메뉴 건너뛰기




Volumn 18, Issue 1, 2003, Pages 323-331

Role of chromatin disruption and histone acetylation in thyroid hormone receptor action: Implications in the regulation of HIV-1 LTR

Author keywords

AIDS; Chromatin; Histone acetylation; HIV; Thyroid hormone receptor

Indexed keywords

DNA; HISTONE; HISTONE DEACETYLASE; THYROID HORMONE; THYROID HORMONE RECEPTOR;

EID: 0037215985     PISSN: 02133911     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (12)

References (77)
  • 3
    • 0021337076 scopus 로고
    • The nuclear 3,5,3′-triiodothyronine receptor in human leukaemic cell lines
    • Bernal J. and Andersson L.C. (1984). The nuclear 3,5,3′-triiodothyronine receptor in human leukaemic cell lines. Acta Endocrinol. 105, 429-432.
    • (1984) Acta Endocrinol. , vol.105 , pp. 429-432
    • Bernal, J.1    Andersson, L.C.2
  • 4
    • 0033815579 scopus 로고    scopus 로고
    • Co-repressors 2000
    • Burke L.J. and Baniahmad A. (2000). Co-repressors 2000. FASEB J. 14, 1876-1888.
    • (2000) FASEB J. , vol.14 , pp. 1876-1888
    • Burke, L.J.1    Baniahmad, A.2
  • 5
    • 0032470461 scopus 로고    scopus 로고
    • Coactivation and corepression in transcriptional regulation by steroid/nuclear hormone receptors
    • Chen J.D. and Li H. (1998). Coactivation and corepression in transcriptional regulation by steroid/nuclear hormone receptors. Cri. Rev. Eukaryot. Gene Express. 8, 169-190.
    • (1998) Cri. Rev. Eukaryot. Gene Express. , vol.8 , pp. 169-190
    • Chen, J.D.1    Li, H.2
  • 6
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y. and Evans R.M. (1997). Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90, 569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 7
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • Chen H., Richar J.L., Xie W., Wilpitz D. and Evans R.M. (1999). Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 98, 675-686.
    • (1999) Cell , vol.98 , pp. 675-686
    • Chen, H.1    Richar, J.L.2    Xie, W.3    Wilpitz, D.4    Evans, R.M.5
  • 8
    • 0028101212 scopus 로고
    • Cloning of a thyroid hormone-responsive Rana catesbeiana c-erbA-beta gene
    • Davey J.C., Schneider M.J. and Galton V.A. (1994). Cloning of a thyroid hormone-responsive Rana catesbeiana c-erbA-beta gene. Dev Genet 15, 339-346.
    • (1994) Dev Genet , vol.15 , pp. 339-346
    • Davey, J.C.1    Schneider, M.J.2    Galton, V.A.3
  • 9
    • 0027202123 scopus 로고
    • The NF-kB and Sp1 motifs of the human immunodeficiency virus type 1 long terminal repeat function as novel thyroid hormone response elements
    • Desai-Yajnik V. and Samuels H.H. (1993). The NF-kB and Sp1 motifs of the human immunodeficiency virus type 1 long terminal repeat function as novel thyroid hormone response elements. Mol. Cell. Biol. 13, 5057-5069.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5057-5069
    • Desai-Yajnik, V.1    Samuels, H.H.2
  • 11
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans R.M. (1988). The steroid and thyroid hormone receptor superfamily. Science 240, 889-895.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 12
    • 0027240151 scopus 로고
    • Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: Implications for active repression
    • Fondell J.D., Roy A.L. and Roeder R.G. (1993). Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: Implications for active repression. Genes Dev. 7, 1400-1410.
    • (1993) Genes Dev. , vol.7 , pp. 1400-1410
    • Fondell, J.D.1    Roy, A.L.2    Roeder, R.G.3
  • 13
  • 14
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W. and Roeder R. G. (1997). Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 15
    • 0034192756 scopus 로고    scopus 로고
    • A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness
    • Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A. and Shiekhattar R. (2000). A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. Genes Dev. 14, 1048-1057.
    • (2000) Genes Dev. , vol.14 , pp. 1048-1057
    • Guenther, M.G.1    Lane, W.S.2    Fischle, W.3    Verdin, E.4    Lazar, M.A.5    Shiekhattar, R.6
  • 16
    • 0002439050 scopus 로고
    • Regulation of thermogenesis by thyroid hormones
    • Oppenheimer J. and Samuels H. (eds). Academic Press. New York
    • Guernsey D.L. and Edelman I.S. (1983). Regulation of thermogenesis by thyroid hormones. In: Molecular Basis of Thyroid Hormone Action. Oppenheimer J. and Samuels H. (eds). Academic Press. New York. pp 293-324.
    • (1983) Molecular Basis of Thyroid Hormone Action , pp. 293-324
    • Guernsey, D.L.1    Edelman, I.S.2
  • 17
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • Hassig C.A., Fleischer T.C., Billin A.N., Schreiber S.L. and Ayer D.E. (1997). Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89, 34134-7.
    • (1997) Cell , vol.89 , pp. 34134-34137
    • Hassig, C.A.1    Fleischer, T.C.2    Billin, A.N.3    Schreiber, S.L.4    Ayer, D.E.5
  • 20
    • 0036261558 scopus 로고    scopus 로고
    • Chromatin disruption and histone acetylation in the regulation of HIV-LTR by thyroid hormone receptor
    • Hsia S.-C.V. and Shi Y.-B. (2002). Chromatin disruption and histone acetylation in the regulation of HIV-LTR by thyroid hormone receptor. Mol. Cell Biol. 22, 4043-4052.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4043-4052
    • Hsia, S.-C.V.1    Shi, Y.-B.2
  • 21
    • 0035294247 scopus 로고    scopus 로고
    • Involvement of chromatin and histone acetylation in the regulation of HIV-LTR by thyroid hormone receptor
    • Hsia S.-C.V., Wang H. and Shi Y.-B. (2001). Involvement of chromatin and histone acetylation in the regulation of HIV-LTR by thyroid hormone receptor. Cell Res. 11, 8-16.
    • (2001) Cell Res. , vol.11 , pp. 8-16
    • Hsia, S.-C.V.1    Wang, H.2    Shi, Y.-B.3
  • 22
    • 0034045480 scopus 로고    scopus 로고
    • Transcriptional repression by nuclear hormone receptors
    • Hu X. and Lazar M.A. (2000). Transcriptional repression by nuclear hormone receptors. TEM 11: 1, 6-10.
    • (2000) TEM , vol.11
    • Hu, X.1    Lazar, M.A.2
  • 23
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang E.Y., Zhang J., Miska E.A., Guenther M.G., Kouzarides T. and Lazar M.A. (2000). Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway Genes Dev. 14, 45-54.
    • (2000) Genes Dev. , vol.14 , pp. 45-54
    • Huang, E.Y.1    Zhang, J.2    Miska, E.A.3    Guenther, M.G.4    Kouzarides, T.5    Lazar, M.A.6
  • 24
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof A., Yang X.J., Ogryzko V.V., Nakatani Y., Wolffe A.P. and Ge H. (1997). Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7, 689-692.
    • (1997) Curr. Biol. , vol.7 , pp. 689-692
    • Imhof, A.1    Yang, X.J.2    Ogryzko, V.V.3    Nakatani, Y.4    Wolffe, A.P.5    Ge, H.6
  • 25
    • 0035318741 scopus 로고    scopus 로고
    • The TRAP/SMCC/Mediator complex and thyroid hormone receptor function
    • Ito M. and Roeder R.G. (2001). The TRAP/SMCC/Mediator complex and thyroid hormone receptor function. Trends Endocrinol. Metab. 12, 127-134.
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 127-134
    • Ito, M.1    Roeder, R.G.2
  • 26
    • 0033105821 scopus 로고    scopus 로고
    • Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators
    • Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.Y., Zhang X., Qin J. and Roeder R.G. (1999). Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators. Mol. Cell 3, 361-370.
    • (1999) Mol. Cell , vol.3 , pp. 361-370
    • Ito, M.1    Yuan, C.-X.2    Malik, S.3    Gu, W.4    Fondell, J.D.5    Yamamura, S.6    Fu, Z.Y.7    Zhang, X.8    Qin, J.9    Roeder, R.G.10
  • 27
    • 0035937783 scopus 로고    scopus 로고
    • Multiple N-CoR complexes contain distinct histone deacetylases
    • Jones P.L., Sachs L.M., Rouse N., Wade P.A. and Shi Y.B. (2001). Multiple N-CoR complexes contain distinct histone deacetylases. J. Biol. Chem. 276, 8807-8811.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8807-8811
    • Jones, P.L.1    Sachs, L.M.2    Rouse, N.3    Wade, P.A.4    Shi, Y.B.5
  • 28
    • 0029063189 scopus 로고
    • Interplay between chromatin structure and transcription
    • Kornberg R.D. and Lorch Y. (1995). Interplay between chromatin structure and transcription. Curr. Opin. Cell. Biol. 7, 371-375.
    • (1995) Curr. Opin. Cell. Biol. , vol.7 , pp. 371-375
    • Kornberg, R.D.1    Lorch, Y.2
  • 29
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
    • Laherty C.D., Yang W.M., Sun J.M., Davie J.R., Seto E. and Eisenman R.N. (1997). Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89, 349-356.
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 31
    • 0024345926 scopus 로고
    • Maternal thyroxine and congenital hypothyroidism
    • Larsen P.R. (1989). Maternal thyroxine and congenital hypothyroidism. N. Engl. J. Med. 321, 444-446.
    • (1989) N. Engl. J. Med. , vol.321 , pp. 444-446
    • Larsen, P.R.1
  • 32
    • 0027973041 scopus 로고
    • Chromatin and gene expression: Constant questions, but changing answers
    • Lewin B. (1994). Chromatin and gene expression: Constant questions, but changing answers. Cell 79, 397-406.
    • (1994) Cell , vol.79 , pp. 397-406
    • Lewin, B.1
  • 33
    • 0033993510 scopus 로고    scopus 로고
    • p300 requires its histone acetyltransferase activity and SRC-1 interaction domain to facilitate thyroid hormone receptor activation in chromatin
    • Li J., O'Malley B.W. and Wong J. (2000a). p300 requires its histone acetyltransferase activity and SRC-1 interaction domain to facilitate thyroid hormone receptor activation in chromatin. Mol. Cell. Biol. 20, 2031-2042.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2031-2042
    • Li, J.1    O'Malley, B.W.2    Wong, J.3
  • 34
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and C-CoR exist in large protein complexes containing HDAC3
    • Li J., Wang J., Nawaz Z., Liu J.M., Qin J. and Wong J. (2000b). Both corepressor proteins SMRT and C-CoR exist in large protein complexes containing HDAC3. EMBO J. 19, 4342-4350.
    • (2000) EMBO J , vol.19 , pp. 4342-4350
    • Li, J.1    Wang, J.2    Nawaz, Z.3    Liu, J.M.4    Qin, J.5    Wong, J.6
  • 35
    • 0033569770 scopus 로고    scopus 로고
    • p300 stimulates transcription instigated by ligand-bound thyroid hormone receptor at a step subsequent to chromatin disruption
    • Li Q., Imhof A., Collingwood T.N., Urnov F.D. and Wolffe A.P. (1999). p300 stimulates transcription instigated by ligand-bound thyroid hormone receptor at a step subsequent to chromatin disruption. EMBO J. 18, 5634-5652.
    • (1999) EMBO J. , vol.18 , pp. 5634-5652
    • Li, Q.1    Imhof, A.2    Collingwood, T.N.3    Urnov, F.D.4    Wolffe, A.P.5
  • 36
    • 0024318624 scopus 로고
    • Unique alterations of thyroid-hormone indexes in the acquired immunodeficiency syndrome (Aids)
    • Lopresti J.S., Fried J.C., Spencer C.A. and Nicoloff J.T. (1989). Unique alterations of thyroid-hormone indexes in the acquired immunodeficiency syndrome (Aids). Ann. Intern. Med. 110, 970-975.
    • (1989) Ann. Intern. Med. , vol.110 , pp. 970-975
    • Lopresti, J.S.1    Fried, J.C.2    Spencer, C.A.3    Nicoloff, J.T.4
  • 38
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • McKenna N.J., Lanz R.B. and O'Malley B.W. (1999). Nuclear receptor coregulators: Cellular and molecular biology. Endocr. Rev. 20, 321-344.
    • (1999) Endocr. Rev. , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 41
    • 0037154963 scopus 로고    scopus 로고
    • Cooperation between complexes that regulate chromatin structure and transcription
    • Narlikar G.J., Fan H.-Y. and Kingston R. (2002). Cooperation between complexes that regulate chromatin structure and transcription. Cell 108, 475-487.
    • (2002) Cell , vol.108 , pp. 475-487
    • Narlikar, G.J.1    Fan, H.-Y.2    Kingston, R.3
  • 42
    • 0018379663 scopus 로고
    • Thyroid hormone action at the cellular level
    • Oppenheimer J.H. (1979). Thyroid hormone action at the cellular level. Science 203, 971-979.
    • (1979) Science , vol.203 , pp. 971-979
    • Oppenheimer, J.H.1
  • 44
    • 0034142332 scopus 로고    scopus 로고
    • A compilation of cellular transcription factor interactions with the HIV-1 LTR promoter
    • Pereira L.A., Bentley K., Peeters A., Churchill M.J. and Deacon N.J. (2000). A compilation of cellular transcription factor interactions with the HIV-1 LTR promoter. Nuclei Acids Research 28, 663-668.
    • (2000) Nuclei Acids Research , vol.28 , pp. 663-668
    • Pereira, L.A.1    Bentley, K.2    Peeters, A.3    Churchill, M.J.4    Deacon, N.J.5
  • 45
    • 0020079551 scopus 로고
    • Thyroid hormone nuclear receptor. Evidence for multimeric organization in chromatin
    • Perlman A.J., Stanley F. and Samuels H.H. (1982). Thyroid hormone nuclear receptor. Evidence for multimeric organization in chromatin. J. Biol. Chem. 257, 930-938.
    • (1982) J. Biol. Chem. , vol.257 , pp. 930-938
    • Perlman, A.J.1    Stanley, F.2    Samuels, H.H.3
  • 46
    • 0030853945 scopus 로고    scopus 로고
    • Both thyroid hormone and 9-cis retinoic acid receptors are required to efficiently mediate the effects of thyroid hormone on embryonic development and specific gene regulation in Xenopus laevis
    • Puzianowsak-Kuznicka M., Damjanovski S. and Shi Y.-B. (1997). Both thyroid hormone and 9-cis retinoic acid receptors are required to efficiently mediate the effects of thyroid hormone on embryonic development and specific gene regulation in Xenopus laevis. Mol. Cell. Biol. 17, 4738-4749.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4738-4749
    • Puzianowsak-Kuznicka, M.1    Damjanovski, S.2    Shi, Y.-B.3
  • 47
    • 0030449245 scopus 로고    scopus 로고
    • Functional characterization of a mutant thyroid hormone receptor in Xenopus laevis
    • Puzianowsak-Kuznicka M., Wong J., Kanamori A. and Shi Y.-B. (1996). Functional characterization of a mutant thyroid hormone receptor in Xenopus laevis. J. Biol. Chem. 271, 33394-33403.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33394-33403
    • Puzianowsak-Kuznicka, M.1    Wong, J.2    Kanamori, A.3    Shi, Y.-B.4
  • 48
    • 0034603725 scopus 로고    scopus 로고
    • Mechanisms of gene regulation by vitamin D(3) receptor: A network of coactivator interactions
    • Rachez C. and Freedman L.P. (2000). Mechanisms of gene regulation by vitamin D(3) receptor: A network of coactivator interactions. Gene 246, 9-21.
    • (2000) Gene , vol.246 , pp. 9-21
    • Rachez, C.1    Freedman, L.P.2
  • 50
    • 0029590777 scopus 로고
    • A unique thyroid hormone response element in the human immunodeficiency virus type 1 long terminal repeat that overlaps the Sp1 binding sites
    • Rahman A., Esmaili A. and Saatcioglu F. (1995). A unique thyroid hormone response element in the human immunodeficiency virus type 1 long terminal repeat that overlaps the Sp1 binding sites. J. Biol. Chem. 270, 31059-31064.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31059-31064
    • Rahman, A.1    Esmaili, A.2    Saatcioglu, F.3
  • 51
    • 0028102748 scopus 로고
    • Transcriptional repression of Xenopus TR beta gene is mediated by a thyroid hormone response element located near the start site
    • Ranjan M., Wong J. and Shi Y.B. (1994). Transcriptional repression of Xenopus TR beta gene is mediated by a thyroid hormone response element located near the start site. J. Biol. Chem. 269, 24699-24705.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24699-24705
    • Ranjan, M.1    Wong, J.2    Shi, Y.B.3
  • 52
    • 0033521956 scopus 로고    scopus 로고
    • The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1
    • Ryu S., Zhou S., Ladurner A.G. and Tjian R. (1999). The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1. Nature 397, 446-450.
    • (1999) Nature , vol.397 , pp. 446-450
    • Ryu, S.1    Zhou, S.2    Ladurner, A.G.3    Tjian, R.4
  • 53
    • 0034700122 scopus 로고    scopus 로고
    • Targeted chromatin binding and histone acetylation in vivo by thyroid hormone receptor during amphibian development
    • Sachs L.M. and Shi Y.-B. (2000). Targeted chromatin binding and histone acetylation in vivo by thyroid hormone receptor during amphibian development. Proc. Natl. Acad. Sci. USA 97, 13138-13143.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13138-13143
    • Sachs, L.M.1    Shi, Y.-B.2
  • 55
    • 0031455415 scopus 로고    scopus 로고
    • Histone acetyltransferases regulate HIV-1 enhancer activity in vitro
    • Sheridan P.L., Mayall T.P., Verdin E. and Jones K.A. (1997). Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. Genes Dev. 11, 3324-3340.
    • (1997) Genes Dev. , vol.11 , pp. 3327-3340
    • Sheridan, P.L.1    Mayall, T.P.2    Verdin, E.3    Jones, K.A.4
  • 56
    • 0035756689 scopus 로고    scopus 로고
    • Thyroid hormone regulation of apoptotic tissue remodeling during anuran metamorphosis
    • Shi Y.B., Fu L., Hsia S.C., Tomita A and Buchholz D. (2001). Thyroid hormone regulation of apoptotic tissue remodeling during anuran metamorphosis. Cell Res. 11, 245-252.
    • (2001) Cell Res. , vol.11 , pp. 245-252
    • Shi, Y.B.1    Fu, L.2    Hsia, S.C.3    Tomita, A.4    Buchholz, D.5
  • 57
    • 0029561581 scopus 로고
    • Thyroid hormone control of thermogenesis and energy balance
    • Silva J.E. (1995). Thyroid hormone control of thermogenesis and energy balance. Thyroid 5, 481-492.
    • (1995) Thyroid , vol.5 , pp. 481-492
    • Silva, J.E.1
  • 58
    • 0032573167 scopus 로고    scopus 로고
    • Purified histone acetyltransferase complexes stimulate HIV-1 transcription from preassembled nucleosomal arrays
    • Steger D.J., Eberharter A., John S., Grant P.A. and Wokman J.L. (1998). Purified histone acetyltransferase complexes stimulate HIV-1 transcription from preassembled nucleosomal arrays. Proc. Natl. Acad. Sci. USA 95, 12924-12929.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12924-12929
    • Steger, D.J.1    Eberharter, A.2    John, S.3    Grant, P.A.4    Workman, J.L.5
  • 59
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D. and Allis C.D. (2000). The language of covalent histone modifications. Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 60
    • 0027413988 scopus 로고
    • Histones, nucleosomes and transcription
    • Svaren J. and Horz W. (1993). Histones, nucleosomes and transcription. Curr. Opin. Gen. Dev. 3, 219-225.
    • (1993) Curr. Opin. Gen. Dev. , vol.3 , pp. 219-225
    • Svaren, J.1    Horz, W.2
  • 61
    • 0024949755 scopus 로고
    • Thyroid-hormone levels in the acquired immunodeficiency syndrome (Aids)
    • Tang W.W. and Kaptein E.M. (1989). Thyroid-hormone levels in the acquired immunodeficiency syndrome (Aids). Western J. Med. 151, 627-631.
    • (1989) Western J. Med. , vol.151 , pp. 627-631
    • Tang, W.W.1    Kaptein, E.M.2
  • 62
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai M.J. and O'Malley B.W. (1994). Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63, 451-486.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.W.2
  • 63
    • 0034704078 scopus 로고    scopus 로고
    • A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1
    • Underhill C., Qutob M.S., Yee S.P. and Torchia J. (2000). A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1 J. Biol. Chem. 275, 40463-4070.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40463-44070
    • Underhill, C.1    Qutob, M.S.2    Yee, S.P.3    Torchia, J.4
  • 64
    • 0034254668 scopus 로고    scopus 로고
    • Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erbA yields a chromatin infrastructure-dependent transcriptional repression pathway
    • Urnov F.D., Yee J., Sachs L., Collingwood T.N., Bauer A., Beug H., Shi Y.B. and Wolffe A.P. (2000). Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erbA yields a chromatin infrastructure-dependent transcriptional repression pathway. EMBO J. 19, 4074-4090.
    • (2000) EMBO J. , vol.19 , pp. 4074-4090
    • Urnov, F.D.1    Yee, J.2    Sachs, L.3    Collingwood, T.N.4    Bauer, A.5    Beug, H.6    Shi, Y.B.7    Wolffe, A.P.8
  • 67
    • 0031308763 scopus 로고    scopus 로고
    • Chromatin remodeling regulated by steroid and nuclear receptors
    • Wolffe A.P. (1997). Chromatin remodeling regulated by steroid and nuclear receptors. Cell Res. 7, 127-142.
    • (1997) Cell Res. , vol.7 , pp. 127-142
    • Wolffe, A.P.1
  • 69
    • 0032518799 scopus 로고    scopus 로고
    • Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase
    • Wong J., Patterton D., Imhof D., Guschin D., Shi Y.-B. and Wolffe A.P. (1998). Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. EMBO J. 17, 520-534.
    • (1998) EMBO J. , vol.17 , pp. 520-534
    • Wong, J.1    Patterton, D.2    Imhof, D.3    Guschin, D.4    Shi, Y.-B.5    Wolffe, A.P.6
  • 70
    • 0030946171 scopus 로고    scopus 로고
    • Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: Hormone-regulated chromatin disruption is not sufficient for transcriptional activation
    • Wong J., Shi Y.-B. and Wolffe A.P. (1997). Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: Hormone-regulated chromatin disruption is not sufficient for transcriptional activation. EMBO J. 16, 3158-3171.
    • (1997) EMBO J. , vol.16 , pp. 3158-3171
    • Wong, J.1    Shi, Y.-B.2    Wolffe, A.P.3
  • 71
    • 0028860925 scopus 로고
    • A role for nucleosome assembly in both silencing and activation of the Xenopus TR beta A gene by the thyroid hormone receptor
    • Wong J., Shi Y.B. and Wolffe A.P. (1995). A role for nucleosome assembly in both silencing and activation of the Xenopus TR beta A gene by the thyroid hormone receptor. Genes Dev. 9, 2696-2711.
    • (1995) Genes Dev. , vol.9 , pp. 2696-2711
    • Wong, J.1    Shi, Y.B.2    Wolffe, A.P.3
  • 72
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman J.L. and Kingston R.E. (1998). Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67, 545-579.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 73
    • 0029850735 scopus 로고    scopus 로고
    • Hormone receptor regulation of the human immunodeficiency virus type 1 and type 2 long terminal repeats
    • Xu J., Luznik L., Wong-Staal F. and Gill G.N. (1996). Hormone receptor regulation of the human immunodeficiency virus type 1 and type 2 long terminal repeats. J. Biomed. Sci. 3, 323-331.
    • (1996) J. Biomed. Sci. , vol.3 , pp. 323-331
    • Xu, J.1    Luznik, L.2    Wong-Staal, F.3    Gill, G.N.4
  • 74
    • 0033119162 scopus 로고    scopus 로고
    • Coactivator and corepressor complexes in nuclear receptor function
    • Xu L., Glass C.K. and Rosenfeld M.G. (1999). Coactivator and corepressor complexes in nuclear receptor function. Curr. Op. Genet. Dev. 9, 140-147.
    • (1999) Curr. Op. Genet. Dev. , vol.9 , pp. 140-147
    • Xu, L.1    Glass, C.K.2    Rosenfeld, M.G.3
  • 75
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen P.M. (2001). Physiological and molecular basis of thyroid hormone action. Physiol. Rev. 81, 1097-142.
    • (2001) Physiol. Rev. , vol.81 , pp. 1097-1142
    • Yen, P.M.1
  • 76
    • 0028296032 scopus 로고
    • New advances in understanding the molecular mechanisms of thyroid hormone action
    • Yen P.M. and Chin W.W. (1994). New advances in understanding the molecular mechanisms of thyroid hormone action. Trends Endocrinol. Metab. 5, 65-72.
    • (1994) Trends Endocrinol. Metab. , vol.5 , pp. 65-72
    • Yen, P.M.1    Chin, W.W.2
  • 77
    • 0033859843 scopus 로고    scopus 로고
    • The mechanism of action of thyroid hormones
    • Zhang J. and Lazar M.A. (2000). The mechanism of action of thyroid hormones. Annu. Rev. Physiol. 62, 439-466.
    • (2000) Annu. Rev. Physiol. , vol.62 , pp. 439-466
    • Zhang, J.1    Lazar, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.