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Volumn 16, Issue 3, 1996, Pages 899-906

Casein kinase II phosphorylates Iκbα at S-283, S-289, S-293, and T-291 and is required for its degradation

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PHOSPHOPROTEIN;

EID: 0030022860     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.16.3.899     Document Type: Article
Times cited : (175)

References (76)
  • 2
    • 0024294357 scopus 로고
    • Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-κB transcription factor
    • Baeuerle, P. A., and D. Baltimore. 1988. Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-κB transcription factor. Cell 53:211-217
    • (1988) Cell , vol.53 , pp. 211-217
    • Baeuerle, P.A.1    Baltimore, D.2
  • 3
    • 0024759789 scopus 로고
    • A 65-kD subunit of active NF-κB is required for inhibition of NF-κB by IκB
    • Baeuerle, P. A., and D. Baltimore. 1989. A 65-kD subunit of active NF-κB is required for inhibition of NF-κB by IκB. Genes Dev. 3:1689-1698.
    • (1989) Genes Dev. , vol.3 , pp. 1689-1698
    • Baeuerle, P.A.1    Baltimore, D.2
  • 4
    • 0023724778 scopus 로고
    • IκB: A specific inhibitor of the NF-κB transcription factor
    • Baeuerle, P., and D. Baltimore. 1988. IκB: a specific inhibitor of the NF-κB transcription factor. Science 242:540-546.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.1    Baltimore, D.2
  • 5
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P. A., and T. Henkel. 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
  • 7
    • 0027207242 scopus 로고
    • Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of IκBα: A mechanism of NF-κB activation
    • Beg, A. A., T. S. Finco, P. V. Nantermet, and A. S. Baldwin. 1993. Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of IκBα: a mechanism of NF-κB activation. Mol. Cell. Biol. 13:3301-3310.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3301-3310
    • Beg, A.A.1    Finco, T.S.2    Nantermet, P.V.3    Baldwin, A.S.4
  • 8
    • 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. 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.S.6
  • 9
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W. J., P. Van Der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201:110-149
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 10
    • 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
    • Britta-Mareen Traenckner, E., S. Wilk, and P. A. Baeuerle. 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
    • Britta-Mareen Traenckner, E.1    Wilk, S.2    Baeuerle, P.A.3
  • 12
    • 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
  • 13
    • 0027462682 scopus 로고
    • Mutual regulation of the transcriptional activator NF-κB and its inhibitor, IκB-α
    • Brown, K., S. Park, T. Kanno, G. Franzoso, and U. Siebenlist. 1993. Mutual regulation of the transcriptional 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
  • 14
    • 0024147615 scopus 로고
    • Regulating cell growth: Casein kinase II-dependent phosphorylation of nuclear oncoproteins
    • Carroll, D., N. Santoro, and D. Marshak. 1988. Regulating cell growth: casein kinase II-dependent phosphorylation of nuclear oncoproteins. Cold Spring Harbor Symp. Quant. Biol. 53:91-95.
    • (1988) Cold Spring Harbor Symp. Quant. Biol. , vol.53 , pp. 91-95
    • Carroll, D.1    Santoro, N.2    Marshak, D.3
  • 15
    • 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
  • 16
    • 0023739122 scopus 로고
    • Isolation, sequencing, and disruption of the CKA1 gene, encoding the alpha subunit of yeast casein kinase II
    • Chen-Wu, J. L., R. Padmanabha, and C. V. Glover. 1988. Isolation, sequencing, and disruption of the CKA1 gene, encoding the alpha subunit of yeast casein kinase II. Mol. Cell. Biol. 8:4981-4990.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4981-4990
    • Chen-Wu, J.L.1    Padmanabha, R.2    Glover, C.V.3
  • 17
    • 0028965096 scopus 로고
    • Identification and characterization of protein kinase CKII isoforms in HeLa cells
    • Chester, N., I. J. Yu, and D. R. Marshak. 1995. Identification and characterization of protein kinase CKII isoforms in HeLa cells. J. Biol. Chem. 270:7501-7514.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7501-7514
    • Chester, N.1    Yu, I.J.2    Marshak, D.R.3
  • 18
    • 0027212534 scopus 로고
    • Lipopolysaccharide induces phosphorylation of MAD3 and activation of c-rel and related NF-κB proteins in human monocytic THP-1 cells
    • Cordle, S. R., R. Donald, M. A. Read, and J. Hawiger. 1993 Lipopolysaccharide induces phosphorylation of MAD3 and activation of c-rel and related NF-κB proteins in human monocytic THP-1 cells. J. Biol. Chem. 268:11803-11810
    • (1993) J. Biol. Chem. , vol.268 , pp. 11803-11810
    • Cordle, S.R.1    Donald, R.2    Read, M.A.3    Hawiger, J.4
  • 21
    • 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
  • 22
    • 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. 15:872-882.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 872-882
    • Ernst, M.K.1    Dunn, L.L.2    Rice, N.R.3
  • 23
    • 0028172869 scopus 로고
    • Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited by 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 by 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
  • 24
    • 0024748979 scopus 로고
    • The E7 protein of human papillomavirus type 16 is phosphorylated by casein kinase II
    • Firzlaff, J., J. Galloway, R. Eisenman, and B. Luscher. 1989. The E7 protein of human papillomavirus type 16 is phosphorylated by casein kinase II. New Biol. 1:44-53.
    • (1989) New Biol. , vol.1 , pp. 44-53
    • Firzlaff, J.1    Galloway, J.2    Eisenman, R.3    Luscher, B.4
  • 27
    • 0025266685 scopus 로고
    • Activation in vitro of NF-κB by phosphorylation of its inhibitor IκB
    • Ghosh, S., and D. Baltimore. 1990. Activation in vitro of NF-κB by phosphorylation of its inhibitor IκB. Nature (London) 344:678-682
    • (1990) Nature (London) , vol.344 , pp. 678-682
    • Ghosh, S.1    Baltimore, D.2
  • 28
    • 0024467314 scopus 로고
    • The c-Erb-A α-encoded thyroid hormone receptor is phosphorylated in its amino terminal domain by casein kinase II
    • Glineur, C., M. Bailly, and J. Ghysdael. 1989. The c-Erb-A α-encoded thyroid hormone receptor is phosphorylated in its amino terminal domain by casein kinase II. Oncogene 4:1247-1254.
    • (1989) Oncogene , vol.4 , pp. 1247-1254
    • Glineur, C.1    Bailly, M.2    Ghysdael, J.3
  • 30
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han, J., J. D. Lee, L. Bibbs, and R. J. Ulevitch. 1994. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265:808-811.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 32
    • 0019198966 scopus 로고
    • Inhibition of casein kinase II by heparin J
    • Hathaway, G. M., T. H. Lubben, and J. A. Traugh. 1980. Inhibition of casein kinase II by heparin J. Biol. Chem. 255:8038-8041.
    • (1980) Biol. Chem. , vol.255 , pp. 8038-8041
    • Hathaway, G.M.1    Lubben, T.H.2    Traugh, J.A.3
  • 34
    • 0028987382 scopus 로고
    • LMP-1 activates NF-κB by targeting the inhibitory molecule IκBα
    • Herrero, J. A., P. Mathew, and C. V. Paya. 1995 LMP-1 activates NF-κB by targeting the inhibitory molecule IκBα J. Virol. 69:2168-2174
    • (1995) J. Virol. , vol.69 , pp. 2168-2174
    • Herrero, J.A.1    Mathew, P.2    Paya, C.V.3
  • 35
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- And UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Hibi, M., A. Lin, T. Smeal, A. Minden, and M. Karin. 1993. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev. 7:2135-2148.
    • (1993) Genes Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 36
    • 0026590966 scopus 로고
    • IκB-gamma, a 70 kD protein identical to the C-terminal half of p110 NF-κB: A new member of the IκB family
    • Inoue, J. I., L. D. Kerr, A. Kakizuka, and I. M. Verma. 1992. IκB-gamma, a 70 kD protein identical to the C-terminal half of p110 NF-κB: a new member of the IκB family. Cell 68:1109-1120.
    • (1992) Cell , vol.68 , pp. 1109-1120
    • Inoue, J.I.1    Kerr, L.D.2    Kakizuka, A.3    Verma, I.M.4
  • 37
    • 0024358172 scopus 로고
    • A sensitive method tor detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • Kameshita, I., and H. Fujasawa. 1989. A sensitive method tor detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal. Biochem. 183:139-143.
    • (1989) Anal. Biochem. , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujasawa, H.2
  • 39
    • 0025666845 scopus 로고
    • Cyclic-AMP-responsive transcriptional activation of CREB-327 involves interdependent phosphorylated subdomains
    • Lee, C., Y. Yun, J. Hoeffler, and J. Habener. 1990. Cyclic-AMP-responsive transcriptional activation of CREB-327 involves interdependent phosphorylated subdomains. EMBO J. 9:4455-4465
    • (1990) EMBO J. , vol.9 , pp. 4455-4465
    • Lee, C.1    Yun, Y.2    Hoeffler, J.3    Habener, J.4
  • 40
    • 0027482547 scopus 로고
    • Raf-1 protein kinase activates the NF-κB transcription factor by dissociating the cytoplasmic NF-κB-IκB complex
    • Li, S., and J. M. Sedivy. 1993. Raf-1 protein kinase activates the NF-κB transcription factor by dissociating the cytoplasmic NF-κB-IκB complex. Proc. Natl. Acad. Sci. USA 90:9247-9251.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9247-9251
    • Li, S.1    Sedivy, J.M.2
  • 42
    • 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.-C., 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.-C.1    Brown, K.2    Siebenlist, U.3
  • 43
    • 0027618650 scopus 로고
    • Regulation of the NF-κB/rel transcription factor and IκB inhibitor system
    • Liou, H.-C., and D. Baltimore. 1993. Regulation of the NF-κB/rel transcription factor and IκB inhibitor system. Curr. Opin. Cell Biol. 5:477-487.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 477-487
    • Liou, H.-C.1    Baltimore, D.2
  • 44
    • 0026740422 scopus 로고
    • The NF-κB precursor p105 contains an internal IκB-like inhibitor that preferentially inhibits p50
    • Liou, H.-C., G. P. Nolan, S. Ghosh, T. Fujita, and D. Baltimore. 1992. The NF-κB precursor p105 contains an internal IκB-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
  • 45
    • 0025231273 scopus 로고
    • Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation
    • Luscher, B., E. Christenson, D. Litchfield, E. Krebs, and R. Eisenman. 1990. Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation. Nature (London) 344:517-522.
    • (1990) Nature (London) , vol.344 , pp. 517-522
    • Luscher, B.1    Christenson, E.2    Litchfield, D.3    Krebs, E.4    Eisenman, R.5
  • 46
    • 0024446021 scopus 로고
    • Myc oncoproteins are phosphorylated by casein kinase II
    • Luscher, B., E. A. Kuenzel, E. G. Krebs, and R. N. Eisenman. 1989. Myc oncoproteins are phosphorylated by casein kinase II. EMBO J 8:1111-1119.
    • (1989) EMBO J , vol.8 , pp. 1111-1119
    • Luscher, B.1    Kuenzel, E.A.2    Krebs, E.G.3    Eisenman, R.N.4
  • 47
    • 0025313511 scopus 로고
    • Casein kinase II enhances the DNA binding activity of serum response factor
    • Manak, R., N. deBisschop, R. Kris, and R. Prywes. 1990. Casein kinase II enhances the DNA binding activity of serum response factor. Genes Dev. 4:955-967.
    • (1990) Genes Dev. , vol.4 , pp. 955-967
    • Manak, R.1    DeBisschop, N.2    Kris, R.3    Prywes, R.4
  • 48
    • 0028983035 scopus 로고
    • Regulation of IκBα and p105 in monocytes and macrophages persistently infected with human immunodeficiency virus
    • McElhinny, J. A., W. S. MacMorran, G. D. Bren, R. M. Ten, A. Israel, and C. V. Paya. 1995. Regulation of IκBα and p105 in monocytes and macrophages persistently infected with human immunodeficiency virus. J. Virol. 69:1500-1509.
    • (1995) J. Virol. , vol.69 , pp. 1500-1509
    • McElhinny, J.A.1    MacMorran, W.S.2    Bren, G.D.3    Ten, R.M.4    Israel, A.5    Paya, C.V.6
  • 49
    • 0025143302 scopus 로고
    • The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II
    • Meek, D., S. Simon, U. Kikkawa, and W. Eckhart. 1990. The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II. EMBO J. 9:3253-3260.
    • (1990) EMBO J. , vol.9 , pp. 3253-3260
    • Meek, D.1    Simon, S.2    Kikkawa, U.3    Eckhart, W.4
  • 50
    • 0026177469 scopus 로고
    • Phosphorylation of transcripdonal factors and cell-cycle-dependent proteins by casein kinase II
    • Meisner, H., and M. P. Czech. 1991. Phosphorylation of transcripdonal factors and cell-cycle-dependent proteins by casein kinase II. Curr. Opin. Cell Biol. 3:474-483.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 474-483
    • Meisner, H.1    Czech, M.P.2
  • 51
    • 0024582158 scopus 로고
    • Molecular cloning of the human casein kinase II alpha subunit
    • Meisner, H., R. Heller-Harrison, J. Buxton, and M. P. Czech. 1989. Molecular cloning of the human casein kinase II alpha subunit. Biochemistry 28:4072-4076.
    • (1989) Biochemistry , vol.28 , pp. 4072-4076
    • Meisner, H.1    Heller-Harrison, R.2    Buxton, J.3    Czech, M.P.4
  • 52
    • 0023046921 scopus 로고
    • Sequence analysis of phosphoserine-containing peptides: Modification for picomolar sensitivity
    • Meyer, H. E., E. Hoffmann Posorske, H. Korte, and L. M. G. Heilmeyer, Jr. 1986. Sequence analysis of phosphoserine-containing peptides: modification for picomolar sensitivity. FEBS Lett 204:61-66
    • (1986) FEBS Lett , vol.204 , pp. 61-66
    • Meyer, H.E.1    Hoffmann Posorske, E.2    Korte, H.3    Heilmeyer Jr., L.M.G.4
  • 53
    • 0028926561 scopus 로고
    • PEST sequences do not influence substrate susceptibility to calpain proteolysis
    • Molinari, M., J. Anagli, and E. Carafoli. 1995. PEST sequences do not influence substrate susceptibility to calpain proteolysis. J. Biol. Chem. 270: 2032-2035.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2032-2035
    • Molinari, M.1    Anagli, J.2    Carafoli, E.3
  • 54
    • 0025975795 scopus 로고
    • DNA binding and IκB inhibition of the cloned p65 subunit of NF-κB, a rel related polypeptide
    • Nolan, G. P., S. Ghosh, H.-C. Liou, P. Tempst, and D. Baltimore. 1991. DNA binding and IκB inhibition of the cloned p65 subunit of NF-κB, a rel related polypeptide. Cell 64:961-969.
    • (1991) Cell , vol.64 , pp. 961-969
    • Nolan, G.P.1    Ghosh, S.2    Liou, H.-C.3    Tempst, P.4    Baltimore, D.5
  • 55
    • 0025281150 scopus 로고
    • Isolation, sequencing, and disruption of the yeast CKA2 gene casein kinase II is essential for viability in Saccharomyces cerevisiae
    • Padmanabha, R., J. L.-P. Chen-Wu, D. E. Hanna, and C. V. C. Glover. 1990. Isolation, sequencing, and disruption of the yeast CKA2 gene casein kinase II is essential for viability in Saccharomyces cerevisiae. Mol Cell. Biol. 10: 4089-4099
    • (1990) Mol Cell. Biol. , vol.10 , pp. 4089-4099
    • Padmanabha, R.1    Chen-Wu, J.L.-P.2    Hanna, D.E.3    Glover, C.V.C.4
  • 56
    • 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
  • 57
    • 0026770221 scopus 로고
    • NF-κB-dependent induction of the NF-κB p50 subunit gene promoter underlies self-perpetuation of human immunodeficiency virus transcription in monocytic cells
    • Paya, C. V., R. M. Ten, C. Bessia, J. Alcami, R. T. Hay, and J.-L. Virelizier. 1992. NF-κB-dependent induction of the NF-κB p50 subunit gene promoter underlies self-perpetuation of human immunodeficiency virus transcription in monocytic cells. Proc. Natl. Acad. Sci. USA 89:7826-7830
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7826-7830
    • Paya, C.V.1    Ten, R.M.2    Bessia, C.3    Alcami, J.4    Hay, R.T.5    Virelizier, J.-L.6
  • 58
    • 0025113220 scopus 로고
    • Casein kinase 2: An 'eminence grise' in cellular regulation ?
    • Pinna, L. A. 1990. Casein kinase 2: an 'eminence grise' in cellular regulation ? Biochim. Biophys. Acta 1054:267-284.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 59
    • 0028218041 scopus 로고
    • Selective precipitation purification procedure for multiple phosphoseryl-containing peptides and methods for their identification
    • Reynolds, C., P. F. Riley, and J. J. Adamson. 1994 Selective precipitation purification procedure for multiple phosphoseryl-containing peptides and methods for their identification Anal. Biochem. 217:277-284.
    • (1994) Anal. Biochem. , vol.217 , pp. 277-284
    • Reynolds, C.1    Riley, P.F.2    Adamson, J.J.3
  • 60
    • 0027451924 scopus 로고
    • In vivo control of NF-κB activation by IκBα
    • Rice, N. R., and M. K. Ernst. 1994 In vivo control of NF-κB activation by IκBα. EMBO J. 12:4685-4695
    • (1994) EMBO J. , vol.12 , pp. 4685-4695
    • Rice, N.R.1    Ernst, M.K.2
  • 61
    • 0026742527 scopus 로고
    • The precursor of NF-κB has IκB-like functions
    • Rice, N. R., M. L. MacKichan, and A. Israël. 1992. The precursor of NF-κB has IκB-like functions. Cell 71:243-253
    • (1992) Cell , vol.71 , pp. 243-253
    • Rice, N.R.1    MacKichan, M.L.2    Israël, A.3
  • 62
    • 0028986111 scopus 로고
    • Inducible degradation of IκBα in vitro and in vivo requires the acidic C-terminal domain of the protein
    • Rodriguez, M. S., I. Michalopoulos, F. Arenzana-Seisdedos, and R. T. Hay. 1995. Inducible degradation of IκBα in vitro and in vivo requires the acidic C-terminal domain of the protein. Mol. Cell. Biol 15:2413-2419.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 2413-2419
    • Rodriguez, M.S.1    Michalopoulos, I.2    Arenzana-Seisdedos, F.3    Hay, R.T.4
  • 63
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., R. Wells, and M. Rechsteiner. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 64
    • 0026539204 scopus 로고
    • Induction of monocytic differentiation and NF-κB-like activities by human immunodeficiency virus 1 infection of myelomonoblastic cells
    • Roulston, A., M. D'Addario, F. Boulerice, S. Caplan, M. A. Wainberg, and J. Hiscott. 1992. Induction of monocytic differentiation and NF-κB-like activities by human immunodeficiency virus 1 infection of myelomonoblastic cells J. Exp. Med. 175:751-763
    • (1992) J. Exp. Med. , vol.175 , pp. 751-763
    • Roulston, A.1    D'Addario, M.2    Boulerice, F.3    Caplan, S.4    Wainberg, M.A.5    Hiscott, J.6
  • 65
    • 0023423872 scopus 로고
    • Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase II
    • Saxena, A., R. Padmanabha, and C. V. Glover. 1987. Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase II. Mol Cell. Biol 7:3409-3417.
    • (1987) Mol Cell. Biol , vol.7 , pp. 3409-3417
    • Saxena, A.1    Padmanabha, R.2    Glover, C.V.3
  • 66
    • 0027439305 scopus 로고
    • NF-κB p100 (Lyt-10) is a component of H2TF1 and can function as an IκB-like molecule
    • Scheinman, R. I., A. A. Beg, and A. S. Baldwin, Jr. 1993 NF-κB p100 (Lyt-10) is a component of H2TF1 and can function as an IκB-like molecule. Mol. Cell. Biol. 13:6089-6101.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6089-6101
    • Scheinman, R.I.1    Beg, A.A.2    Baldwin Jr., A.S.3
  • 67
    • 0028985936 scopus 로고
    • Casein kinase IIα transgene-induced marine lymphoma: Relation to theiteriosis in cattle
    • Seldin, D. C., and P. Leder. 1995. Casein kinase IIα transgene-induced marine lymphoma: relation to theiteriosis in cattle. Science 267:894-897.
    • (1995) Science , vol.267 , pp. 894-897
    • Seldin, D.C.1    Leder, P.2
  • 68
    • 0022481133 scopus 로고
    • Multiple nuclear factors interact with the immunoglobulin enhancer sequences
    • Sen, R., and D. Baltimore. 1986. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 46:705-716.
    • (1986) Cell , vol.46 , pp. 705-716
    • Sen, R.1    Baltimore, D.2
  • 69
    • 0024355977 scopus 로고
    • In vitro activation and nuclear translocation of NF-κB catalyzed by cyclic AMP-dependent protein kinase and protein kinase C
    • Shirakawa, F., and S. B. Mizel. 1989. In vitro activation and nuclear translocation of NF-κB catalyzed by cyclic AMP-dependent protein kinase and protein kinase C. Mol. Cell. Biol. 9:2424-2430.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2424-2430
    • Shirakawa, F.1    Mizel, S.B.2
  • 70
    • 0023890077 scopus 로고
    • Detection and characterization of the protein encoded by the chicken c-rel protooncogene
    • Simek, S., and N. R. Rice. 1988. Detection and characterization of the protein encoded by the chicken c-rel protooncogene. Oncogene Res. 2:103-119
    • (1988) Oncogene Res. , vol.2 , pp. 103-119
    • Simek, S.1    Rice, N.R.2
  • 71
    • 0027960533 scopus 로고
    • Human T-cell leukemia type I virus Tax activation of NF-κB/Rel involves phosphorylation and degradation of IκBα and RelA (p65)-mediated induction of the c-rel gene
    • Sun, S.-C., J. Elwood, C. Beraud, and W. C. Greene. 1994. Human T-cell leukemia type I virus Tax activation of NF-κB/Rel involves phosphorylation and degradation of IκBα and RelA (p65)-mediated induction of the c-rel gene. Mol. Cell. Biol. 14:7377-7384
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7377-7384
    • Sun, S.-C.1    Elwood, J.2    Beraud, C.3    Greene, W.C.4
  • 72
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor IκB 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 IκB 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
  • 73
    • 0028181243 scopus 로고
    • Autoregulation of the NF-κB transactivator RelA (p65) by multiple cytoplasmic inhibitors containing ankyrin motifs
    • Sun, S.-C., P. A. Ganchi, C. Beraud, D. W. Ballard, and W. C. Greene. 1994 Autoregulation of the NF-κB transactivator RelA (p65) by multiple cytoplasmic inhibitors containing ankyrin motifs. Proc. Natl. Acad. Sci. USA 91:1346-1350.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1346-1350
    • Sun, S.-C.1    Ganchi, P.A.2    Beraud, C.3    Ballard, D.W.4    Greene, W.C.5
  • 74
    • 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.-M., 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.-M.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 75
    • 0029122799 scopus 로고
    • N- and C-terminal sequences control degradation of MAD3 IκBα in response to inducers of NF-κB activity
    • Whiteside, S. T., M. K. Ernst, O. LeBail, C. Laurent-Winter, N. Rice, and A. Israël. 1995. N- and C-terminal sequences control degradation of MAD3 IκBα in response to inducers of NF-κB activity. Mol. Cell. Biol. 15:5339-5345.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5339-5345
    • Whiteside, S.T.1    Ernst, M.K.2    Lebail, O.3    Laurent-Winter, C.4    Rice, N.5    Israël, A.6
  • 76
    • 0025304791 scopus 로고
    • Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA
    • Zabel, U., and P. A. Baeuerle. 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


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