메뉴 건너뛰기




Volumn 8, Issue 2, 2003, Pages 78-85

Nuclear transport as a target for cell growth

Author keywords

[No Author keywords available]

Indexed keywords

7 HYDROXYSTAUROSPORINE; APTAMER; IMATINIB; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LEPTOMYCIN B; MIDOSTAURIN; PEPTIDE; PROTEIN KINASE C INHIBITOR; PROTEIN P53; STAUROSPORINE DERIVATIVE; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN;

EID: 0037439329     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(02)02562-X     Document Type: Review
Times cited : (62)

References (74)
  • 1
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R., et al. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110:1990;883-894.
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1
  • 2
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno M., et al. Nucleocytoplasmic transport: the last 200 nanometers. Cell. 92:1998;327-336.
    • (1998) Cell , vol.92 , pp. 327-336
    • Ohno, M.1
  • 3
    • 0034738489 scopus 로고    scopus 로고
    • Diverse nuclear transport pathways regulate cell proliferation and oncogenesis
    • Hood J.K., Silver P.A. Diverse nuclear transport pathways regulate cell proliferation and oncogenesis. Biochim. Biophys. Acta. 1471:2000;M31-M41.
    • (2000) Biochim. Biophys. Acta , vol.1471 , pp. 31-M41
    • Hood, J.K.1    Silver, P.A.2
  • 4
    • 0034789829 scopus 로고    scopus 로고
    • Protein export from the nucleus
    • Ossareh-Nazari B., et al. Protein export from the nucleus. Traffic. 2:2001;684-689.
    • (2001) Traffic , vol.2 , pp. 684-689
    • Ossareh-Nazari, B.1
  • 5
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich D., Kutay U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15:1999;607-660.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 6
    • 0021277559 scopus 로고
    • A new antitumor antibiotic, kazusamycin
    • Umezawa I., et al. A new antitumor antibiotic, kazusamycin. J. Antibiot. (Tokyo). 37:1984;706-711.
    • (1984) J. Antibiot. (Tokyo) , vol.37 , pp. 706-711
    • Umezawa, I.1
  • 7
    • 0021990473 scopus 로고
    • Novel antitumor antibiotics, CI-940 (PD 114720) and PD 114,721: Taxonomy, fermentation and biological activity
    • Tunac J.B., et al. Novel antitumor antibiotics, CI-940 (PD 114720) and PD 114,721: taxonomy, fermentation and biological activity. J. Antibiot. (Tokyo). 38:1985;460-465.
    • (1985) J. Antibiot. (Tokyo) , vol.38 , pp. 460-465
    • Tunac, J.B.1
  • 8
    • 0022647482 scopus 로고
    • In vivo and in vitro anticancer activity of the structurally novel and highly potent antibiotic CI-940 and its hydroxy analog (PD 114,721)
    • Roberts B.J., et al. In vivo and in vitro anticancer activity of the structurally novel and highly potent antibiotic CI-940 and its hydroxy analog (PD 114,721). Cancer Chemother. Pharmacol. 16:1986;95-101.
    • (1986) Cancer Chemother. Pharmacol. , vol.16 , pp. 95-101
    • Roberts, B.J.1
  • 9
    • 0025014776 scopus 로고
    • Effects of leptomycin B on the cell cycle of fibroblasts and fission yeast cells
    • Yoshida M., et al. Effects of leptomycin B on the cell cycle of fibroblasts and fission yeast cells. Exp. Cell Res. 187:1990;150-156.
    • (1990) Exp. Cell Res. , vol.187 , pp. 150-156
    • Yoshida, M.1
  • 10
    • 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., et al. 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
  • 11
    • 0024654957 scopus 로고
    • Higher order chromosome structure is affected by cold-sensitive mutations in a Schizosaccharomyces pombe gene crm1? which encodes a 115-kD protein preferentially localized in the nucleus at its periphery
    • Adachi Y., Yanagida M. Higher order chromosome structure is affected by cold-sensitive mutations in a Schizosaccharomyces pombe gene crm1? which encodes a 115-kD protein preferentially localized in the nucleus at its periphery. J. Cell Biol. 108:1989;1195-1207.
    • (1989) J. Cell Biol. , vol.108 , pp. 1195-1207
    • Adachi, Y.1    Yanagida, M.2
  • 12
    • 0028318159 scopus 로고
    • Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression
    • Nishi K., et al. Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J. Biol. Chem. 269:1994;6320-6324.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6320-6324
    • Nishi, K.1
  • 13
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda M., et al. 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
  • 14
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B., et al. 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
  • 15
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., et al. 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
  • 16
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade K., et al. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell. 90:1997;1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1
  • 17
    • 0032146749 scopus 로고    scopus 로고
    • Leptomycin B inhibition of signal mediated nuclear export by direct binding to CRM1
    • Kudo N., et al. Leptomycin B inhibition of signal mediated nuclear export by direct binding to CRM1. Exp. Cell Res. 242:1998;540-547.
    • (1998) Exp. Cell Res. , vol.242 , pp. 540-547
    • Kudo, N.1
  • 18
    • 0033529866 scopus 로고    scopus 로고
    • Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region
    • Kudo N., et al. Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc. Natl. Acad. Sci. U. S. A. 96:1999;9112-9117.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9112-9117
    • Kudo, N.1
  • 19
    • 0037195181 scopus 로고    scopus 로고
    • A synthetic HIV-1 Rev inhibitor interfering with the CRM1-mediated nuclear export
    • Daelemans D., et al. A synthetic HIV-1 Rev inhibitor interfering with the CRM1-mediated nuclear export. Proc. Natl. Acad. Sci. U. S. A. 99:2002;14440-14445.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14440-14445
    • Daelemans, D.1
  • 20
    • 0029737848 scopus 로고    scopus 로고
    • Phase I trial of elactocin
    • Newlands E.S., et al. Phase I trial of elactocin. Br. J. Cancer. 74:1996;648-649.
    • (1996) Br. J. Cancer , vol.74 , pp. 648-649
    • Newlands, E.S.1
  • 21
    • 0343938848 scopus 로고    scopus 로고
    • Accumulating active p53 in the nucleus by inhibition of nuclear export: A novel strategy to promote the p53 tumor suppressor function
    • Lain S., et al. Accumulating active p53 in the nucleus by inhibition of nuclear export: a novel strategy to promote the p53 tumor suppressor function. Exp. Cell Res. 253:1999;315-324.
    • (1999) Exp. Cell Res. , vol.253 , pp. 315-324
    • Lain, S.1
  • 22
    • 0035122485 scopus 로고    scopus 로고
    • Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase
    • Vigneri P., Wang J.Y. Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase. Nat. Med. 7:2001;228-234.
    • (2001) Nat. Med. , vol.7 , pp. 228-234
    • Vigneri, P.1    Wang, J.Y.2
  • 23
    • 0033231276 scopus 로고    scopus 로고
    • Regulated nuclear localization of stress-responsive factors: How the nuclear trafficking of protein kinases and transcription factors contributes to cell survival
    • Ferrigno P., Silver P.A. Regulated nuclear localization of stress-responsive factors: how the nuclear trafficking of protein kinases and transcription factors contributes to cell survival. Oncogene. 18:1999;6129-6134.
    • (1999) Oncogene , vol.18 , pp. 6129-6134
    • Ferrigno, P.1    Silver, P.A.2
  • 25
    • 0036546501 scopus 로고    scopus 로고
    • NF-κB in cancer: From innocent bystander to major culprit
    • Karin M., et al. NF-κB in cancer: from innocent bystander to major culprit. Nat. Rev. Cancer. 2:2002;301-310.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 301-310
    • Karin, M.1
  • 26
    • 0033596126 scopus 로고    scopus 로고
    • Diverse agents act at multiple levels to inhibit the Rel/NF-κB signal transduction pathway
    • Epinat J.C., Gilmore T.D. Diverse agents act at multiple levels to inhibit the Rel/NF-κB signal transduction pathway. Oncogene. 18:1999;6896-6909.
    • (1999) Oncogene , vol.18 , pp. 6896-6909
    • Epinat, J.C.1    Gilmore, T.D.2
  • 27
    • 0032588186 scopus 로고    scopus 로고
    • NF-κB controls cell growth and differentiation through transcriptional regulation of cyclin D1
    • Guttridge D.C., et al. NF-κB controls cell growth and differentiation through transcriptional regulation of cyclin D1. Mol. Cell. Biol. 19:1999;5785-5799.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5785-5799
    • Guttridge, D.C.1
  • 28
    • 0032588170 scopus 로고    scopus 로고
    • 1-to-S-Phase transition
    • 1-to-S-Phase transition. Mol. Cell. Biol. 19:1999;2690-2698.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2690-2698
    • Hinz, M.1
  • 29
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • Beg A.A., Baltimore D. An essential role for NF-κB in preventing TNF-α-induced cell death. Science. 274:1996;782-784.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 30
    • 0030298294 scopus 로고    scopus 로고
    • Dissenction of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis, while NF-κB activaton prevents cell death
    • Liu Z.G., et al. Dissenction of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis, while NF-κB activaton prevents cell death. Cell. 87:1996;565-576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1
  • 31
    • 0029992609 scopus 로고    scopus 로고
    • Suppression of TNF-α-induced apoptosis by NF-κB
    • Van Antwerp D.J., et al. Suppression of TNF-α-induced apoptosis by NF-κB. Science. 274:1996;784-787.
    • (1996) Science , vol.274 , pp. 784-787
    • Van Antwerp, D.J.1
  • 32
    • 0026523562 scopus 로고
    • Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit
    • Henkel T., et al. Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit. Cell. 68:1992;1121-1133.
    • (1992) Cell , vol.68 , pp. 1121-1133
    • Henkel, T.1
  • 33
    • 0026783210 scopus 로고
    • IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg A.A., et al. IκB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6:1992;1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1
  • 34
    • 0027078835 scopus 로고
    • IκB/MAD-3 masks the nuclear localization signal of NF-κB p65 and requires the transactivation domain to inhibit NF-κB p65 DNA binding
    • Ganchi P.S., et al. IκB/MAD-3 masks the nuclear localization signal of NF-κB p65 and requires the transactivation domain to inhibit NF-κB p65 DNA binding. Mol. Biol. Cell. 3:1992;1339-1352.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1339-1352
    • Ganchi, P.S.1
  • 35
    • 0032575567 scopus 로고    scopus 로고
    • An allosteric drug, o,o′-bismyristoyl thiamine disulfide, suppresses HIV-1 replication through prevention of nuclear translocation of both HIV-1 Tat and NF-κB
    • Shoji S., et al. An allosteric drug, o,o′-bismyristoyl thiamine disulfide, suppresses HIV-1 replication through prevention of nuclear translocation of both HIV-1 Tat and NF-κB. Biochem. Biophys. Res. Commun. 249:1998;745-753.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 745-753
    • Shoji, S.1
  • 36
    • 0037025347 scopus 로고    scopus 로고
    • Inhibition of tumor necrosis factor-α-induced nuclear translocation and activation of NF-κB by dehydroxymehylepoxyquinomicin
    • Ariga A., et al. Inhibition of tumor necrosis factor-α-induced nuclear translocation and activation of NF-κB by dehydroxymehylepoxyquinomicin. J. Biol. Chem. 277:2002;24625-24630.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24625-24630
    • Ariga, A.1
  • 37
    • 0034178264 scopus 로고    scopus 로고
    • Synthesis of NF-κB activation inhibitors derived from epoxyquinomicin C
    • Matsumoto N., et al. Synthesis of NF-κB activation inhibitors derived from epoxyquinomicin C. Bioorg. Med. Chem. Lett. 10:2000;865-869.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 865-869
    • Matsumoto, N.1
  • 38
    • 0034725636 scopus 로고    scopus 로고
    • Truncated form of importin α identified in breast cancer cell inhibits nuclear import of p53
    • Kim I.S., et al. Truncated form of importin α identified in breast cancer cell inhibits nuclear import of p53. J. Biol. Chem. 275:2000;23139-23145.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23139-23145
    • Kim, I.S.1
  • 39
    • 0034669037 scopus 로고    scopus 로고
    • Negative cross-talk between p53 and the glucocorticoid receptor and its role in neuroblastoma cells
    • Sengupta S., et al. Negative cross-talk between p53 and the glucocorticoid receptor and its role in neuroblastoma cells. EMBO J. 19:2000;6051-6064.
    • (2000) EMBO J. , vol.19 , pp. 6051-6064
    • Sengupta, S.1
  • 40
    • 0035370483 scopus 로고    scopus 로고
    • Regulation and function of the p53 tumor suppressor protein
    • Ryan K.M., et al. Regulation and function of the p53 tumor suppressor protein. Curr. Opin. Cell Biol. 13:2001;332-337.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 332-337
    • Ryan, K.M.1
  • 41
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pthway used by the human immunodeficiency virus rev protein
    • Roth J., et al. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pthway used by the human immunodeficiency virus rev protein. EMBO J. 17:1998;554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1
  • 42
    • 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., et al. 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
  • 43
    • 0035827335 scopus 로고    scopus 로고
    • A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation
    • Zhang Y., Xiong Y. A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation. Science. 292:2001;1910-1915.
    • (2001) Science , vol.292 , pp. 1910-1915
    • Zhang, Y.1    Xiong, Y.2
  • 44
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING-finger domain is required to promote p53 nuclear export
    • Geyer R.K., et al. The MDM2 RING-finger domain is required to promote p53 nuclear export. Nat. Cell Biol. 2:2000;569-573.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 569-573
    • Geyer, R.K.1
  • 45
    • 0034282102 scopus 로고    scopus 로고
    • An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
    • Boyd S.D., et al. An intact HDM2 RING-finger domain is required for nuclear exclusion of p53. Nat. Cell Biol. 2:2000;563-568.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 563-568
    • Boyd, S.D.1
  • 46
    • 0034306461 scopus 로고    scopus 로고
    • P53 is associated with cellular microtubules and is transported to the nucleus by dynein
    • Giannakakou P., et al. p53 is associated with cellular microtubules and is transported to the nucleus by dynein. Nat. Cell Biol. 2:2000;709-717.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 709-717
    • Giannakakou, P.1
  • 47
    • 0038298110 scopus 로고    scopus 로고
    • An inhibitor of nuclear export activates the p53 response and induces the localization of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs
    • Lain S., et al. An inhibitor of nuclear export activates the p53 response and induces the localization 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
    • Lain, S.1
  • 48
    • 0034682468 scopus 로고    scopus 로고
    • Activation of p53 in cervical carcinoma cells by small molecules
    • Hietanen S., et al. Activation of p53 in cervical carcinoma cells by small molecules. Proc. Natl. Acad. Sci. U. S. A. 97:2000;8501-8506.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8501-8506
    • Hietanen, S.1
  • 49
    • 0033957661 scopus 로고    scopus 로고
    • The PTEN tumor suppressor protein: An antagonist of phosphoinositide 3-kinase signaling
    • Vazquez F., Sellers W.R. The PTEN tumor suppressor protein: an antagonist of phosphoinositide 3-kinase signaling. Biochim. Biophys. Acta. 1470:2000;M21-M35.
    • (2000) Biochim. Biophys. Acta , vol.1470 , pp. 21-M35
    • Vazquez, F.1    Sellers, W.R.2
  • 51
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-triphosphate
    • Maehama T., Dixon J.E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-triphosphate. J. Biol. Chem. 273:1998;13375-13378.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 52
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta S.R., et al. Cellular survival: a play in three Akts. Genes Dev. 13:1999;2905-2927.
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1
  • 53
    • 0029768753 scopus 로고    scopus 로고
    • A phosphatidylinositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans
    • Morris J.Z., et al. A phosphatidylinositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans. Nature. 382:1996;536-539.
    • (1996) Nature , vol.382 , pp. 536-539
    • Morris, J.Z.1
  • 54
    • 0030813398 scopus 로고    scopus 로고
    • Daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans
    • Kimura K.D., et al. daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans. Science. 277:1997;942-946.
    • (1997) Science , vol.277 , pp. 942-946
    • Kimura, K.D.1
  • 55
    • 0033151613 scopus 로고    scopus 로고
    • A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3-kinase signals that regulate diapause in Caenorhabditis elegans
    • Paradis S., et al. A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3-kinase signals that regulate diapause in Caenorhabditis elegans. Genes Dev. 13:1999;1438-1452.
    • (1999) Genes Dev. , vol.13 , pp. 1438-1452
    • Paradis, S.1
  • 56
    • 15644381754 scopus 로고    scopus 로고
    • Role of translocation in the activation and function of protein kinase B
    • Andjelkovic M., et al. Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272:1997;31515-31524.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31515-31524
    • Andjelkovic, M.1
  • 57
    • 0030727172 scopus 로고    scopus 로고
    • Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase B
    • Meier R., et al. Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase B. J. Biol. Chem. 272:1997;30491-30497.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30491-30497
    • Meier, R.1
  • 58
    • 0033560896 scopus 로고    scopus 로고
    • Direct control of the Forkhead transcription factor AFX by protein kinase B
    • Kops G.J., et al. Direct control of the Forkhead transcription factor AFX by protein kinase B. Nature. 398:1999;630-634.
    • (1999) Nature , vol.398 , pp. 630-634
    • Kops, G.J.1
  • 59
    • 0035034038 scopus 로고    scopus 로고
    • Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX
    • Brownawell A.M., et al. Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX. Mol. Cell. Biol. 21:2001;3534-3546.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3534-3546
    • Brownawell, A.M.1
  • 60
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • Brunet A., et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell. 96:1999;857-868.
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1
  • 61
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • Rena G., et al. Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J. Biol. Chem. 274:1999;17179-17183.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17179-17183
    • Rena, G.1
  • 62
    • 0034462121 scopus 로고    scopus 로고
    • Forkhead transcription factors are critical effectors of cell death and cell cycle arrest downstream of PTEN
    • Nakamura N., et al. Forkhead transcription factors are critical effectors of cell death and cell cycle arrest downstream of PTEN. Mol. Cell. Biol. 20:2000;8969-8982.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8969-8982
    • Nakamura, N.1
  • 63
    • 0033595011 scopus 로고    scopus 로고
    • Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1
    • Biggs W.H., et al. Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. Proc. Natl. Acad. Sci. U. S. A. 96:1999;7421-7426.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7421-7426
    • Biggs, W.H.1
  • 64
    • 0035340356 scopus 로고    scopus 로고
    • The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site
    • Woods Y.L., et al. The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site. Biochem. J. 355:2001;597-607.
    • (2001) Biochem. J. , vol.355 , pp. 597-607
    • Woods, Y.L.1
  • 65
    • 0035135841 scopus 로고    scopus 로고
    • Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)
    • Brunet A., et al. Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol. Cell. Biol. 21:2001;952-965.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 952-965
    • Brunet, A.1
  • 66
    • 0035868368 scopus 로고    scopus 로고
    • Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targeting
    • Rena G., et al. Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targeting. Biochem. J. 354:2001;605-612.
    • (2001) Biochem. J. , vol.354 , pp. 605-612
    • Rena, G.1
  • 67
    • 0037018148 scopus 로고    scopus 로고
    • 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport
    • Brunet A., et al. 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport. J. Cell Biol. 156:2002;817-828.
    • (2002) J. Cell Biol. , vol.156 , pp. 817-828
    • Brunet, A.1
  • 68
    • 0037034928 scopus 로고    scopus 로고
    • Interference with PDK1-Akt survival signaling pathway by UCN-01 (7-hydroxystaurosporine)
    • Sato S., et al. Interference with PDK1-Akt survival signaling pathway by UCN-01 (7-hydroxystaurosporine). Oncogene. 21:2002;1727-1738.
    • (2002) Oncogene , vol.21 , pp. 1727-1738
    • Sato, S.1
  • 69
    • 0035889243 scopus 로고    scopus 로고
    • The phosphotidylinositide 3′-kinase/Akt survival pathway is a target for the anticancer and radiosensitizing agent PKC412, an inhibitor of protein kinase C
    • Tenzer A., et al. The phosphotidylinositide 3′-kinase/Akt survival pathway is a target for the anticancer and radiosensitizing agent PKC412, an inhibitor of protein kinase C. Cancer Res. 61:2001;8203-8210.
    • (2001) Cancer Res. , vol.61 , pp. 8203-8210
    • Tenzer, A.1
  • 70
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • Colas P., et al. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. Nature. 380:1996;548-550.
    • (1996) Nature , vol.380 , pp. 548-550
    • Colas, P.1
  • 71
    • 0032564350 scopus 로고    scopus 로고
    • An artificial cell-cycle inhibitor isolated from a combinatorial library
    • Cohen B.A., et al. An artificial cell-cycle inhibitor isolated from a combinatorial library. Proc. Natl. Acad. Sci. U. S. A. 95:1998;14272-14277.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14272-14277
    • Cohen, B.A.1
  • 72
    • 0033614968 scopus 로고    scopus 로고
    • Inhibition of mammalian cell proliferation by genetically selected peptide aptamers that functionally antagonize E2F activity
    • Fabbrizio E., et al. Inhibition of mammalian cell proliferation by genetically selected peptide aptamers that functionally antagonize E2F activity. Oncogene. 18:1999;4357-4363.
    • (1999) Oncogene , vol.18 , pp. 4357-4363
    • Fabbrizio, E.1
  • 73
    • 0034612296 scopus 로고    scopus 로고
    • Induction of apoptosis in human papillomavirus-positive cancer cell by peptide aptamers targeting the viral E6 oncoprotein
    • Butz K., et al. Induction of apoptosis in human papillomavirus-positive cancer cell by peptide aptamers targeting the viral E6 oncoprotein. Proc. Natl. Acad. Sci. U. S. A. 97:2000;6693-6697.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6693-6697
    • Butz, K.1
  • 74
    • 0034610373 scopus 로고    scopus 로고
    • Targeted modification and transportation of cellular proteins
    • Colas P., et al. Targeted modification and transportation of cellular proteins. Proc. Natl. Acad. Sci. U. S. A. 97:2000;13720-13725.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13720-13725
    • Colas, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.