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Volumn 387, Issue 4, 2009, Pages 717-722

Interactions between the nuclear matrix and an enhancer of the tryptophan oxygenase gene

Author keywords

Glucocorticoid receptor; Hepatocyte; Nuclear matrix; S MAR; Tryptophan oxygenase

Indexed keywords

DEXAMETHASONE; LAMIN; RIBONUCLEOPROTEIN; RIBONUCLEOPROTEIN U; TRYPTOPHAN 2,3 DIOXYGENASE; UNCLASSIFIED DRUG;

EID: 68549115137     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.07.095     Document Type: Article
Times cited : (4)

References (24)
  • 1
    • 0017652886 scopus 로고
    • The structure of histone-depleted metaphase chromosomes
    • Paulson J.R., and Laemmli U.K. The structure of histone-depleted metaphase chromosomes. Cell 12 (1977) 817-828
    • (1977) Cell , vol.12 , pp. 817-828
    • Paulson, J.R.1    Laemmli, U.K.2
  • 2
    • 0017752811 scopus 로고
    • Role of nonhistone proteins in metaphase chromosomes structure
    • Adolph K.W., Cheng S.M., and Laemmli U.K. Role of nonhistone proteins in metaphase chromosomes structure. Cell 12 (1977) 805-816
    • (1977) Cell , vol.12 , pp. 805-816
    • Adolph, K.W.1    Cheng, S.M.2    Laemmli, U.K.3
  • 3
    • 0344413285 scopus 로고
    • Dysfunction of chromosomal loop attachment sites: illegitimate recombination linked to matrix association regions and topoisomerase II
    • Sperry A.O., Blasquez V.C., and Garrard W.T. Dysfunction of chromosomal loop attachment sites: illegitimate recombination linked to matrix association regions and topoisomerase II. Proc. Natl. Acad. Sci. USA 86 (1989) 5497-5501
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5497-5501
    • Sperry, A.O.1    Blasquez, V.C.2    Garrard, W.T.3
  • 4
    • 0029918905 scopus 로고    scopus 로고
    • Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA
    • Renz A., and Fackelmayer F.O. Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA. Nucleic Acids Res. 24 (1996) 843-849
    • (1996) Nucleic Acids Res. , vol.24 , pp. 843-849
    • Renz, A.1    Fackelmayer, F.O.2
  • 5
    • 0026737332 scopus 로고
    • Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements
    • Romig H., Fackelmayer F.O., Renz A., Ramsperger U., and Richter A. Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements. EMBO J. 11 (1992) 3431-3440
    • (1992) EMBO J. , vol.11 , pp. 3431-3440
    • Romig, H.1    Fackelmayer, F.O.2    Renz, A.3    Ramsperger, U.4    Richter, A.5
  • 6
    • 0029848521 scopus 로고    scopus 로고
    • Histone modifications, chromatin structure, and the nuclear matrix
    • Davie J.R. Histone modifications, chromatin structure, and the nuclear matrix. J. Cell. Biochem. 62 (1996) 149-157
    • (1996) J. Cell. Biochem. , vol.62 , pp. 149-157
    • Davie, J.R.1
  • 7
    • 0031241290 scopus 로고    scopus 로고
    • Role of nuclear architecture in the initiation of eukaryotic DNA replication
    • Hyrien O., Maric C., and Lucas I. Role of nuclear architecture in the initiation of eukaryotic DNA replication. Biochimie 79 (1997) 541-548
    • (1997) Biochimie , vol.79 , pp. 541-548
    • Hyrien, O.1    Maric, C.2    Lucas, I.3
  • 8
    • 0038380293 scopus 로고    scopus 로고
    • Chromatin remodeling by nuclear receptors
    • Hebbar P.B., and Archer T.K. Chromatin remodeling by nuclear receptors. Chromosoma 111 (2003) 495-504
    • (2003) Chromosoma , vol.111 , pp. 495-504
    • Hebbar, P.B.1    Archer, T.K.2
  • 9
    • 0033821409 scopus 로고    scopus 로고
    • Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1-induced histone H4 acetylation on lysines 8 and 12
    • Ito K., Barnes P.J., and Adcock I.M. Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1-induced histone H4 acetylation on lysines 8 and 12. Mol. Cell. Biol. 20 (2000) 6891-6903
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6891-6903
    • Ito, K.1    Barnes, P.J.2    Adcock, I.M.3
  • 10
    • 0034461148 scopus 로고    scopus 로고
    • A specificity and targeting subunit of a human SWI/SNF family-related chromatin-remodeling complex
    • Nie Z., Xue Y., Yang D., Zhou S., Deroo B.J., Archer T.K., and Wang W. A specificity and targeting subunit of a human SWI/SNF family-related chromatin-remodeling complex. Mol. Cell. Biol. 20 (2000) 8879-8888
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8879-8888
    • Nie, Z.1    Xue, Y.2    Yang, D.3    Zhou, S.4    Deroo, B.J.5    Archer, T.K.6    Wang, W.7
  • 12
    • 0348141449 scopus 로고
    • Glucocorticoid induction of the rat tryptophan oxygenase gene is mediated by two widely separated glucocorticoid-responsive elements
    • Danesch U., Gloss B., Schmid W., Schütz G., Schüle R., and Renkawitz R. Glucocorticoid induction of the rat tryptophan oxygenase gene is mediated by two widely separated glucocorticoid-responsive elements. EMBO J. 6 (1987) 625-630
    • (1987) EMBO J. , vol.6 , pp. 625-630
    • Danesch, U.1    Gloss, B.2    Schmid, W.3    Schütz, G.4    Schüle, R.5    Renkawitz, R.6
  • 13
    • 0028258829 scopus 로고
    • DNase I hypersensitive sites far upstream of the rat tryptophan oxygenase gene direct developmentally regulated transcription in livers of transgenic mice
    • Kaltschmidt C., Muller M., Brem G., and Renkawitz R. DNase I hypersensitive sites far upstream of the rat tryptophan oxygenase gene direct developmentally regulated transcription in livers of transgenic mice. Mech. Dev. 45 (1994) 203-210
    • (1994) Mech. Dev. , vol.45 , pp. 203-210
    • Kaltschmidt, C.1    Muller, M.2    Brem, G.3    Renkawitz, R.4
  • 14
    • 0031759085 scopus 로고    scopus 로고
    • Differentiation and proliferation of primary rat hepatocytes cultured as spheroids
    • Hamamoto R., Yamada K., Kamihira M., and Iijima S. Differentiation and proliferation of primary rat hepatocytes cultured as spheroids. J. Biochem. 124 (1998) 972-979
    • (1998) J. Biochem. , vol.124 , pp. 972-979
    • Hamamoto, R.1    Yamada, K.2    Kamihira, M.3    Iijima, S.4
  • 15
    • 9144253197 scopus 로고    scopus 로고
    • Transcriptional coactivators CBP and p300 cooperatively enhance HNF-1-mediated expression of the albumin gene in hepatocytes
    • Dohda T., Kaneoka H., Inayoshi Y., Kamihira M., Miyake K., and Iijima S. Transcriptional coactivators CBP and p300 cooperatively enhance HNF-1-mediated expression of the albumin gene in hepatocytes. J. Biochem. 136 (2004) 313-319
    • (2004) J. Biochem. , vol.136 , pp. 313-319
    • Dohda, T.1    Kaneoka, H.2    Inayoshi, Y.3    Kamihira, M.4    Miyake, K.5    Iijima, S.6
  • 16
    • 28244446715 scopus 로고    scopus 로고
    • Repression of GR-mediated expression of the tryptophan oxygenase gene by the SWI/SNF complex during liver development
    • Inayoshi Y., Kaneoka H., Machida Y., Terajima M., Dohda T., Miyake K., and Iijima S. Repression of GR-mediated expression of the tryptophan oxygenase gene by the SWI/SNF complex during liver development. J. Biochem. 138 (2005) 457-465
    • (2005) J. Biochem. , vol.138 , pp. 457-465
    • Inayoshi, Y.1    Kaneoka, H.2    Machida, Y.3    Terajima, M.4    Dohda, T.5    Miyake, K.6    Iijima, S.7
  • 17
    • 0021675784 scopus 로고
    • Organization of the higher-order chromatin loop: specific DNA attachment sites on nuclear scaffold
    • Mirkovitch J., Mirault M.E., and Laemmli U.K. Organization of the higher-order chromatin loop: specific DNA attachment sites on nuclear scaffold. Cell 39 (1994) 223-232
    • (1994) Cell , vol.39 , pp. 223-232
    • Mirkovitch, J.1    Mirault, M.E.2    Laemmli, U.K.3
  • 18
    • 0035110880 scopus 로고    scopus 로고
    • Experimental observations of a nuclear matrix
    • Nickerson J.A. Experimental observations of a nuclear matrix. J. Cell Sci. 114 (2001) 463-474
    • (2001) J. Cell Sci. , vol.114 , pp. 463-474
    • Nickerson, J.A.1
  • 19
    • 17844391563 scopus 로고    scopus 로고
    • Actin and hnRNP U cooperate for productive transcription by RNA polymerase II
    • Kukalev A., Nord Y., Palmberg C., Bergman T., and Percipalle P. Actin and hnRNP U cooperate for productive transcription by RNA polymerase II. Nat. Struct. Biol. 12 (2005) 238-244
    • (2005) Nat. Struct. Biol. , vol.12 , pp. 238-244
    • Kukalev, A.1    Nord, Y.2    Palmberg, C.3    Bergman, T.4    Percipalle, P.5
  • 22
    • 0033538831 scopus 로고    scopus 로고
    • Three-dimensional visualization of transcription sites and their association with splicing factor-rich nuclear speckles
    • Wei X., Somanathan S., Samarabandu J., and Berezney R. Three-dimensional visualization of transcription sites and their association with splicing factor-rich nuclear speckles. J. Cell Biol. 146 (1999) 543-558
    • (1999) J. Cell Biol. , vol.146 , pp. 543-558
    • Wei, X.1    Somanathan, S.2    Samarabandu, J.3    Berezney, R.4
  • 23
    • 0028914933 scopus 로고
    • Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix
    • van Steensel B., Jenster G., Damm K., Brinkmann A.O., and van Driel R. Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix. J. Cell. Biochem. 57 (1995) 465-478
    • (1995) J. Cell. Biochem. , vol.57 , pp. 465-478
    • van Steensel, B.1    Jenster, G.2    Damm, K.3    Brinkmann, A.O.4    van Driel, R.5
  • 24
    • 0037128211 scopus 로고    scopus 로고
    • Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription
    • Spann T.P., Goldman A.E., Wang C., Huang S., and Goldman R.D. Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription. J. Cell Biol. 156 (2002) 603-608
    • (2002) J. Cell Biol. , vol.156 , pp. 603-608
    • Spann, T.P.1    Goldman, A.E.2    Wang, C.3    Huang, S.4    Goldman, R.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.