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Volumn 18, Issue 5, 1998, Pages 2524-2534

Nuclear localization of IκBα is mediated by the second ankyrin repeat: The IκBα ankyrin repeats define a novel class of cis-acting nuclear import sequences

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TRANSCRIPTION FACTOR; DNA BINDING PROTEIN; I KAPPA B; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA; ONCOPROTEIN; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR REL; TRANSCRIPTION FACTOR RELA;

EID: 0031596724     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.5.2524     Document Type: Article
Times cited : (134)

References (78)
  • 1
    • 0028967819 scopus 로고
    • Inducible nuclear expression of newly synthesized IκBα negatively regulates DNA-binding and transcriptional activities of NF-κB
    • Arenzana-Seisdedos, F., J. Thompson, M. S. Rodriguez, F. Bachelerie, D. Thomas, and R. T. Hay. 1995. Inducible nuclear expression of newly synthesized IκBα negatively regulates DNA-binding and transcriptional activities of NF-κB. Mol. Cell. Biol. 15:2689-2696.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2689-2696
    • Arenzana-Seisdedos, F.1    Thompson, J.2    Rodriguez, M.S.3    Bachelerie, F.4    Thomas, D.5    Hay, R.T.6
  • 3
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin, A. S., Jr. 1996. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:649-681.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-681
    • Baldwin Jr., A.S.1
  • 4
    • 0026783210 scopus 로고
    • IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg, A. A., S. M. Ruben, R. I. Scheinman, S. Haskill, C. A. Rosen, and A. S. Baldwin, Jr. 1992. IκB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6:1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin Jr., A.S.6
  • 5
    • 0027332498 scopus 로고
    • The IκB proteins: Multifunctional regulators of Rel/NF-κB in the immune system
    • Beg, A. A., and A. S. Baldwin, Jr. 1993. The IκB proteins: multifunctional regulators of Rel/NF-κB in the immune system. Genes Dev. 7:2064-2070.
    • (1993) Genes Dev. , vol.7 , pp. 2064-2070
    • Beg, A.A.1    Baldwin Jr., A.S.2
  • 6
    • 0028971291 scopus 로고
    • Constitutive NF-κB activation, enhanced granulopoiesis, and neonatal lethality in IκBα deficient mice
    • Beg, A. A., W. C. Sha, R. T. Bronson, and D. Baltimore. 1995. Constitutive NF-κB activation, enhanced granulopoiesis, and neonatal lethality in IκBα deficient mice. Genes Dev. 9:2736-2746.
    • (1995) Genes Dev. , vol.9 , pp. 2736-2746
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Baltimore, D.4
  • 7
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB
    • Beg, A. A., W. C. Sha, R. T. Bronson, S. Ghosh, and D. Baltimore. 1995. Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB. Nature (London) 376:167-170.
    • (1995) Nature (London) , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Ghosh, S.4    Baltimore, D.5
  • 8
    • 0027446955 scopus 로고
    • The oncoprotein Bcl-3 directly transactivates through kappa-B motifs via association with DNA-binding p50B homodimers
    • Bours, V., G. Franzoso, V. Azarenko, S. Park, T. Kanno, K. Brown, and U. Siebenlist. 1993. The oncoprotein Bcl-3 directly transactivates through kappa-B motifs via association with DNA-binding p50B homodimers. Cell 72: 729-739.
    • (1993) Cell , vol.72 , pp. 729-739
    • Bours, V.1    Franzoso, G.2    Azarenko, V.3    Park, S.4    Kanno, T.5    Brown, K.6    Siebenlist, U.7
  • 10
    • 0028986075 scopus 로고
    • Control of IκBα proteolysis by site-specific, signal-induced phosphorylation
    • Brown, K., S. Gerstberger, L. Carlson, G. Franzoso, and U. Siebenlist. 1995. Control of IκBα proteolysis by site-specific, signal-induced phosphorylation. Science 267:1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 12
    • 0029115837 scopus 로고
    • Sequence and characterization of cytoplasmic nuclear import factor p97
    • Chi, N., E. Adam, and S. Adam. 1995. Sequence and characterization of cytoplasmic nuclear import factor p97. J. Cell Biol. 130:265-274.
    • (1995) J. Cell Biol. , vol.130 , pp. 265-274
    • Chi, N.1    Adam, E.2    Adam, S.3
  • 13
    • 0027317849 scopus 로고
    • IκBα can localize in the nucleus but shows no direct transactivation potential
    • Cressman, D. E., and R. Taub. 1993. IκBα can localize in the nucleus but shows no direct transactivation potential. Oncogene 8:2567-2573.
    • (1993) Oncogene , vol.8 , pp. 2567-2573
    • Cressman, D.E.1    Taub, R.2
  • 15
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato, J. A., F. Mercurio, C. Rosette, J. Wu-Li, H. Suyang, S. Ghosh, and M. Karin. 1996. Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16:1295-1304.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • DiDonato, J.A.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 16
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato, J. A., M. Hayakawa, D. M. Rothwarf, E. Zandi, and M. Karin. 1997. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature (London) 388:548-554.
    • (1997) Nature (London) , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 17
    • 0022979325 scopus 로고
    • High mutation rate of a spleen necrosis virus-based retrovirus vector
    • Dougherty, J. P., and H. M. Temin. 1986. High mutation rate of a spleen necrosis virus-based retrovirus vector. Mol. Cell. Biol. 6:4387-4395.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4387-4395
    • Dougherty, J.P.1    Temin, H.M.2
  • 18
    • 0025856717 scopus 로고
    • TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms
    • Ellisen, L. W., J. Bird, D. C. West, A. L. Soreng, T. C. Reynolds, S. D. Smith, and J. Sklar. 1991. TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms. Cell 66:649-661.
    • (1991) Cell , vol.66 , pp. 649-661
    • Ellisen, L.W.1    Bird, J.2    West, D.C.3    Soreng, A.L.4    Reynolds, T.C.5    Smith, S.D.6    Sklar, J.7
  • 19
    • 0029025345 scopus 로고
    • Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes
    • Enenkel, C., G. Blobel, and M. Rexach. 1995. Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. J. Biol. Chem. 270:16499-16502.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16499-16502
    • Enenkel, C.1    Blobel, G.2    Rexach, M.3
  • 20
    • 0028983432 scopus 로고
    • The PEST-like sequence of IκBα is responsible for inhibition of DNA binding but not for cytoplasmic retention of c-Rel or RelA homodimers
    • Ernst, M. K., L. L. Dunn, and N. R. Rice. 1995. The PEST-like sequence of IκBα is responsible for inhibition of DNA binding but not for cytoplasmic retention of c-Rel or RelA homodimers. Mol. Cell. Biol. 15:872-883.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 872-883
    • Ernst, M.K.1    Dunn, L.L.2    Rice, N.R.3
  • 21
    • 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., J. Huber, W. C. Boelens, I. W. Mattaj, and R. Luhrmann. 1995. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82:475-484.
    • (1995) Cell , vol.82 , pp. 475-484
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 22
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., M. Ohno, M. Yoshida, and I. W. Mattaj. 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
  • 24
    • 0030198504 scopus 로고    scopus 로고
    • HIV Rev uses a conserved cellular protein export pathway for nucleocytoplasmic transport of viral RNAs
    • Fritz, C. C., and M. R. Green. 1996. HIV Rev uses a conserved cellular protein export pathway for nucleocytoplasmic transport of viral RNAs. Curr. Biol. 6:848-854.
    • (1996) Curr. Biol. , vol.6 , pp. 848-854
    • Fritz, C.C.1    Green, M.R.2
  • 26
    • 0027078835 scopus 로고
    • IκBα/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. A., S. C. Sun, W. C. Greene, and D. W. Ballard. 1992. IκBα/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. 3:1339-1352.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1339-1352
    • Ganchi, P.A.1    Sun, S.C.2    Greene, W.C.3    Ballard, D.W.4
  • 27
    • 0026486817 scopus 로고
    • cactus, a gene involved in clorsoventral pattern formation of Drosophila, is related to the IκB gene family of vertebrates
    • Geisler, R., A. Bergmann, Y. Hiromi, and C. Nusslein-Volhard. 1992. cactus, a gene involved in clorsoventral pattern formation of Drosophila, is related to the IκB gene family of vertebrates. Cell 71:613-621.
    • (1992) Cell , vol.71 , pp. 613-621
    • Geisler, R.1    Bergmann, A.2    Hiromi, Y.3    Nusslein-Volhard, C.4
  • 28
    • 0022516112 scopus 로고
    • Different localization of the product of the v-rel oncogene in chicken fibroblasts and spleen cells correlates with transformation by REV-T
    • Gilmore, T. D., and H. M. Temin. 1986. Different localization of the product of the v-rel oncogene in chicken fibroblasts and spleen cells correlates with transformation by REV-T. Cell 44:791-800.
    • (1986) Cell , vol.44 , pp. 791-800
    • Gilmore, T.D.1    Temin, H.M.2
  • 29
    • 0023853764 scopus 로고
    • v-Rel oncoproteins in the nucleus and in the cytoplasm transform chicken spleen cells
    • Gilmore, T. D., and H. M. Temin. 1988. v-Rel oncoproteins in the nucleus and in the cytoplasm transform chicken spleen cells. J. Virol. 62:703-714.
    • (1988) J. Virol. , vol.62 , pp. 703-714
    • Gilmore, T.D.1    Temin, H.M.2
  • 32
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina, S., and N. P. Pavletich. 1996. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274:1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 33
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Görlich, D., S. Prehn, R. A. Laskey, and E. Hartmann. 1994. Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79:767-778.
    • (1994) Cell , vol.79 , pp. 767-778
    • Görlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 34
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Görlich, D., S. Kostka, R. Kraft, C. Dingwall, R. Laskey, E. Hartmann, and S. Prehn. 1995. Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr. Biol. 5:383-392.
    • (1995) Curr. Biol. , vol.5 , pp. 383-392
    • Görlich, D.1    Kostka, S.2    Kraft, R.3    Dingwall, C.4    Laskey, R.5    Hartmann, E.6    Prehn, S.7
  • 35
    • 0029059548 scopus 로고
    • Distinct functions for the two importin subunits in nuclear protein import
    • Görlich, D., G. Vogel, A. Mills, E. Hartmann, and R. Laskey. 1995. Distinct functions for the two importin subunits in nuclear protein import. Nature (London) 377:246-248.
    • (1995) Nature (London) , vol.377 , pp. 246-248
    • Görlich, D.1    Vogel, G.2    Mills, A.3    Hartmann, E.4    Laskey, R.5
  • 36
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich, D., and I. W. Mattaj. 1996. Nucleocytoplasmic transport. Science 271:1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 37
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Görlich, D., N. Pante, U. Kutay, U. Aebi, and F. R. Bischoff. 1996. Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J. 15:5584-5594.
    • (1996) EMBO J. , vol.15 , pp. 5584-5594
    • Görlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 38
    • 0029980867 scopus 로고    scopus 로고
    • T cell leukemia-associated Notch/Translocation-associated Notch homologue has IκB-like activity and physically interacts with Nuclear Factor-κB proteins in T cells
    • Guan, E., J. Wang, J. Laborda, M. Norcross, P. A. Baeuerle, and T. Hoffman. 1996. T cell leukemia-associated Notch/Translocation-associated Notch homologue has IκB-like activity and physically interacts with Nuclear Factor-κB proteins in T cells. J. Exp. Med. 183:2025-2032.
    • (1996) J. Exp. Med. , vol.183 , pp. 2025-2032
    • Guan, E.1    Wang, J.2    Laborda, J.3    Norcross, M.4    Baeuerle, P.A.5    Hoffman, T.6
  • 41
    • 0026600367 scopus 로고
    • Direct association of pp40/IκB-β with Rel/NF-κB transcription factors: Role of ankyrin repeats in the inhibition of DNA binding activity
    • Inoue, J. I., L. D. Kerr, D. Rashid, N. Davis, H. R. Bose, Jr., and I. M. Verma. 1992. Direct association of pp40/IκB-β with Rel/NF-κB transcription factors: Role of ankyrin repeats in the inhibition of DNA binding activity. Proc. Natl. Acad. Sci. USA 89:4333-4337.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4333-4337
    • Inoue, J.I.1    Kerr, L.D.2    Rashid, D.3    Davis, N.4    Bose Jr., H.R.5    Verma, I.M.6
  • 42
    • 0028170124 scopus 로고
    • Three NF-κB sites in the IκBα promoter are required for induction of gene expression by TNF-α
    • Ito, C. Y., A. G. Kazantsev, and A. S. Baldwin, Jr. 1994. Three NF-κB sites in the IκBα promoter are required for induction of gene expression by TNF-α. Nucleic Acids Res. 22:3787-3792.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3787-3792
    • Ito, C.Y.1    Kazantsev, A.G.2    Baldwin Jr., A.S.3
  • 43
    • 0021716406 scopus 로고
    • A short amino acid sequence able to specify nuclear location
    • Kalderon, D., B. L. Roberts, W. D. Richardson, and A. E. Smith. 1984. A short amino acid sequence able to specify nuclear location. Cell 39:499-509.
    • (1984) Cell , vol.39 , pp. 499-509
    • Kalderon, D.1    Roberts, B.L.2    Richardson, W.D.3    Smith, A.E.4
  • 44
    • 0025861382 scopus 로고
    • Identification of Ets- and notch-related subunits in GA binding protein
    • La Marco, K., C. C. Thompson, B. P. Byers, E. M. Walton, and S. L. McKnight. 1991. Identification of Ets- and notch-related subunits in GA binding protein. Science 253:789-792.
    • (1991) Science , vol.253 , pp. 789-792
    • La Marco, K.1    Thompson, C.C.2    Byers, B.P.3    Walton, E.M.4    McKnight, S.L.5
  • 45
    • 0027453548 scopus 로고
    • Promoter analysis of the gene encoding the IκBα/MAD-3 inhibitor of NF-κB: Positive regulation by members of the Rel/NF-κB family
    • Le Bail, O., R. Schmidt-Ulrich, and A. Israel. 1993. Promoter analysis of the gene encoding the IκBα/MAD-3 inhibitor of NF-κB: positive regulation by members of the Rel/NF-κB family. EMBO J. 12:5043-5049.
    • (1993) EMBO J. , vol.12 , pp. 5043-5049
    • Le Bail, O.1    Schmidt-Ulrich, R.2    Israel, A.3
  • 46
    • 0030756303 scopus 로고    scopus 로고
    • A new member of the IκB protein family, IκBε, inhibits RelA (p65)-mediated NF-εB transcription
    • Li, Z., and G. J. Nabel. 1997. A new member of the IκB protein family, IκBε, inhibits RelA (p65)-mediated NF-εB transcription. Mol. Cell. Biol. 17:6184-6190.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6184-6190
    • Li, Z.1    Nabel, G.J.2
  • 47
    • 0026740422 scopus 로고
    • The NF-kappa B precursor, p105, contains an internal I kappa B-like inhibitor that preferentially inhibits p50
    • Liou, H. C., G. P. Nolan, S. Ghosh, T. Fujita, and D. Baltimore. 1992. The NF-kappa B precursor, p105, contains an internal I kappa B-like inhibitor that preferentially inhibits p50. EMBO J. 11:3003-3009.
    • (1992) EMBO J. , vol.11 , pp. 3003-3009
    • Liou, H.C.1    Nolan, G.P.2    Ghosh, S.3    Fujita, T.4    Baltimore, D.5
  • 49
    • 0028845313 scopus 로고
    • A nuclear export signal in hnRNP A1: A signal-mediated temperature-dependent nuclear protein export pathway
    • Michael, W. M., M. Choi, and G. Dreyfuss. 1995. A nuclear export signal in hnRNP A1: a signal-mediated temperature-dependent nuclear protein export pathway. Cell 83:415-422.
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.2    Dreyfuss, G.3
  • 50
    • 0026553660 scopus 로고
    • The C-terminus of the NF-κB p50 precursor and an IκB isoform contain transcription activation domains
    • Morin, P. J., and T. D. Gilmore. 1992. The C-terminus of the NF-κB p50 precursor and an IκB isoform contain transcription activation domains. Nucleic Acids Res. 20:2453-2458.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2453-2458
    • Morin, P.J.1    Gilmore, T.D.2
  • 51
    • 0028962511 scopus 로고
    • Previously identified protein of uncertain function is karyopherin a and together with karyopherin β docks import substrate at the nuclear pore complex
    • Moroianu, J., G. Blobel, and A. Radu. 1995. Previously identified protein of uncertain function is karyopherin a and together with karyopherin β docks import substrate at the nuclear pore complex. Proc. Natl. Acad. Sci. USA 92:2008-2011.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2008-2011
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 52
    • 0028983494 scopus 로고
    • 2 bind nuclear localization signal and β interacts with peptide repeat containing nucleoporins
    • 2 bind nuclear localization signal and β interacts with peptide repeat containing nucleoporins. Proc. Natl. Acad. Sci. USA 92:6532-6536.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6532-6536
    • Moroianu, J.1    Hijikata, M.2    Blobel, G.3    Radu, A.4
  • 54
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Signals, mechanisms and regulation
    • Nigg, E. A. 1997. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature (London) 386:779-787.
    • (1997) Nature (London) , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 55
    • 0025324450 scopus 로고
    • The candidate protooncogene bcl-3 is related to genes implicated in cell lineage determination and cell cycle control
    • Ohno, H., G. Takimoto, and T. W. McKeithan. 1990. The candidate protooncogene bcl-3 is related to genes implicated in cell lineage determination and cell cycle control. Cell 60:991-997.
    • (1990) Cell , vol.60 , pp. 991-997
    • Ohno, H.1    Takimoto, G.2    McKeithan, T.W.3
  • 56
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., F. Bachelerie, and C. Dargemont. 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
  • 57
    • 0030611782 scopus 로고    scopus 로고
    • Regulation of IκBβ in WEHI 231 mature B cells
    • Phillips, R. J., and S. Ghosh. 1997. Regulation of IκBβ in WEHI 231 mature B cells. Mol. Cell. Biol. 17:4390-4396.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4390-4396
    • Phillips, R.J.1    Ghosh, S.2
  • 59
    • 0028950991 scopus 로고
    • Identification of a protein complex that is required for nuclear-protein import and mediates docking of import substrate to distinct nucleoporins
    • Radu, A., G. Blobel, and M. S. Moore. 1995. Identification of a protein complex that is required for nuclear-protein import and mediates docking of import substrate to distinct nucleoporins. Proc. Natl. Acad. Sci. USA 92: 1769-1773.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1769-1773
    • Radu, A.1    Blobel, G.2    Moore, M.S.3
  • 60
  • 61
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors and nucleoporins
    • Rexach, M., and G. Blobel. 1995. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors and nucleoporins. Cell 83:683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 62
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins, J., S. M. Dilworth, R. A. Laskey, and C. Dingwall. 1988. Two interdependent basic domains in nucleoplasmin targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell 64:615-623.
    • (1988) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 64
    • 0029916228 scopus 로고
    • PEST-dependent cytoplasmic retention of v-Rel by IκBα: Evidence that IκBα regulates the cellular localization of c-Rel and v-Rel by distinct mechanisms
    • Rottjakob, E. M., S. Sachdev, C. A. Leanna, T. A. McKinsey, and M. Hannink. 1995. PEST-dependent cytoplasmic retention of v-Rel by IκBα: evidence that IκBα regulates the cellular localization of c-Rel and v-Rel by distinct mechanisms. J. Virol. 70:3176-3188.
    • (1995) J. Virol. , vol.70 , pp. 3176-3188
    • Rottjakob, E.M.1    Sachdev, S.2    Leanna, C.A.3    McKinsey, T.A.4    Hannink, M.5
  • 66
    • 0028979595 scopus 로고
    • IκBα mediated inhibition of nuclear transport and DNA-binding by Rel proteins are separable functions: Phosphorylation of C-terminal serine residues of IκBα is specifically required for inhibition of DNA-binding
    • Sachdev, S., E. M. Rottjakob, J. A. Diehl, and M. Hannink. 1995. IκBα mediated inhibition of nuclear transport and DNA-binding by Rel proteins are separable functions: phosphorylation of C-terminal serine residues of IκBα is specifically required for inhibition of DNA-binding. Oncogene 11: 811-823.
    • (1995) Oncogene , vol.11 , pp. 811-823
    • Sachdev, S.1    Rottjakob, E.M.2    Diehl, J.A.3    Hannink, M.4
  • 68
    • 0028804551 scopus 로고
    • Targeted disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses
    • Sha, W. C., H. C. Liou, E. I. Tuomanen, and D. Baltimore. 1995. Targeted disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses. Cell 80:321-330.
    • (1995) Cell , vol.80 , pp. 321-330
    • Sha, W.C.1    Liou, H.C.2    Tuomanen, E.I.3    Baltimore, D.4
  • 69
    • 0028930155 scopus 로고
    • A nuclear localization domain in the hnRNP A1 protein
    • Siomi, H., and G. Dreyfuss. 1995. A nuclear localization domain in the hnRNP A1 protein. J. Cell Biol. 129:551-560.
    • (1995) J. Cell Biol. , vol.129 , pp. 551-560
    • Siomi, H.1    Dreyfuss, G.2
  • 70
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade, K., C. S. Ford, C. Guthrie, and K. Weis. 1997. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90:1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 71
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor κB-α: Evidence for an inducible autoregulatory pathway
    • Sun, S.-C., P. A. Ganchi, D. W. Ballard, and W. C. Greene. 1993. NF-κB controls expression of inhibitor κB-α: evidence for an inducible autoregulatory pathway. Science 259:1912-1915.
    • (1993) Science , vol.259 , pp. 1912-1915
    • Sun, S.-C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 72
    • 0028986194 scopus 로고
    • IκBβ regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J. E., R. J. Phillips, H. Erdjument-Bromage, P. Tempst, and S. Ghosh. 1995. IκBβ regulates the persistent response in a biphasic activation of NF-κB. Cell 80:573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 73
    • 0028978032 scopus 로고
    • Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli
    • Traenckner, E. B., H. L. Pahl, T. Henkel, K. N. Schmidt, S. Wilk, and P. A. Baeuerle. 1995. Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14:2876-2883.
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 74
    • 0030745885 scopus 로고    scopus 로고
    • Distinct functional properties of IκBα and IκBβ
    • Tran, K., M. Merika, and D. Thanos. 1997. Distinct functional properties of IκBα and IκBβ. Mol. Cell. Biol. 17:5386-5399.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5386-5399
    • Tran, K.1    Merika, M.2    Thanos, D.3
  • 75
    • 0028988731 scopus 로고
    • Identification of hSRP1α as a functional receptor for nuclear localization signals
    • Weis, K., I. W. Mattaj, and A. I. Lamond. 1995. Identification of hSRP1α as a functional receptor for nuclear localization signals. Science 268:1049-1053.
    • (1995) Science , vol.268 , pp. 1049-1053
    • Weis, K.1    Mattaj, I.W.2    Lamond, A.I.3
  • 76
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., J. L. Meinkoth, R. Y. Tsien, and S. S. Taylor. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82:463-474.
    • (1995) Cell , vol.82 , pp. 463-474
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 77
    • 0030611595 scopus 로고    scopus 로고
    • IκB kinase-β: NF-κB activation and complex formation with IκB kinase-α and NIK
    • Woronicz, J. D., X. Gao, Z. Cao, M. Rothe, and D. V. Goeddel. 1997. IκB kinase-β: NF-κB activation and complex formation with IκB kinase-α and NIK. Science 278:866-869.
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 78
    • 0027400286 scopus 로고
    • Nuclear uptake control of NF-κB by MAD-3, an IκB protein present in the nucleus
    • Zabel, U., T. Henkel, M. S. Silva, and P. A. Baeuerle. 1993. Nuclear uptake control of NF-κB by MAD-3, an IκB protein present in the nucleus. EMBO J. 12:201-211.
    • (1993) EMBO J. , vol.12 , pp. 201-211
    • Zabel, U.1    Henkel, T.2    Silva, M.S.3    Baeuerle, P.A.4


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