메뉴 건너뛰기




Volumn 17, Issue 10, 1997, Pages 6184-6190

A new member of the Iκb protein family, IκBε, inhibits RelA (p65)- mediated NF-κB transcription

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; DNA BINDING PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; MESSENGER RNA; PHORBOL ESTER; SYNAPTOTAGMIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 0030756303     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.17.10.6184     Document Type: Article
Times cited : (96)

References (49)
  • 1
    • 0027501871 scopus 로고
    • Cross-linking of HLA class II antigens modulates the release of tumor necrosis factor-alpha by the EBV-B lymphoblastoid cell line JY
    • Altomonte, M., C. Pucillo, G. Damante, and M. Maio. 1993. Cross-linking of HLA class II antigens modulates the release of tumor necrosis factor-alpha by the EBV-B lymphoblastoid cell line JY. J. Immunol. 151:5115-5122.
    • (1993) J. Immunol. , vol.151 , pp. 5115-5122
    • Altomonte, M.1    Pucillo, C.2    Damante, G.3    Maio, M.4
  • 2
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle, P. A., and D. Baltimore. 1996. NF-κB: ten years after. Cell 87:13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 3
    • 0030070803 scopus 로고    scopus 로고
    • Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of IκB-α
    • Baldi, L., K. Brown, G. Franzoso, and U. Siebenlist. 1996. Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of IκB-α. J. Biol. Chem. 271:376-379.
    • (1996) J. Biol. Chem. , vol.271 , pp. 376-379
    • Baldi, L.1    Brown, K.2    Franzoso, G.3    Siebenlist, U.4
  • 4
    • 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
  • 6
    • 0027332498 scopus 로고
    • The IκB proteins: Multifunctional regulators of Rel/NF-κB transcription factors
    • Beg, A. A., and A. S. Baldwin, Jr. 1993. The IκB proteins: multifunctional regulators of Rel/NF-κB transcription factors. Genes Dev. 7:2064-2070.
    • (1993) Genes Dev. , vol.7 , pp. 2064-2070
    • Beg, A.A.1    Baldwin Jr., A.S.2
  • 7
    • 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
  • 8
    • 0029843343 scopus 로고    scopus 로고
    • Differential regulation of NF-κB2(p100) processing and control by amino-terminal sequences
    • Betts, J. C., and G. J. Nabel. 1996. Differential regulation of NF-κB2(p100) processing and control by amino-terminal sequences. Mol. Cell. Biol. 16: 6363-6371.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6363-6371
    • Betts, J.C.1    Nabel, G.J.2
  • 11
    • 0028986075 scopus 로고
    • Control of IκB-α proteolysis by site-specific, signal-induced phosphorylation
    • Brown, K., S. Gerstberger, L. Carlson, G. Franzoso, and U. Siebenlist. 1995. Control of IκB-α 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
    • 0027462682 scopus 로고
    • Mutual regulation of the transcription activator NF-κB and its inhibitor IκB-α
    • Brown, K., S. Park, T. Kanno, G. Franzoso, and U. Siebenlist. 1993. Mutual regulation of the transcription activator NF-κB and its inhibitor IκB-α. Proc. Natl. Acad. Sci. USA 90:2532-2536.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2532-2536
    • Brown, K.1    Park, S.2    Kanno, T.3    Franzoso, G.4    Siebenlist, U.5
  • 13
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway
    • Chen, Z., J. Hagler, V. J. Palombella, F. Melandri, D. Scherer, D. Ballard, and T. Maniatis. 1995. Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway. Genes Dev. 9:1586-1597.
    • (1995) Genes Dev. , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 14
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity
    • Chen, Z. J., L. Parent, and T. Maniatis. 1996. Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell 84:853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 16
    • 0029808167 scopus 로고    scopus 로고
    • Basal phosphorylation of the PEST domain in IκBβ regulates its functional interaction with the c-rel proto-oncogene product
    • Chu, Z., T. A. McKinsey, L. Liu, X. Qi, and D. W. Ballard. 1996. Basal phosphorylation of the PEST domain in IκBβ regulates its functional interaction with the c-rel proto-oncogene product. Mol. Cell. Biol. 16:5974-5984.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5974-5984
    • Chu, Z.1    McKinsey, T.A.2    Liu, L.3    Qi, X.4    Ballard, D.W.5
  • 17
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its uhiquitination and degradation
    • DiDonato, J., 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 uhiquitination and degradation. Mol. Cell. Biol. 16:1295-1304.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • DiDonato, J.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 18
    • 0028985190 scopus 로고
    • Phosphorylation of IκBα precedes but is not sufficient for its dissociation from NF-κB
    • DiDonato, J. A., F. Mercurio, and M. Karin. 1995. Phosphorylation of IκBα precedes but is not sufficient for its dissociation from NF-κB. Mol. Cell. Biol. 15:1302-1311.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1302-1311
    • DiDonato, J.A.1    Mercurio, F.2    Karin, M.3
  • 19
    • 0027406040 scopus 로고
    • Dimerization of NF-KB2 with RelA(p65) regulates DNA binding, transcriptional activation, and inhibition by an IκB-α (MAD-3)
    • Duckett, C. S., N. D. Perkins, T. F. Kowalik, R. M. Schmid, E.-S. Huang, A. S. Baldwin, Jr., and G. J. Nabel. 1993 Dimerization of NF-KB2 with RelA(p65) regulates DNA binding, transcriptional activation, and inhibition by an IκB-α (MAD-3). Mol. Cell. Biol. 13:1315-1322.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1315-1322
    • Duckett, C.S.1    Perkins, N.D.2    Kowalik, T.F.3    Schmid, R.M.4    Huang, E.-S.5    Baldwin Jr., A.S.6    Nabel, G.J.7
  • 20
    • 0028172869 scopus 로고
    • Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited bv protease inhibitors
    • Finco, T. S., A. A. Beg, and A. S. Baldwin, Jr. 1994. Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited bv protease inhibitors. Proc. Natl. Acad. Sci. USA 91:11884-11888.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11884-11888
    • Finco, T.S.1    Beg, A.A.2    Baldwin Jr., A.S.3
  • 21
    • 0024451426 scopus 로고
    • Regulation of the IL-2 receptor α-gene: Interaction of a κB binding protein with cell-specific transcription factors
    • Freimuth, W. W., J. M. Depper, and G. J. Nabel. 1989. Regulation of the IL-2 receptor α-gene: interaction of a κB binding protein with cell-specific transcription factors. J. Immunol. 143:3064-3068.
    • (1989) J. Immunol. , vol.143 , pp. 3064-3068
    • Freimuth, W.W.1    Depper, J.M.2    Nabel, G.J.3
  • 23
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway
    • Lee, F. S., J. Hagler, Z. J. Chen, and T. Maniatis. 1997. Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell 88: 213-222.
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.S.1    Hagler, J.2    Chen, Z.J.3    Maniatis, T.4
  • 24
    • 0023900857 scopus 로고
    • HTLV-I transactivator induces interleukin-2 receptor expression through an NF-κB-like factor
    • Leung, K., and G. J. Nabel. 1988. HTLV-I transactivator induces interleukin-2 receptor expression through an NF-κB-like factor. Nature 333:776-778.
    • (1988) Nature , vol.333 , pp. 776-778
    • Leung, K.1    Nabel, G.J.2
  • 25
    • 0029924035 scopus 로고    scopus 로고
    • A glycine-rich region in NF-κB p105 functions as a processing signal for the generation of the p50 subunit
    • Lin, L., and S. Ghosh. 1996. A glycine-rich region in NF-κB p105 functions as a processing signal for the generation of the p50 subunit. Mol. Cell. Biol. 16:2248-2254.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2248-2254
    • Lin, L.1    Ghosh, S.2
  • 26
    • 0029670085 scopus 로고    scopus 로고
    • Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability
    • Lin, R., P. Beauparlant, C. Makris, S. Meloche, and J. Hiscott. 1996. Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability. Mol. Cell. Biol. 16:1401-1409.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1401-1409
    • Lin, R.1    Beauparlant, P.2    Makris, C.3    Meloche, S.4    Hiscott, J.5
  • 27
    • 0028981050 scopus 로고
    • Activation of NF-κB requires proteolysis of the inhibitor IκB-α: Signal induced phosphorylation of IκB-α alone does not release active NF-κB
    • Lin, Y., K. Brown, and U. Siebenlist. 1995. Activation of NF-κB requires proteolysis of the inhibitor IκB-α: signal induced phosphorylation of IκB-α alone does not release active NF-κB. Proc. Natl. Acad. Sci. USA 92:552-556.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 552-556
    • Lin, Y.1    Brown, K.2    Siebenlist, U.3
  • 28
    • 0026740422 scopus 로고
    • The NF-kappa B p50 precursor, p 105, 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 p50 precursor, p 105, 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
  • 29
    • 0030022860 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates IκBα at S-283, S-289, S-293, and T-291 and is required for its degradation
    • McElhinny, J. A., S. A. Trushin, G. D. Bren, N. Chester, and C. V. Paya. 1996. Casein kinase II phosphorylates IκBα at S-283, S-289, S-293, and T-291 and is required for its degradation. Mol. Cell. Biol. 16:899-906.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 899-906
    • McElhinny, J.A.1    Trushin, S.A.2    Bren, G.D.3    Chester, N.4    Paya, C.V.5
  • 30
    • 0029664659 scopus 로고    scopus 로고
    • Inactivation of IκBβ by the Tax protein of human T-cell leukemia virus type 1: A potential mechanism for constitutive induction of NF-κB
    • McKinsey, T. A., J. A. Brockman, D. C. Scherer, S. W. Al-Murrani, P. L. Green, and D. W. Ballard. 1996. Inactivation of IκBβ by the Tax protein of human T-cell leukemia virus type 1: a potential mechanism for constitutive induction of NF-κB. Mol. Cell. Biol. 16:2083-2090.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2083-2090
    • McKinsey, T.A.1    Brockman, J.A.2    Scherer, D.C.3    Al-Murrani, S.W.4    Green, P.L.5    Ballard, D.W.6
  • 31
    • 0028557348 scopus 로고
    • Tumor necrosis factor alpha-induced phosphorylation of IκB-α is a signal for its degradation but not dissociation from NF-κB
    • Miyamoto, S., M. Maki, M. J. Schmitt, M. Hatanaka, and I. M. Verma. 1994. Tumor necrosis factor alpha-induced phosphorylation of IκB-α is a signal for its degradation but not dissociation from NF-κB. Proc. Natl. Acad. Sci. USA 91:12740-12744.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12740-12744
    • Miyamoto, S.1    Maki, M.2    Schmitt, M.J.3    Hatanaka, M.4    Verma, I.M.5
  • 33
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. 1994. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 34
    • 0027983512 scopus 로고
    • An interaction between the DNA-binding domains of RelA(p65) and Sp1 mediates human immunodeficiency virus gene activation
    • Perkins, N. D., A. B. Agranoff, E. Pascal, and G. J. Nabel. 1994. An interaction between the DNA-binding domains of RelA(p65) and Sp1 mediates human immunodeficiency virus gene activation. Mol. Cell. Biol. 14:6570-6583.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6570-6583
    • Perkins, N.D.1    Agranoff, A.B.2    Pascal, E.3    Nabel, G.J.4
  • 35
    • 0027209915 scopus 로고
    • A cooperative interaction between NF-κB and Sp1 is required for HIV-1 enhancer activation
    • Perkins, N. D., N. L. Edwards, C. S. Duckett, A. B. Agranoff, R. M. Schmid, and G. J. Nabel. 1993. A cooperative interaction between NF-κB and Sp1 is required for HIV-1 enhancer activation. EMBO J. 12:3551-3558.
    • (1993) EMBO J. , vol.12 , pp. 3551-3558
    • Perkins, N.D.1    Edwards, N.L.2    Duckett, C.S.3    Agranoff, A.B.4    Schmid, R.M.5    Nabel, G.J.6
  • 36
    • 0029665597 scopus 로고    scopus 로고
    • Constitutive phosphorylation of IκBα by casein kinase II occurs preferentially at serine 293: Requirement for degradation of free IκBα
    • Schwarz, E. M., D. Van Antwerp, and I. M. Verma. 1996. Constitutive phosphorylation of IκBα by casein kinase II occurs preferentially at serine 293: requirement for degradation of free IκBα. Mol. Cell. Biol. 16:3554-3559.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3554-3559
    • Schwarz, E.M.1    Van Antwerp, D.2    Verma, I.M.3
  • 37
    • 0031041284 scopus 로고    scopus 로고
    • NFκB/IκB proteins: Their role in cell growth, differentation, and development
    • Siebenlist, U. 1997. NFκB/IκB proteins: their role in cell growth, differentation, and development. Biochim. Biophys. Acta 1332:7-13.
    • (1997) Biochim. Biophys. Acta , vol.1332 , pp. 7-13
    • Siebenlist, U.1
  • 39
    • 0030026562 scopus 로고    scopus 로고
    • Both amino- and carboxylterminal sequences within IκBα regulate its inducible degradation
    • Sun, S.-C., J. Elwood, and W. C. Greene. 1996. Both amino- and carboxylterminal sequences within IκBα regulate its inducible degradation. Mol. Cell. Biol. 16:1058-1065.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1058-1065
    • Sun, S.-C.1    Elwood, J.2    Greene, W.C.3
  • 40
    • 0027168447 scopus 로고
    • NF-kappa B controls expression of inhibitor 1 kappa B alpha: Evidence of an inducible autoregulatory pathway
    • Sun, S.-C., P. A. Ganchi, D. W. Ballard, and W. C. Greene. 1993. NF-kappa B controls expression of inhibitor 1 kappa B alpha: evidence of 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
  • 41
    • 0029814276 scopus 로고    scopus 로고
    • Role of unphosphorylated, newly synthesized IκBβ in persistent activation of NF-κB
    • Suyang, H., R. Phillips, I. Douglas, and S. Ghosh. 1996. Role of unphosphorylated, newly synthesized IκBβ in persistent activation of NF-κB. Mol. Cell. Biol. 16:5444-5449.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5444-5449
    • Suyang, H.1    Phillips, R.2    Douglas, I.3    Ghosh, S.4
  • 42
    • 0026508987 scopus 로고
    • The characterization of the promoter of the gene encoding the p50 subunit of NF-kappa B indicates that it participates in its own regulation
    • Ten, R. M., C. V. Paya, N. Israel, O. LeBail, M. G. Mattel, J. L. Virelizier, P. Kourilsky, and A. Israel. 1992. The characterization of the promoter of the gene encoding the p50 subunit of NF-kappa B indicates that it participates in its own regulation. EMBO J. 11:195-203.
    • (1992) EMBO J. , vol.11 , pp. 195-203
    • Ten, R.M.1    Paya, C.V.2    Israel, N.3    LeBail, O.4    Mattel, M.G.5    Virelizier, J.L.6    Kourilsky, P.7    Israel, A.8
  • 43
    • 0029932857 scopus 로고    scopus 로고
    • CD28-mediated cytotoxicity by the human leukemic NK cell line YT involves tyrosine phosphorylation, activation of phosphatidylinositol 3-kinase, and protein kinase C
    • Teng, J. M., X. R. Liu, G. B. Mills, and B. Dupont. 1996. CD28-mediated cytotoxicity by the human leukemic NK cell line YT involves tyrosine phosphorylation, activation of phosphatidylinositol 3-kinase, and protein kinase C. J. Immunol. 156:3222-3232.
    • (1996) J. Immunol. , vol.156 , pp. 3222-3232
    • Teng, J.M.1    Liu, X.R.2    Mills, G.B.3    Dupont, B.4
  • 44
    • 0028986194 scopus 로고
    • IκB-β 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. IκB-β 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
  • 45
    • 0028978032 scopus 로고
    • Phosphorylation of human IkB-α on serines 32 and 36 controls IκB-α 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 IkB-α on serines 32 and 36 controls IκB-α 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
  • 47
    • 0028281782 scopus 로고
    • Expression and tumorigenicity of the Epstein-Barr virus BARF1 gene in human Louckes B-lymphocyte cell line
    • Wei, M. X., J. C. Moulin, G. Decaussin, F. Berger, and T. Ooka. 1994. Expression and tumorigenicity of the Epstein-Barr virus BARF1 gene in human Louckes B-lymphocyte cell line. Cancer Res. 54:1843-1848.
    • (1994) Cancer Res. , vol.54 , pp. 1843-1848
    • Wei, M.X.1    Moulin, J.C.2    Decaussin, G.3    Berger, F.4    Ooka, T.5
  • 48
    • 0030899121 scopus 로고    scopus 로고
    • I kappa B epsilon, a novel member of the IκB family, controls Rela and cRel NF-κB activity
    • Whiteside, S. T., J. Epinat, N. R. Rice, and A. Israel. 1997. I kappa B epsilon, a novel member of the IκB family, controls RelA and cRel NF-κB activity. EMBO J. 16:1413-1426.
    • (1997) EMBO J. , vol.16 , pp. 1413-1426
    • Whiteside, S.T.1    Epinat, J.2    Rice, N.R.3    Israel, A.4
  • 49
    • 0028934819 scopus 로고
    • Regulation of human retroviral latency by the NF-κB/IκB family: Inhibition of human immunodeficiency virus replication by IκB through a Rev-dependent mechanism
    • Wu, B., C. Woffendin, C. S. Duckett, T. Ohno, and G. J. Nabel. 1995. Regulation of human retroviral latency by the NF-κB/IκB family: inhibition of human immunodeficiency virus replication by IκB through a Rev-dependent mechanism. Proc. Natl. Acad. Sci. USA 92:1480-1484.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1480-1484
    • Wu, B.1    Woffendin, C.2    Duckett, C.S.3    Ohno, T.4    Nabel, G.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.