메뉴 건너뛰기




Volumn 95, Issue 6, 1998, Pages 749-758

Structure of an IκBα/NF-κB complex

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR PROTEIN; SYNAPTOTAGMIN; DNA BINDING PROTEIN; HYBRID PROTEIN; I KAPPA B; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA; TRANSCRIPTION FACTOR RELA;

EID: 0032217264     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81698-0     Document Type: Article
Times cited : (735)

References (63)
  • 1
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear-location sequence-mediated binding to the nuclear envelope
    • Adams, E.J., and Adams, S.A. (1994). Identification of cytosolic factors required for nuclear-location sequence-mediated binding to the nuclear envelope. J. Cell Biol. 125, 547-555.
    • (1994) J. Cell Biol. , vol.125 , pp. 547-555
    • Adams, E.J.1    Adams, S.A.2
  • 3
    • 0023724778 scopus 로고
    • IκB: A specific inhibitor of the NF-κB transcription factor
    • Baeuerle, P.A., and Baltimore, D. (1988). IκB: a specific inhibitor of the NF-κB transcription factor. Science 242, 540-546.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 4
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P.A., and Henkel, T. (1994). Function and activation of NF-κB in the immune system. Annu. Rev. Immunol 12, 141-179.
    • (1994) Annu. Rev. Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 5
    • 0032512459 scopus 로고    scopus 로고
    • The structure of GABPα/β: An ETS domain-ankyrin repeat heterodimer bound to DNA
    • Batchelor, A.H., Piper, D.E., de-la-Brousse, F.C., McKnight, S.L., and Wolberger, C. (1998). The structure of GABPα/β: an ETS domain-ankyrin repeat heterodimer bound to DNA. Science 279, 1037-1041.
    • (1998) Science , vol.279 , pp. 1037-1041
    • Batchelor, A.H.1    Piper, D.E.2    De-la-Brousse, F.C.3    McKnight, S.L.4    Wolberger, C.5
  • 6
    • 0026783210 scopus 로고
    • IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg, A.A., Ruben, S.M., Scheinman, R.I., Haskill, S., Rosen, C.A., and Baldwin, A., 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 A., Jr.6
  • 8
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • Bennett, V., and Stenbuck, P.J. (1979). The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature 280, 468-473.
    • (1979) Nature , vol.280 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 9
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?
    • Bork, P. (1993). Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? Proteins: Struct. Funct. Genet. 17, 363-374.
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 363-374
    • Bork, P.1
  • 12
    • 0031455585 scopus 로고    scopus 로고
    • Diverse effects of BCL3 phosphorylation on its modulation of NF-κB p52 homodimer binding to DNA
    • Bundy, D.L., and McKeithan, T.W. (1997). Diverse effects of BCL3 phosphorylation on its modulation of NF-κB p52 homodimer binding to DNA. J. Biol. Chem. 272, 33132-33139.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33132-33139
    • Bundy, D.L.1    McKeithan, T.W.2
  • 13
    • 0001037624 scopus 로고
    • Algorithm for ribbon models of proteins
    • Carson, M., and Bugg, C.E. (1986). Algorithm for ribbon models of proteins. J. Mol. Graph. 4, 121-122.
    • (1986) J. Mol. Graph. , vol.4 , pp. 121-122
    • Carson, M.1    Bugg, C.E.2
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4). (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50, 760-763.
    • (1994) Acta Crystallogr. D. , vol.50 , pp. 760-763
  • 15
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway
    • Chen, Z., Hagler, J., Palombella, V.J., Melandri, F., Scherer, D., Ballard, D., and Maniatis, T. (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
  • 16
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen, F.E., Huang, D.B., Chen, Y.Q., and Ghosh, G. (1998a). Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391, 410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 17
    • 0031964687 scopus 로고    scopus 로고
    • A novel DNA recognition mode by the NF-κB p65 homodimer
    • Chen, Y.Q., Ghosh, S., and Ghosh, G. (1998b). A novel DNA recognition mode by the NF-κB p65 homodimer. Nat. Struct. Biol. 5, 67-73.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 67-73
    • Chen, Y.Q.1    Ghosh, S.2    Ghosh, G.3
  • 18
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin-α
    • Conti, E., Uy, M., Leighton, L., Blobel, G., and Kuriyan, J. (1998). Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin-α. Cell 94, 193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 19
  • 20
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato, J., Mercurio, F., Rosette, C., Wu-Li, J., Suyang, H., Ghosh, S., and Karin, M. (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.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 21
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato, J.A., Hayakawa, M., Rothwarf, D.M., Zandi, E., and Karin, M. (1997). A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 388, 548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 22
    • 0028983432 scopus 로고
    • The PEST-like sequence of IαBκ is responsible for inhibition of DNA binding but not for cytoplasmic retention of c-Rel or RelA homodimers
    • Ernst, M.K., Dunn, L.L., and Rice, N.R. (1995). The PEST-like sequence of IαBκ is responsible for inhibition of DNA binding but not for cytoplasmic retention of c-Rel or RelA homodimers. Mol. Cell Biol. 15, 872-882.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 872-882
    • Ernst, M.K.1    Dunn, L.L.2    Rice, N.R.3
  • 23
    • 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.A., Sun, S.C., Greene, W.C., and Ballard, D.W. (1992). 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, 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
  • 24
    • 0028979479 scopus 로고
    • Structure of NF-κB p50 homodimer bound to a kB site
    • Ghosh, G., van Duyne, G., Ghosh, S., and Sigler, P.B. (1995). Structure of NF-κB p50 homodimer bound to a KB site. Nature 373, 303-310.
    • (1995) Nature , vol.373 , pp. 303-310
    • Ghosh, G.1    Van Duyne, G.2    Ghosh, S.3    Sigler, P.B.4
  • 25
    • 0031897632 scopus 로고    scopus 로고
    • NF-κB and Rel proteins: Evolutionary conserved mediators of immune responses
    • Ghosh, S., May, M.J., and Kopp, E.B. (1998). NF-κB and Rel proteins: evolutionary conserved mediators of immune responses. Annu. Rev. Immunol. 16, 225-260.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 26
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina, S., and Pavletich, N.P. (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
  • 27
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Görlich, D., Prehn, S., Laskey, R.A., and Hartmann, E. (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
  • 28
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison, S.C. (1996). Peptide-surface association: the case of PDZ and PTB domains. Cell 86, 341-343.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 30
    • 0026523562 scopus 로고
    • Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit
    • Henkel, T., Zabel, U., van Zee, K., Muller, J.M., Fanning, E., and Baeuerle, P.A. (1992). Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit. Cell 68, 1121-1133.
    • (1992) Cell , vol.68 , pp. 1121-1133
    • Henkel, T.1    Zabel, U.2    Van Zee, K.3    Muller, J.M.4    Fanning, E.5    Baeuerle, P.A.6
  • 31
    • 0031573470 scopus 로고    scopus 로고
    • The role of DNA in the mechanism of NF-κB dimer formation: Crystal structures of the dimerization domains of the p50 and p65 subunits
    • Huang, D.B., Huxford, T., Chen, Y.Q., and Ghosh, G. (1997). The role of DNA in the mechanism of NF-κB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits. Structures, 1427-1436.
    • (1997) Structures , pp. 1427-1436
    • Huang, D.B.1    Huxford, T.2    Chen, Y.Q.3    Ghosh, G.4
  • 32
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation
    • this issue
    • Huxford, T., Huang, D.-B., Malek, S., and Ghosh, G. (1998). The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell 95, this issue, 759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.-B.2    Malek, S.3    Ghosh, G.4
  • 33
    • 0026600367 scopus 로고
    • Direct association of pp40/IκBβ with rel/NF-κB transcription factors: Role of ankyrin repeats in the inhibition of DNA binding activity
    • Inoue, J., Kerr, L.D., Rashid, D., Davis, N., Bose, H., Jr., and Verma, I.M. (1992). Direct association of pp40/IκBβ 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.1    Kerr, L.D.2    Rashid, D.3    Davis, N.4    Bose H., Jr.5    Verma, I.M.6
  • 34
    • 0028986046 scopus 로고
    • Domain organization of IκBα and sites of interaction with NF-κB p65
    • Jaffray, E., Wood, K.M., and Hay, R.T. (1995). Domain organization of IκBα and sites of interaction with NF-κB p65. Mol. Cell Biol. 15, 2166-2172.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2166-2172
    • Jaffray, E.1    Wood, K.M.2    Hay, R.T.3
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjelgard, M.W. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgard, M.W.4
  • 36
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 37
    • 0026652879 scopus 로고
    • The RxxRxRxxC motif conserved in all Rel/κB proteins is essential for the DMA-binding activity and redox regulation of the v-Rel oncoprotein
    • Kumar, S., Rabson, A.B., and Gelinas, C. (1992). The RxxRxRxxC motif conserved in all Rel/κB proteins is essential for the DMA-binding activity and redox regulation of the v-Rel oncoprotein. Mol. Cell Biol. 12, 3094-3106.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 3094-3106
    • Kumar, S.1    Rabson, A.B.2    Gelinas, C.3
  • 38
    • 0031897457 scopus 로고    scopus 로고
    • The N-terminal domain of IκBα masks the nuclear localization signal(s) of p50 and c-Rel homodimers
    • Latimer, M., Ernst, M.K., Dunn, L.L., Drutskaya, M., and Rice, N.R. (1998). The N-terminal domain of IκBα masks the nuclear localization signal(s) of p50 and c-Rel homodimers. Mol. Cell Biol. 18, 2640-2649.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2640-2649
    • Latimer, M.1    Ernst, M.K.2    Dunn, L.L.3    Drutskaya, M.4    Rice, N.R.5
  • 39
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway
    • Lee, F.S., Hagler, J., Chen, Z.J., and Maniatis, T. (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
  • 42
    • 0031594291 scopus 로고    scopus 로고
    • Distinct domains of IκBα regulate c-Rel in the cytoplasm and in the nucleus
    • Luque, I., and Gélinas, C. (1998). Distinct domains of IκBα regulate c-Rel in the cytoplasm and in the nucleus. Mol. Cell Biol. 18, 1213-1224.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 1213-1224
    • Luque, I.1    Gélinas, C.2
  • 43
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
    • Lux, S.E., John, K.M., and Bennett, V. (1990). Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature 344, 36-42.
    • (1990) Nature , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 45
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 282-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 282-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 46
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N.W. Isaacs, and S. Bailey, eds. (Warrington, England: SERC Daresbury Laboratory)
    • Otwinoski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing, L. Sawyer, N.W. Isaacs, and S. Bailey, eds. (Warrington, England: SERC Daresbury Laboratory).
    • (1993) Data Collection and Processing
    • Otwinoski, Z.1
  • 47
    • 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., Rando, O.J., Goldberg, A.L., and Maniatis, T. (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
  • 48
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu, N.S., and Read, R.J. (1996). Improved structure refinement through maximum likelihood. Acta Crystallogr. A 52, 659-668.
    • (1996) Acta Crystallogr. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 49
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice, L.M., and Brünger, A.T. (1994). Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins: Struct. Funct. Genet. 19, 277-290.
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 50
    • 0026742527 scopus 로고
    • The precursor of NF-κB p50 has IκB-like functions
    • Rice, N.R., MacKichan, M.L., and Israel, A. (1992). The precursor of NF-κB p50 has IκB-like functions. Cell 71, 243-253.
    • (1992) Cell , vol.71 , pp. 243-253
    • Rice, N.R.1    MacKichan, M.L.2    Israel, A.3
  • 55
    • 0027278529 scopus 로고
    • Limited proeolysis and site-directed mutagenesis of the NF-κB p50 DNA-binding subunit
    • Sodeoka, M., Larson, C.J., Chen, L., Lane, W.S., and Verdine, G.L. (1993a). Limited proeolysis and site-directed mutagenesis of the NF-κB p50 DNA-binding subunit. Bioorg. Med. Chem. Lett. 3, 1095.
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 1095
    • Sodeoka, M.1    Larson, C.J.2    Chen, L.3    Lane, W.S.4    Verdine, G.L.5
  • 56
    • 0027156397 scopus 로고
    • A multifunctional plasmid for protein expression by ECPCR: Overproduction of NF-κB p50 DNA-binding subunit
    • Sodeoka, M., Larson, C.J., Chen, L., Leclair, K.P., and Verdine, G.L. (1993b). A multifunctional plasmid for protein expression by ECPCR: overproduction of NF-κB p50 DNA-binding subunit. Bioorg. Med. Chem. Lett. 3, 1089.
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 1089
    • Sodeoka, M.1    Larson, C.J.2    Chen, L.3    Leclair, K.P.4    Verdine, G.L.5
  • 57
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB
    • Traenckner, E.B., Wilk, S., and Baeuerle, P.A. (1994). A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB. EMBO J. 13, 5433-5441.
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traenckner, E.B.1    Wilk, S.2    Baeuerle, P.A.3
  • 58
    • 0031985318 scopus 로고    scopus 로고
    • Crystal structure of the CDK4/6 inhibitory protein p18INK4c provides insights into ankyrin-like repeat structure/function and tumor-derived p16INK4 mutations
    • Venkataramani, R., Swaminathan, K., and Marmorstein, R. (1998). Crystal structure of the CDK4/6 inhibitory protein p18INK4c provides insights into ankyrin-like repeat structure/function and tumor-derived p16INK4 mutations. Nat. Struct. Biol. 5, 74-81.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 74-81
    • Venkataramani, R.1    Swaminathan, K.2    Marmorstein, R.3
  • 60
    • 0025304791 scopus 로고
    • Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA
    • Zabel, U., and Baeuerle, P.A. (1990). Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA. Cell 61, 255-265.
    • (1990) Cell , vol.61 , pp. 255-265
    • Zabel, U.1    Baeuerle, P.A.2
  • 61
    • 0027400286 scopus 로고
    • Nuclear uptake control of NF-κB by MAD-3, an IκB protein present in the nucleus
    • Zabel, U., Henkel, T., Silva, M.S., and Baeuerle, P.A. (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
  • 62
    • 0030991201 scopus 로고    scopus 로고
    • The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism
    • Zhong, H., SuYang, H., Erdjument-Bromage, H., Tempst, P., and Ghosh, S. (1997). The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell 89, 413-424.
    • (1997) Cell , vol.89 , pp. 413-424
    • Zhong, H.1    Suyang, H.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 63
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300
    • Zhong, H., Voll, R.E., and Ghosh, S. (1998). Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol. Cell 1,661-671.
    • (1998) Mol. Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.