메뉴 건너뛰기




Volumn 64, Issue 5-6, 2002, Pages 963-970

Regulation of the transcriptional activity of the nuclear factor-κB p65 subunit

Author keywords

Gene regulation; Histone modification; MSK; NF B; Phosphorylation; Transcriptional activity

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTRANSFERASE; PROTEIN SUBUNIT; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOTAGMIN; WORTMANNIN;

EID: 0036710479     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(02)01161-9     Document Type: Article
Times cited : (289)

References (85)
  • 1
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin M., Ben-Neriah Y. Phosphorylation meets ubiquitination: The control of NF-κB activity. Annu. Rev. Immunol. 18:2000;621-663.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 2
    • 0034283837 scopus 로고    scopus 로고
    • The Rel/NF-κB family: Friend and foe
    • Perkins N.D. The Rel/NF-κB family: Friend and foe. Trends Biochem. Sci. 25:2000;434-440.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 434-440
    • Perkins, N.D.1
  • 3
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl H.L. Activators and target genes of Rel/NF-κB transcription factors. Oncogene. 18:1999;6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 4
    • 0033595892 scopus 로고    scopus 로고
    • The Rel/NF-κB signal transduction pathway: Introduction
    • Gilmore T.D. The Rel/NF-κB signal transduction pathway: Introduction. Oncogene. 18:1999;6842-6844.
    • (1999) Oncogene , vol.18 , pp. 6842-6844
    • Gilmore, T.D.1
  • 5
    • 0035976962 scopus 로고    scopus 로고
    • IκBβ but not IκBα functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both NF-κB nuclear localization sequences in resting cells
    • Malek S., Chen Y., Huxford T., Ghosh G. IκBβ but not IκBα functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both NF-κB nuclear localization sequences in resting cells. J. Biol. Chem. 276:2001;45225-45235.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45225-45235
    • Malek, S.1    Chen, Y.2    Huxford, T.3    Ghosh, G.4
  • 6
    • 0035896543 scopus 로고    scopus 로고
    • IκB family members function by different mechanisms
    • Tam W.F., Sen R. IκB family members function by different mechanisms. J. Biol. Chem. 276:2001;7701-7704.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7701-7704
    • Tam, W.F.1    Sen, R.2
  • 7
    • 0033486033 scopus 로고    scopus 로고
    • An N-terminal nuclear export signal is required for the nucleocytoplasmic shuttling of IκBα
    • Johnson C., Van Antwerp D., Hope T.J. An N-terminal nuclear export signal is required for the nucleocytoplasmic shuttling of IκBα EMBO J. 18:1999;6682-6693.
    • (1999) EMBO J. , vol.18 , pp. 6682-6693
    • Johnson, C.1    Van Antwerp, D.2    Hope, T.J.3
  • 8
    • 0033953587 scopus 로고    scopus 로고
    • A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes
    • Huang T.T., Kudo N., Yoshida M., Miyamoto S. A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes. Proc. Natl. Acad. Sci. U.S.A. 97:2000;1014-1019.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1014-1019
    • Huang, T.T.1    Kudo, N.2    Yoshida, M.3    Miyamoto, S.4
  • 9
    • 0034175930 scopus 로고    scopus 로고
    • The IKK complex: An integrator of all signals that activate NF-κB?
    • Israel A. The IKK complex: An integrator of all signals that activate NF-κB? Trends Cell Biol. 10:2000;129-133.
    • (2000) Trends Cell Biol. , vol.10 , pp. 129-133
    • Israel, A.1
  • 10
    • 0033595893 scopus 로고    scopus 로고
    • How NF-κB is activated: The role of the IκB kinase (IKK) complex
    • Karin M. How NF-κB is activated: The role of the IκB kinase (IKK) complex. Oncogene. 18:1999;6867-6874.
    • (1999) Oncogene , vol.18 , pp. 6867-6874
    • Karin, M.1
  • 11
    • 0035282213 scopus 로고    scopus 로고
    • IκB-independent control of NF-κB activity by modulatory phosphorylations
    • Schmitz M.L., Bacher S., Kracht M. IκB-independent control of NF-κB activity by modulatory phosphorylations. Trends Biochem. Sci. 26:2001;186-190.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 186-190
    • Schmitz, M.L.1    Bacher, S.2    Kracht, M.3
  • 12
    • 0032491485 scopus 로고    scopus 로고
    • Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-α is mediated through phosphorylation of RelA/p65 on serine 529
    • Wang D., Baldwin A.S. Jr. Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-α is mediated through phosphorylation of RelA/p65 on serine 529. J. Biol. Chem. 273:1998;29411-29416.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29411-29416
    • Wang, D.1    Baldwin, A.S.2
  • 13
    • 0034693133 scopus 로고    scopus 로고
    • Tumor necrosis factor α-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II
    • Wang D., Westerheide S.D., Hanson J.L., Baldwin A.S. Jr. Tumor necrosis factor α-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II. J. Biol. Chem. 275:2000;32592-32597.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32592-32597
    • Wang, D.1    Westerheide, S.D.2    Hanson, J.L.3    Baldwin, A.S.4
  • 14
    • 0031437893 scopus 로고    scopus 로고
    • Activation of nuclear transcription factor NF-κB by interleukin-1 is accompanied by casein kinase II-mediated phosphorylation of the p65 subunit
    • Bird T.A., Schooley K., Dower S.K., Hagen H., Virca G.D. Activation of nuclear transcription factor NF-κB by interleukin-1 is accompanied by casein kinase II-mediated phosphorylation of the p65 subunit. J. Biol. Chem. 272:1997;32606-32612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32606-32612
    • Bird, T.A.1    Schooley, K.2    Dower, S.K.3    Hagen, H.4    Virca, G.D.5
  • 15
    • 0032589462 scopus 로고    scopus 로고
    • IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain
    • Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W. IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain. J. Biol. Chem. 274:1999;30353-30356.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 16
    • 0029058962 scopus 로고
    • Transactivation domain 2 (TA2) of p65 NF-κB: Similarity to TA1 and phorbol ester-stimulated activity and phosphorylation in intact cells
    • Schmitz M.L., dos Santos Silva M.A., Baeuerle P.A. Transactivation domain 2 (TA2) of p65 NF-κB: Similarity to TA1 and phorbol ester-stimulated activity and phosphorylation in intact cells. J. Biol. Chem. 270:1995;15576-15584.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15576-15584
    • Schmitz, M.L.1    Dos Santos Silva, M.A.2    Baeuerle, P.A.3
  • 18
    • 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., Ghosh S. The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell. 89:1997;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
  • 21
    • 0035930630 scopus 로고    scopus 로고
    • Protein phosphatase 2A interacts with and directly dephosphorylates RelA
    • Yang J., Fan G.H., Wadzinski B.E., Sakurai H., Richmond A. Protein phosphatase 2A interacts with and directly dephosphorylates RelA. J. Biol. Chem. 276:2001;47828-47833.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47828-47833
    • Yang, J.1    Fan, G.H.2    Wadzinski, B.E.3    Sakurai, H.4    Richmond, A.5
  • 22
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • Ashburner B.P., Westerheide S.D., Baldwin A.S. Jr. The p65 (RelA) subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. Mol. Cell Biol. 21:2001;7065-7077.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin, A.S.3
  • 23
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-κB action regulated by reversible acetylation
    • Chen L., Fischle W., Verdin E., Greene W.C. Duration of nuclear NF-κB action regulated by reversible acetylation. Science. 293:2001;1653-1657.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 24
    • 0033517189 scopus 로고    scopus 로고
    • NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes O.N., Mayo L.D., Gustin J.A., Pfeffer S.R., Pfeffer L.M., Donner D.B. NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature. 401:1999;82-85.
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5    Donner, D.B.6
  • 26
    • 0034603994 scopus 로고    scopus 로고
    • Wortmannin inhibits activation of nuclear transcription factors NF-κB and activated protein-1 induced by lipopolysaccharide and phorbol ester
    • Manna S.K., Aggarwal B.B. Wortmannin inhibits activation of nuclear transcription factors NF-κB and activated protein-1 induced by lipopolysaccharide and phorbol ester. FEBS Lett. 473:2000;113-118.
    • (2000) FEBS Lett. , vol.473 , pp. 113-118
    • Manna, S.K.1    Aggarwal, B.B.2
  • 27
    • 0033038491 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-κB p65/RelA subunit
    • Sizemore N., Leung S., Stark G.R. Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-κB p65/RelA subunit. Mol. Cell Biol. 19:1999;4798-4805.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4798-4805
    • Sizemore, N.1    Leung, S.2    Stark, G.R.3
  • 28
    • 0033961280 scopus 로고    scopus 로고
    • Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB
    • Madrid L.V., Wang C.Y., Guttridge D.C., Schottelius A.J., Baldwin A.S. Jr., Mayo M.W. Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB. Mol. Cell Biol. 20:2000;1626-1638.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1626-1638
    • Madrid, L.V.1    Wang, C.Y.2    Guttridge, D.C.3    Schottelius, A.J.4    Baldwin, A.S.5    Mayo, M.W.6
  • 29
    • 0035379555 scopus 로고    scopus 로고
    • Akt stimulates the transactivation potential of the RelA/p65 subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38
    • Madrid L.V., Mayo M.W., Reuther J.Y., Baldwin A.S. Jr. Akt stimulates the transactivation potential of the RelA/p65 subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38. J. Biol. Chem. 276:2001;18934-18940.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin, A.S.4
  • 30
    • 0037039665 scopus 로고    scopus 로고
    • Distinct roles of the IκB kinase a and b subunits in liberating NF-κB from IκB and in phosphorylating the p65 subunit of NF-κB
    • Sizemore N., Lerner N., Dombrowski N., Sakuria H., Stark G.R. Distinct roles of the IκB kinase a and b subunits in liberating NF-κB from IκB and in phosphorylating the p65 subunit of NF-κB. J. Biol. Chem. 277:2002;3863-3869.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3863-3869
    • Sizemore, N.1    Lerner, N.2    Dombrowski, N.3    Sakuria, H.4    Stark, G.R.5
  • 31
    • 0034720896 scopus 로고    scopus 로고
    • Kinase regulation in inflammatory response
    • Delhase M., Li N., Karin M. Kinase regulation in inflammatory response. Nature. 406:2000;367-368.
    • (2000) Nature , vol.406 , pp. 367-368
    • Delhase, M.1    Li, N.2    Karin, M.3
  • 32
    • 0034685915 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt pathway, activated by tumor necrosis factor or interleukin-1 inhibits apoptosis but does not activate NF-κB in human endothelial cells
    • Madge L.A., Pober J.S. A phosphatidylinositol 3-kinase/Akt pathway, activated by tumor necrosis factor or interleukin-1 inhibits apoptosis but does not activate NF-κB in human endothelial cells. J. Biol. Chem. 275:2000;15458-15465.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15458-15465
    • Madge, L.A.1    Pober, J.S.2
  • 33
    • 0034623313 scopus 로고    scopus 로고
    • PDGF-induced Akt phosphorylation does not activate NF-κB in human vascular smooth muscle cells and fibroblasts
    • Rauch B.H., Weber A., Braun M., Zimmermann N., Schror K. PDGF-induced Akt phosphorylation does not activate NF-κB in human vascular smooth muscle cells and fibroblasts. FEBS Lett. 481:2000;3-7.
    • (2000) FEBS Lett. , vol.481 , pp. 3-7
    • Rauch, B.H.1    Weber, A.2    Braun, M.3    Zimmermann, N.4    Schror, K.5
  • 34
    • 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., Ghosh S. Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol. Cell. 1:1998;661-671.
    • (1998) Mol. Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3
  • 35
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38 and may mediate activation of CREB
    • Deak M., Clifton A.D., Lucocq L.M., Alessi D.R. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38 and may mediate activation of CREB. EMBO J. 17:1998;4426-4441.
    • (1998) EMBO J. , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 36
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase
    • Thomson S., Clayton A.L., Hazzalin C.A., Rose S., Barratt M.J., Mahadevan L.C. The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. EMBO J. 18:1999;4779-4793.
    • (1999) EMBO J. , vol.18 , pp. 4779-4793
    • Thomson, S.1    Clayton, A.L.2    Hazzalin, C.A.3    Rose, S.4    Barratt, M.J.5    Mahadevan, L.C.6
  • 37
    • 0032491440 scopus 로고    scopus 로고
    • RSK-B a novel ribosomal S6 kinase family member is a CREB kinase under dominant control of p38α mitogen-activated protein kinase (p38αMAPK)
    • Pierrat B., Correia J.S., Mary J.L., Tomas Zuber M., Lesslauer W. RSK-B a novel ribosomal S6 kinase family member is a CREB kinase under dominant control of p38α mitogen-activated protein kinase (p38αMAPK). J. Biol. Chem. 273:1998;29661-29671.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29661-29671
    • Pierrat, B.1    Correia, J.S.2    Mary, J.L.3    Tomas Zuber, M.4    Lesslauer, W.5
  • 38
    • 0040777392 scopus 로고    scopus 로고
    • Control sites of ribosomal S6 kinase B and persistent activation through tumor necrosis factor
    • Tomas-Zuber M., Mary J.L., Lesslauer W. Control sites of ribosomal S6 kinase B and persistent activation through tumor necrosis factor. J. Biol. Chem. 275:2000;23549-23558.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23549-23558
    • Tomas-Zuber, M.1    Mary, J.L.2    Lesslauer, W.3
  • 42
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions
    • Radhakrishnan I., Perez Alvarado G.C., Parker D., Dyson H.J., Montminy M.R., Wright P.E. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions. Cell. 91:1997;741-752.
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Perez Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 43
    • 0030029419 scopus 로고    scopus 로고
    • Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator
    • Kee B.L., Arias J., Montminy M.R. Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator. J. Biol. Chem. 271:1996;2373-2375.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2373-2375
    • Kee, B.L.1    Arias, J.2    Montminy, M.R.3
  • 44
    • 0030902507 scopus 로고    scopus 로고
    • Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors
    • Nakajima T., Uchida C., Anderson S.F., Parvin J.D., Montminy M. Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors. Genes Dev. 11:1997;738-747.
    • (1997) Genes Dev. , vol.11 , pp. 738-747
    • Nakajima, T.1    Uchida, C.2    Anderson, S.F.3    Parvin, J.D.4    Montminy, M.5
  • 47
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 87:1996;953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 48
    • 0035834648 scopus 로고    scopus 로고
    • MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells
    • Zhang Y., Liu G., Dong Z. MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells. J. Biol. Chem. 276:2001;42534-42542.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42534-42542
    • Zhang, Y.1    Liu, G.2    Dong, Z.3
  • 49
    • 0035816648 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase 1 mediates activation of Akt by ultraviolet B irradiation
    • Nomura M., Kaji A., Ma W.Y., Zhong S., Liu G., Bowden G.T., Miyamoto K.I., Dong Z. Mitogen- and stress-activated protein kinase 1 mediates activation of Akt by ultraviolet B irradiation. J. Biol. Chem. 276:2001;25558-25567.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25558-25567
    • Nomura, M.1    Kaji, A.2    Ma, W.Y.3    Zhong, S.4    Liu, G.5    Bowden, G.T.6    Miyamoto, K.I.7    Dong, Z.8
  • 50
    • 0028291992 scopus 로고
    • Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction
    • Barratt M.J., Hazzalin C.A., Cano E., Mahadevan L.C. Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction. Proc. Natl. Acad. Sci. U.S.A. 91:1994;4781-4785.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 4781-4785
    • Barratt, M.J.1    Hazzalin, C.A.2    Cano, E.3    Mahadevan, L.C.4
  • 51
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P., Tanner K.G., Cheung W.L., Sassone-Corsi P., Denu J.M., Allis C.D. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell. 5:2000;905-915.
    • (2000) Mol. Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, K.G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5    Allis, C.D.6
  • 52
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo W.S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.Y., Allis C.D., Marmorstein R., Berger S.L. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol. Cell. 5:2000;917-926.
    • (2000) Mol. Cell , vol.5 , pp. 917-926
    • Lo, W.S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.Y.5    Allis, C.D.6    Marmorstein, R.7    Berger, S.L.8
  • 53
    • 0035694785 scopus 로고    scopus 로고
    • Independent dynamic regulation of histone phosphorylation and acetylation during immediate-early gene induction
    • Thomson S., Clayton A.L., Mahadevan L.C. Independent dynamic regulation of histone phosphorylation and acetylation during immediate-early gene induction. Mol. Cell. 8:2001;1231-1241.
    • (2001) Mol. Cell , vol.8 , pp. 1231-1241
    • Thomson, S.1    Clayton, A.L.2    Mahadevan, L.C.3
  • 54
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science. 293:2001;1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 55
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • Wolffe A.P., Hayes J.J. Chromatin disruption and modification. Nucl. Acids Res. 27:1999;711-720.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 56
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P., Allis C.D., Sassone-Corsi P. Signaling to chromatin through histone modifications. Cell. 103:2000;263-271.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 57
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature. 403:2000;41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 58
    • 0035430282 scopus 로고    scopus 로고
    • Transcriptional regulation by the phosphorylation-dependent factor CREB
    • Mayr B., Montminy M. Transcriptional regulation by the phosphorylation-dependent factor CREB. Nat. Rev. Mol. Cell Biol. 2:2001;599-609.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 599-609
    • Mayr, B.1    Montminy, M.2
  • 59
    • 0035845567 scopus 로고    scopus 로고
    • Distinct effects of cAMP and mitogenic signals on CREB-binding protein recruitment impart specificity to target gene activation via CREB
    • Mayr B.M., Canettieri G., Montminy M.R. Distinct effects of cAMP and mitogenic signals on CREB-binding protein recruitment impart specificity to target gene activation via CREB. Proc. Natl. Acad. Sci. U.S.A. 98:2001;10936-10941.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10936-10941
    • Mayr, B.M.1    Canettieri, G.2    Montminy, M.R.3
  • 61
    • 0035157041 scopus 로고    scopus 로고
    • Chromatin-dependent cooperativity between constitutive and inducible activation domains in CREB
    • Asahara H., Santoso B., Guzman E., Du K., Cole P.A., Davidson I., Montminy M. Chromatin-dependent cooperativity between constitutive and inducible activation domains in CREB. Mol. Cell. Biol. 21:2001;7892-7900.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7892-7900
    • Asahara, H.1    Santoso, B.2    Guzman, E.3    Du, K.4    Cole, P.A.5    Davidson, I.6    Montminy, M.7
  • 62
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT a human cellular complex containing the set oncoprotein
    • Seo S.B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D. Regulation of histone acetylation and transcription by INHAT a human cellular complex containing the set oncoprotein. Cell. 104:2001;119-130.
    • (2001) Cell , vol.104 , pp. 119-130
    • Seo, S.B.1    McNamara, P.2    Heo, S.3    Turner, A.4    Lane, W.S.5    Chakravarti, D.6
  • 64
    • 0033977889 scopus 로고    scopus 로고
    • The phosphorylation status of a cyclic AMP-responsive activator is modulated via a chromatin-dependent mechanism
    • Michael L.F., Asahara H., Shulman A.I., Kraus W.L., Montminy M. The phosphorylation status of a cyclic AMP-responsive activator is modulated via a chromatin-dependent mechanism. Mol. Cell Biol. 20:2000;1596-1603.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1596-1603
    • Michael, L.F.1    Asahara, H.2    Shulman, A.I.3    Kraus, W.L.4    Montminy, M.5
  • 65
    • 0035809924 scopus 로고    scopus 로고
    • The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body
    • Boisvert F.M., Kruhlak M.J., Box A.K., Hendzel M.J., Bazett-Jones D.P. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J. Cell Biol. 152:2001;1099-1106.
    • (2001) J. Cell Biol. , vol.152 , pp. 1099-1106
    • Boisvert, F.M.1    Kruhlak, M.J.2    Box, A.K.3    Hendzel, M.J.4    Bazett-Jones, D.P.5
  • 66
    • 0034668190 scopus 로고    scopus 로고
    • The promyelocytic (PML) nuclear compartment and transcription control
    • Doucas V. The promyelocytic (PML) nuclear compartment and transcription control. Biochem. Pharmacol. 60:2000;1197-1201.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1197-1201
    • Doucas, V.1
  • 67
    • 0034631852 scopus 로고    scopus 로고
    • CREB-binding protein (CBP)/p300 and RNA polymerase II colocalize in transcriptionally active domains in the nucleus
    • von Mikecz A., Zhang S., Montminy M., Tan E.M., Hemmerich P. CREB-binding protein (CBP)/p300 and RNA polymerase II colocalize in transcriptionally active domains in the nucleus. J. Cell Biol. 150:2000;265-273.
    • (2000) J. Cell Biol. , vol.150 , pp. 265-273
    • Von Mikecz, A.1    Zhang, S.2    Montminy, M.3    Tan, E.M.4    Hemmerich, P.5
  • 68
    • 0037154983 scopus 로고    scopus 로고
    • The contribution of nuclear compartimentalization to gene regulation
    • Carmo-Fonseca M. The contribution of nuclear compartimentalization to gene regulation. Cell. 108:2002;513-521.
    • (2002) Cell , vol.108 , pp. 513-521
    • Carmo-Fonseca, M.1
  • 71
    • 0032558773 scopus 로고    scopus 로고
    • Protein regulation: Tag wrestling with relatives of ubiquitin
    • Hodges M., Tissot C., Freemont P.S. Protein regulation: Tag wrestling with relatives of ubiquitin. Curr. Biol. 8:1998;R749-752.
    • (1998) Curr. Biol. , vol.8 , pp. R749-752
    • Hodges, M.1    Tissot, C.2    Freemont, P.S.3
  • 72
    • 0034813107 scopus 로고    scopus 로고
    • Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities
    • Merienne K., Pannetier S., Harel-Bellan A., Sassone-Corsi P. Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities. Mol. Cell Biol. 21:2001;7089-7096.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 7089-7096
    • Merienne, K.1    Pannetier, S.2    Harel-Bellan, A.3    Sassone-Corsi, P.4
  • 73
    • 0036358038 scopus 로고    scopus 로고
    • Transcription MAPK-regulated transcription: A continuously variable gene switch?
    • Hazzalin C.A., Mahadevan L.C. Transcription MAPK-regulated transcription: A continuously variable gene switch? Nat. Rev. Mol. Cell Biol. 3:2002;30-40.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 30-40
    • Hazzalin, C.A.1    Mahadevan, L.C.2
  • 74
    • 0035849787 scopus 로고    scopus 로고
    • Temporal and quantitative regulation of mitogen-activated protein kinase (MAPK) modulates cell motility and invasion
    • Krueger J.S., Keshamouni V.G., Atanaskova N., Reddy K.B. Temporal and quantitative regulation of mitogen-activated protein kinase (MAPK) modulates cell motility and invasion. Oncogene. 20:2001;4209-4218.
    • (2001) Oncogene , vol.20 , pp. 4209-4218
    • Krueger, J.S.1    Keshamouni, V.G.2    Atanaskova, N.3    Reddy, K.B.4
  • 75
    • 0035956978 scopus 로고    scopus 로고
    • Activity-dependent CREB phosphorylation: Convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogen-activated protein kinase pathway
    • Wu G.Y., Deisseroth K., Tsien R.W. Activity-dependent CREB phosphorylation: Convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogen-activated protein kinase pathway. Proc. Natl. Acad. Sci. U.S.A. 98:2001;2808-2813.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2808-2813
    • Wu, G.Y.1    Deisseroth, K.2    Tsien, R.W.3
  • 76
    • 0034705227 scopus 로고    scopus 로고
    • Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties
    • Levchenko A., Bruck J., Sternberg P.W. Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties. Proc. Natl. Acad. Sci. U.S.A. 97:2000;5818-5823.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5818-5823
    • Levchenko, A.1    Bruck, J.2    Sternberg, P.W.3
  • 77
    • 0033105577 scopus 로고    scopus 로고
    • Nuclear import of the Drosophila Rel protein dorsal is regulated by phosphorylation
    • Drier E.A., Huang L.H., Steward R. Nuclear import of the Drosophila Rel protein dorsal is regulated by phosphorylation. Genes Dev. 13:1999;556-568.
    • (1999) Genes Dev. , vol.13 , pp. 556-568
    • Drier, E.A.1    Huang, L.H.2    Steward, R.3
  • 78
    • 0034892960 scopus 로고    scopus 로고
    • Activation of human immunodeficiency virus transcription in T cells revisited: NF-κB p65 stimulates transcriptional elongation
    • West M.J., Lowe A.D., Karn J. Activation of human immunodeficiency virus transcription in T cells revisited: NF-κB p65 stimulates transcriptional elongation. J. Virol. 75:2001;8524-8537.
    • (2001) J. Virol. , vol.75 , pp. 8524-8537
    • West, M.J.1    Lowe, A.D.2    Karn, J.3
  • 79
    • 0037022226 scopus 로고    scopus 로고
    • Human elongator facilitates RNA polymerase II transcription through chromatin
    • Kim J.H., Lane W.S., Reinberg D. Human elongator facilitates RNA polymerase II transcription through chromatin. Proc. Natl. Acad. Sci. U.S.A. 99:2002;1241-1246.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1241-1246
    • Kim, J.H.1    Lane, W.S.2    Reinberg, D.3
  • 81
    • 0033681250 scopus 로고    scopus 로고
    • Ordered recruitment of chromatin modifying and general transcription factors to the IFN-β promoter
    • Agalioti T., Lomvardas S., Parekh B., Yie J., Maniatis T., Thanos D. Ordered recruitment of chromatin modifying and general transcription factors to the IFN-β promoter. Cell. 103:2000;667-678.
    • (2000) Cell , vol.103 , pp. 667-678
    • Agalioti, T.1    Lomvardas, S.2    Parekh, B.3    Yie, J.4    Maniatis, T.5    Thanos, D.6
  • 82
    • 0032971444 scopus 로고    scopus 로고
    • Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-β promoter
    • Parekh B.S., Maniatis T. Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-β promoter. Mol. Cell. 3:1999;125-129.
    • (1999) Mol. Cell , vol.3 , pp. 125-129
    • Parekh, B.S.1    Maniatis, T.2
  • 83
    • 0035908126 scopus 로고    scopus 로고
    • Two waves of nuclear factor κB recruitment to target promoters
    • Saccani S., Pantano S., Natoli G. Two waves of nuclear factor κB recruitment to target promoters. J. Exp. Med. 193:2001;1351-1359.
    • (2001) J. Exp. Med. , vol.193 , pp. 1351-1359
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 84
    • 0036143654 scopus 로고    scopus 로고
    • P38-dependent marking of inflammatory genes for increased NF-κB recruitment
    • Saccani S., Pantano S., Natoli G. p38-dependent marking of inflammatory genes for increased NF-κB recruitment. Nat. Immunol. 3:2002;69-75.
    • (2002) Nat. Immunol. , vol.3 , pp. 69-75
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 85
    • 0030990093 scopus 로고    scopus 로고
    • Recombination signal sequence binding protein Jκ is constitutively bound to the NF-κB site of the interleukin-6 promoter and acts as a negative regulatory factor
    • Plaisance S., Vanden Berghe W., Boone E., Fiers W., Haegeman G. Recombination signal sequence binding protein Jκ is constitutively bound to the NF-κB site of the interleukin-6 promoter and acts as a negative regulatory factor. Mol. Cell Biol. 17:1997;3733-3743.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 3733-3743
    • Plaisance, S.1    Vanden Berghe, W.2    Boone, E.3    Fiers, W.4    Haegeman, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.