimnaugh, E.G.1    Chen, H.Y.2    Davie, J.R.3    Celis, J.E.4    Neckers, L.5
  • 56
    • 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., Riou G. Wild-type p53 protein undergoes cytoplasmic sequestration in undifferentiated neuroblastomas but not in differentiated tumors. Proc. Natl. Acad. Sci. USA. 92:1995;4404-4411.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4404-4411
    • Moll, U.M.1    Laquaglia, M.2    Benard, J.3    Riou, G.4
  • 57
  • 58
    • 0026694826 scopus 로고
    • Two distinct mechanisms alter p53 in breast-cancer - Mutation and nuclear exclusion
    • Moll U. M., Riou G., Levine A. J. Two distinct mechanisms alter p53 in breast-cancer - Mutation and nuclear exclusion. Proc. Natl. Acad. Sci. USA. 89:1992;7262-7266.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7262-7266
    • Moll, U.M.1    Riou, G.2    Levine, A.J.3
  • 59
    • 0026649648 scopus 로고
    • The mdm2 oncogene product forms a complex with p53 protein and inhibits p53-mediated transactivation
    • Mommand J., Zambetti G. P., Olson D. C., George D., Levine A. J. The mdm2 oncogene product forms a complex with p53 protein and inhibits p53-mediated transactivation. Cell. 69:1992;1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Mommand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 60
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan D. O. Principles of CDK regulation. Nature. 374:1995;131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 61
    • 0031260540 scopus 로고    scopus 로고
    • The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export
    • Neville M., Stutz F., Lee L., Davis L. I., Rosbash M. The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr. Biol. 7:1997;767-775.
    • (1997) Curr. Biol. , vol.7 , pp. 767-775
    • Neville, M.1    Stutz, F.2    Lee, L.3    Davis, L.I.4    Rosbash, M.5
  • 63
    • 0031470835 scopus 로고    scopus 로고
    • Checkpoint pathways come of age
    • Nurse P. Checkpoint pathways come of age. Cell. 91:1997;865-867.
    • (1997) Cell , vol.91 , pp. 865-867
    • Nurse, P.1
  • 65
    • 0026568213 scopus 로고
    • Relocation and distinct subcellular localization of p34cdc2-cyclin B complex at meiosis reinitiation in starfish oocytes
    • Ookata K., Hisanaga S., Okano T., Tachibana K., Kishimoto T. Relocation and distinct subcellular localization of p34cdc2-cyclin B complex at meiosis reinitiation in starfish oocytes. EMBO J. 11:1992;1763-1772.
    • (1992) EMBO J. , vol.11 , pp. 1763-1772
    • Ookata, K.1    Hisanaga, S.2    Okano, T.3    Tachibana, K.4    Kishimoto, T.5
  • 66
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal mediated nuclear protein export
    • Ossareh-Nazari B., Bachelerie F., Dargemont C. Evidence for a role of CRM1 in signal mediated nuclear protein export. Science. 278:1997;141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 67
    • 0033552847 scopus 로고    scopus 로고
    • Checkpoint on the nuclear frontier
    • Pines J. Checkpoint on the nuclear frontier. Nature. 397:1999;104-105.
    • (1999) Nature , vol.397 , pp. 104-105
    • Pines, J.1
  • 68
    • 0026014878 scopus 로고
    • Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport
    • Pines J., Hunter T. Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. J. Cell Biol. 115:1991;1-17.
    • (1991) J. Cell Biol. , vol.115 , pp. 1-17
    • Pines, J.1    Hunter, T.2
  • 69
    • 0027933911 scopus 로고
    • The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B
    • Pines J., Hunter T. The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B. EMBO J. 13:1994;3772-3781.
    • (1994) EMBO J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 70
    • 0022647482 scopus 로고
    • In vivo and in vitro anticancer activity of the structurally novel and highly potent antibiotic CI-940 and its hydroxy analog
    • Roberts B. J., Hamelehle K. L., Selbolt J. S., Leopold W. R. In vivo and in vitro anticancer activity of the structurally novel and highly potent antibiotic CI-940 and its hydroxy analog. Cancer Chemother. Pharmacol. 16:1986;95-101.
    • (1986) Cancer Chemother. Pharmacol. , vol.16 , pp. 95-101
    • Roberts, B.J.1    Hamelehle, K.L.2    Selbolt, J.S.3    Leopold, W.R.4
  • 71
    • 0033605424 scopus 로고    scopus 로고
    • Nuclear retention of IkappaBalpha protects it from signal-induced degradation and inhibits nuclear factor kappaB transcriptional activation
    • Rodriguez M., Thompson J., Hay R. Nuclear retention of IkappaBalpha protects it from signal-induced degradation and inhibits nuclear factor kappaB transcriptional activation. J. Biol. Chem. 274:1999;9108-9115.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9108-9115
    • Rodriguez, M.1    Thompson, J.2    Hay, R.3
  • 72
    • 0032809085 scopus 로고    scopus 로고
    • Nuclear pore localization and nucleocytoplasmic transport of eIF-5A: Evidence for direct interaction with the expor receptor CRM1
    • Rosorius O., Reichart B., Krätzer F., Hegeer P., Dabauvalle M-C., Hauber J. Nuclear pore localization and nucleocytoplasmic transport of eIF-5A: Evidence for direct interaction with the expor receptor CRM1. J. Cell Sci. 112:1999;2369-2380.
    • (1999) J. Cell Sci. , vol.112 , pp. 2369-2380
    • Rosorius, O.1    Reichart, B.2    Krätzer, F.3    Hegeer, P.4    Dabauvalle, M.-C.5    Hauber, J.6
  • 73
    • 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 immunodefficiency virus rev protein
    • Roth J., Dobbelstein M., Freedman D. A., Shenk T., Levine A. J. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodefficiency virus rev protein. EMBO J. 17:1998;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
  • 75
    • 0031780665 scopus 로고    scopus 로고
    • Ubiquitin, E6-AP, and their role in p53 inactivation
    • Scheffner M. Ubiquitin, E6-AP, and their role in p53 inactivation. Pharmacol. Ther. 78:1998;129-139.
    • (1998) Pharmacol. Ther. , vol.78 , pp. 129-139
    • Scheffner, M.1
  • 76
    • 0033545573 scopus 로고    scopus 로고
    • Moving proteins heads for breakdown
    • Scheffner M. Moving proteins heads for breakdown. Nature. 398:1999;103-104.
    • (1999) Nature , vol.398 , pp. 103-104
    • Scheffner, M.1
  • 77
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano M., Lin A. W., McCurrach M. E., Beach D., Lowe S. W. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell. 88:1997;593-602.
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 78
    • 0025203803 scopus 로고
    • Subcellular distribution of the p53 protein during the cell cycle of Balb/C 3T3 cells
    • Shaulsky G., Ben-Ze'ev A., Rotter V. Subcellular distribution of the p53 protein during the cell cycle of Balb/C 3T3 cells. Oncogene. 5:1990a;1707-1711.
    • (1990) Oncogene , vol.5 , pp. 1707-1711
    • Shaulsky, G.1    Ben-Ze'Ev, A.2    Rotter, V.3
  • 79
    • 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., Benzeev A., Rotter V. Nuclear accumulation of p53 protein is mediated by several nuclear-localization signals and plays a role in tumorigenesis. Mol. Cell. Biol. 10:1990b;6565-6577.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6565-6577
    • Shaulsky, G.1    Goldfinger, N.2    Benzeev, A.3    Rotter, V.4
  • 84
    • 0030009042 scopus 로고    scopus 로고
    • The ubiquitin-activating enzyme E1 is phosphorylated and localized to the nucleus in a cell cycle-dependent manner
    • Stephen A. G., Trausch-Azar J. S., Ciechanover A., Schwartz A. L. The ubiquitin-activating enzyme E1 is phosphorylated and localized to the nucleus in a cell cycle-dependent manner. J. Biol. Chem. 271:1996;15608-15614.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15608-15614
    • Stephen, A.G.1    Trausch-Azar, J.S.2    Ciechanover, A.3    Schwartz, A.L.4
  • 85
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking
    • Stommel J. M., Marchenko N. D., Jimenez G. S., Moll U. M., Hope T. J., Wahl G. M. A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking. EMBO J. 18:1999;1660-1672.
    • (1999) EMBO J. , vol.18 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenez, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 87
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao W., Levine A. J. Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc. Natl. Acad. Sci. USA. 96:1999a;3077-3080.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 88
    • 0033536063 scopus 로고    scopus 로고
    • ARF stabilizes p53 by blocking nucleocytoplasmic shuttling of Mdm2
    • ARF stabilizes p53 by blocking nucleocytoplasmic shuttling of Mdm2. Proc. Natl. Acad. Sci. USA. 96:1999b;6937-6941.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 89
    • 0030860911 scopus 로고    scopus 로고
    • Repression of p53-mediated transcription by MDM2: A dual mechanism
    • Thut C. J., Goodrich J. A., Tjian R. Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev. 11:1997;1974-1986.
    • (1997) Genes Dev. , vol.11 , pp. 1974-1986
    • Thut, C.J.1    Goodrich, J.A.2    Tjian, R.3
  • 91
    • 0032525308 scopus 로고    scopus 로고
    • Nuclear export of cyclin B1 and its possible role in DNA damage-induced G2 checkpoint
    • Toyoshima F., Moriguchi T., Wada A., Fukuda M., Nishida E. Nuclear export of cyclin B1 and its possible role in DNA damage-induced G2 checkpoint. EMBO J. 17:1998;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
  • 92
    • 0021990473 scopus 로고
    • Novel antitumour antibiotics, CI-940 (PD 114,720) and PD 114,721. Taxonomy, fermentation and biological activity
    • Tunac J. B., Graham B. D., Dobson W. E., Lenzini M. D. Novel antitumour antibiotics, CI-940 (PD 114,720) and PD 114,721. Taxonomy, fermentation and biological activity. J. Antibiotics. 38:1985;460-465.
    • (1985) J. Antibiotics , vol.38 , pp. 460-465
    • Tunac, J.B.1    Graham, B.D.2    Dobson, W.E.3    Lenzini, M.D.4
  • 93
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • Wada A., Fukuda M., Mishima M., Nishida E. Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 17:1998;1635-1641.
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 94
    • 0028034199 scopus 로고
    • Myc-mediated apoptosis requires wild-type p53 in a manner independent of cell cycle arrest and the ability of p53 to induce p21waf1/cip1
    • Wagner A. J., Kokontis J. M., Hay N. Myc-mediated apoptosis requires wild-type p53 in a manner independent of cell cycle arrest and the ability of p53 to induce p21waf1/cip1. Genes Dev. 8:1994;2817-2830.
    • (1994) Genes Dev. , vol.8 , pp. 2817-2830
    • Wagner, A.J.1    Kokontis, J.M.2    Hay, N.3
  • 95
    • 0030448650 scopus 로고    scopus 로고
    • Identification of a novel p53 functional domain that is necessary for efficient growth suppression
    • Walker K. K., Levine A. J. Identification of a novel p53 functional domain that is necessary for efficient growth suppression. Proc. Natl. Acad. Sci. USA. 93:1996;15335-15340.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15335-15340
    • Walker, K.K.1    Levine, A.J.2
  • 98
    • 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., Wang Y. 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. 4:1997;139-147.
    • (1997) Chem. Biol. , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 99
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X., Bayle J. H., Olson D., Levine A. J. The p53-mdm-2 autoregulatory feedback loop. Genes Dev. 7:1993;1126-1132.
    • (1993) Genes Dev. , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 101
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus impairs both the Rb and p53 tumour suppressor pathways
    • Zhang Y., Xiong Y., Yarbrough G. ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus impairs both the Rb and p53 tumour suppressor pathways. Cell. 92:1998;725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, G.3
  • 102
    • 0033000482 scopus 로고    scopus 로고
    • Mutations in human ARF exon 2 disrupt its nucleolar localisation and impair its ability to block nuclear export of MDM2 and p53
    • Zhang Y., Xiong Y. Mutations in human ARF exon 2 disrupt its nucleolar localisation and impair its ability to block nuclear export of MDM2 and p53. Cell. 3:1999;579-591.
    • (1999) Cell , vol.3 , pp. 579-591
    • Zhang, Y.1    Xiong, Y.2
  • 103
    • 0032192153 scopus 로고    scopus 로고
    • Senescence of human fibroblasts induced by oncogenic Raf
    • Zhu J., Woods D., McMahon M., Bishop J. M. Senescence of human fibroblasts induced by oncogenic Raf. Genes Dev. 12:1998;2997-3007.
    • (1998) Genes Dev. , vol.12 , pp. 2997-3007
    • Zhu, J.1    Woods, D.2    McMahon, M.3    Bishop, J.M.4
  • 104
    • 0343044332 scopus 로고    scopus 로고
    • Effects on normal fibroblasts and neuroblastoma cells of the activation of the p53 response by the nuclear export inhibitor leptomycin B
    • Smart P., Lane E. B., Lane D. P., Midgley C., Vojtesek B., Laín S. Effects on normal fibroblasts and neuroblastoma cells of the activation of the p53 response by the nuclear export inhibitor leptomycin B. Oncogene. 1999.
    • (1999) Oncogene
    • Smart, P.1    Lane, E.B.2    Lane, D.P.3    Midgley, C.4    Vojtesek, B.5    Laín, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.