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Volumn 23, Issue 7, 2004, Pages 1598-1608

Erratum: Transrepression by a liganded nuclear receptor via a bHLH activator through co-regulator switching (EMBO Journal (2004) 23 (15981608) DOI: 10.1038/sj.emboj.7600157);Transrepression by a liganded nuclear receptor via a bHLH activator through co-regulator switching

Author keywords

bHLH type activator; Co regulator; Nuclear receptor; Transrepression; Vitamin D

Indexed keywords

CALCIDIOL 1 MONOOXYGENASE; CELL NUCLEUS RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; DIMER; HELIX LOOP HELIX PROTEIN; HISTONE ACETYLTRANSFERASE; PARATHYROID HORMONE; PROTEIN P300; RETINOID X RECEPTOR; SERINE; TRANSCRIPTION FACTOR; VITAMIN D RECEPTOR;

EID: 2342623470     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201470100     Document Type: Erratum
Times cited : (140)

References (48)
  • 1
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato M, Heerrlich P, Chambon P (1995) Steroid hormone receptors: many actors in search of a plot. Cell 83: 851-857
    • (1995) Cell , vol.83 , pp. 851-857
    • Beato, M.1    Heerrlich, P.2    Chambon, P.3
  • 2
    • 0025061096 scopus 로고
    • TFE3: A helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif
    • Beckmann H, Su LK, Kadesch T (1990) TFE3: a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif. Genes Dev 4: 167-179
    • (1990) Genes Dev , vol.4 , pp. 167-179
    • Beckmann, H.1    Su, L.K.2    Kadesch, T.3
  • 3
    • 0041589541 scopus 로고    scopus 로고
    • Nuclear receptors: A rendezvous for chromatin remodeling factors
    • Belandia B, Parker MG (2003) Nuclear receptors: a rendezvous for chromatin remodeling factors. Cell 114: 277-280
    • (2003) Cell , vol.114 , pp. 277-280
    • Belandia, B.1    Parker, M.G.2
  • 5
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • Chambon P (1996) A decade of molecular biology of retinoic acid receptors. FASEB J 10: 940-954
    • (1996) FASEB J , vol.10 , pp. 940-954
    • Chambon, P.1
  • 6
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM (1995) A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377: 454-457
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 8
    • 0025217856 scopus 로고
    • The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation
    • Davis RL, Cheng PF, Lassar AB, Weinturb H (1990) The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation. Cell 60: 733-746
    • (1990) Cell , vol.60 , pp. 733-746
    • Davis, R.L.1    Cheng, P.F.2    Lassar, A.B.3    Weinturb, H.4
  • 9
    • 0026693809 scopus 로고
    • Sequences in the human parathyroid hormone gene that bind the 1,25-dihydroxyvitamin D3 receptor and mediate transcriptional repression in response to 1,25-dihydroxyvitamin D3
    • Demay MB, Kiernan MS, DeLuca HF, Kronenberg HM (1992) Sequences in the human parathyroid hormone gene that bind the 1,25-dihydroxyvitamin D3 receptor and mediate transcriptional repression in response to 1,25-dihydroxyvitamin D3. Proc Natl Acad Sci USA 89: 8097-8101.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8097-8101
    • Demay, M.B.1    Kiernan, M.S.2    DeLuca, H.F.3    Kronenberg, H.M.4
  • 11
    • 0029969905 scopus 로고    scopus 로고
    • DNA sequences in the rat parathyroid hormone-related peptide gene responsible for 1,25-dihydroxyvitamin D3-mediated transcriptional repression
    • Falzon M (1996) DNA sequences in the rat parathyroid hormone-related peptide gene responsible for 1,25-dihydroxyvitamin D3-mediated transcriptional repression. Mol Endocrinol 10: 672-681
    • (1996) Mol Endocrinol , vol.10 , pp. 672-681
    • Falzon, M.1
  • 12
    • 0029758906 scopus 로고    scopus 로고
    • Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex
    • Fondell JD, Ge H, Roeder RG (1996) Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc Natl Acad Sci USA 93: 8329-8333
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8329-8333
    • Fondell, J.D.1    Ge, H.2    Roeder, R.G.3
  • 13
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG (2000) The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 14: 121-141
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 16
    • 0021989993 scopus 로고
    • Parathyroid hormone modulation of 25-hydroxyvitamin D3 metabolism by cultured chick kidney cells is mimicked and enhanced by forskolin
    • Henry HL (1985) Parathyroid hormone modulation of 25-hydroxyvitamin D3 metabolism by cultured chick kidney cells is mimicked and enhanced by forskolin. Endocrinology 116: 503-510
    • (1985) Endocrinology , vol.116 , pp. 503-510
    • Henry, H.L.1
  • 17
    • 0035958041 scopus 로고    scopus 로고
    • Estrogen receptor binding to DNA is not required for its activity through the nonclassical AP1 pathway
    • Jakacka M, Ito M, Weiss J, Chien PY, Gehm BD, Jameson L (2001) Estrogen receptor binding to DNA is not required for its activity through the nonclassical AP1 pathway. J Biol Chem 276: 13615-13621
    • (2001) J Biol Chem , vol.276 , pp. 13615-13621
    • Jakacka, M.1    Ito, M.2    Weiss, J.3    Chien, P.Y.4    Gehm, B.D.5    Jameson, L.6
  • 18
    • 0030980888 scopus 로고    scopus 로고
    • Mutations in the 1,25-dihydroxylation D3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor II B, in vitro
    • Jurutka PW, Hsieh J-C, Remus LS, Whitfield GK, Thomson PD, Haussler CA, Blanco JC, Ozato K, Haussler MR (1997) Mutations in the 1,25-dihydroxylation D3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor II B, in vitro. J Biol Chem 272: 14592-14599
    • (1997) J Biol Chem , vol.272 , pp. 14592-14599
    • Jurutka, P.W.1    Hsieh, J.-C.2    Remus, L.S.3    Whitfield, G.K.4    Thomson, P.D.5    Haussler, C.A.6    Blanco, J.C.7    Ozato, K.8    Haussler, M.R.9
  • 23
    • 0033553422 scopus 로고    scopus 로고
    • The autonomous transactivation domain in helix H3 of the vitamin D receptor is required for transactivation and coactivator interaction
    • Kraichely DM, Collins III JJ, DeLisle RK, MacDonald PN (1999) The autonomous transactivation domain in helix H3 of the vitamin D receptor is required for transactivation and coactivator interaction. J Biol Chem 274: 14352-14358
    • (1999) J Biol Chem , vol.274 , pp. 14352-14358
    • Kraichely, D.M.1    Collins III, J.J.2    DeLisle, R.K.3    MacDonald, P.N.4
  • 24
    • 0025808242 scopus 로고
    • Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo
    • Lassar AB, Davis RL, Wright WE, Kadesch T, Murre C, Voronova A, Baltimore D, Weinturb H (1991) Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo. Cell 66: 305-315
    • (1991) Cell , vol.66 , pp. 305-315
    • Lassar, A.B.1    Davis, R.L.2    Wright, W.E.3    Kadesch, T.4    Murre, C.5    Voronova, A.6    Baltimore, D.7    Weinturb, H.8
  • 26
    • 0037154974 scopus 로고    scopus 로고
    • Combinational control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW (2002) Combinational control of gene expression by nuclear receptors and coregulators. Cell 108: 465-474
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 27
    • 0035967914 scopus 로고    scopus 로고
    • Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: A humoral mechanism to reset a peripheral clock
    • McNamara P, Seo SP, Rudic RD, Sehgal A, Chakravarti D, FitzGerald GA (2001) Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock. Cell 105: 877-889
    • (2001) Cell , vol.105 , pp. 877-889
    • McNamara, P.1    Seo, S.P.2    Rudic, R.D.3    Sehgal, A.4    Chakravarti, D.5    FitzGerald, G.A.6
  • 28
    • 0032504693 scopus 로고    scopus 로고
    • The promoter of the human 25-hydroxyvitamin D3 1 alpha-hydroxylase gene confers positive and negative responsiveness to PTH, calcitonin, and 1alpha,25(OH)2D3
    • Murayama A, Takeyama K, Kitanaka S, Kodera Y, Hosoya T, Kato S (1998) The promoter of the human 25-hydroxyvitamin D3 1 alpha-hydroxylase gene confers positive and negative responsiveness to PTH, calcitonin, and 1alpha,25(OH)2D3. Biochem Biophys Res Commun 249: 11-16
    • (1998) Biochem Biophys Res Commun , vol.249 , pp. 11-16
    • Murayama, A.1    Takeyama, K.2    Kitanaka, S.3    Kodera, Y.4    Hosoya, T.5    Kato, S.6
  • 29
    • 0033306808 scopus 로고    scopus 로고
    • Positive and negative regulations of the renal 25-hydroxyvitamin D3 1alpha-hydroxylase gene by parathyroid hormone, calcitonin, and 1alpha,25(OH) 2D3 in intact animals
    • Murayama A, Takeyama K, Kitanaka S, Kodera Y, Kawaguchi Y, Hosoya T, Kato S (1999) Positive and negative regulations of the renal 25-hydroxyvitamin D3 1alpha-hydroxylase gene by parathyroid hormone, calcitonin, and 1alpha,25(OH)2D3 in intact animals. Endocrinology 140: 2224-2231
    • (1999) Endocrinology , vol.140 , pp. 2224-2231
    • Murayama, A.1    Takeyama, K.2    Kitanaka, S.3    Kodera, Y.4    Kawaguchi, Y.5    Hosoya, T.6    Kato, S.7
  • 30
    • 0024554495 scopus 로고
    • A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins
    • Murre C, McCaw PS, Baltimore D (1989a) A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56: 777-783
    • (1989) Cell , vol.56 , pp. 777-783
    • Murre, C.1    McCaw, P.S.2    Baltimore, D.3
  • 32
    • 0037622181 scopus 로고    scopus 로고
    • Cloning, gene structure and dietary regulation of the type-IIc Na/Pi cotransporter in the mouse kidney
    • Ohkido I, Segawa H, Yanagida R, Nakamura M, Miyamoto K (2003) Cloning, gene structure and dietary regulation of the type-IIc Na/Pi cotransporter in the mouse kidney. Pflugers Arch 446: 106-115
    • (2003) Pflugers Arch , vol.446 , pp. 106-115
    • Ohkido, I.1    Segawa, H.2    Yanagida, R.3    Nakamura, M.4    Miyamoto, K.5
  • 33
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate SA, Tsai SY, Tsai MJ, O'Malley BW (1995) Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270: 1354-1357
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 34
    • 0035912707 scopus 로고    scopus 로고
    • Targeted ablation of the 25-hydroxy-vitamin D 1alpha-hydroxylase enzyme: Evidence for skeletal, reproductive, and immune dysfunction
    • Panda DK, Miao D, Tremblay ML, Sirois J, Farookhi R, Hendy GN, Goltzman D (2001) Targeted ablation of the 25-hydroxy-vitamin D 1alpha-hydroxylase enzyme: evidence for skeletal, reproductive, and immune dysfunction. Proc Natl Acad Sci USA 98: 7498-7503
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7498-7503
    • Panda, D.K.1    Miao, D.2    Tremblay, M.L.3    Sirois, J.4    Farookhi, R.5    Hendy, G.N.6    Goltzman, D.7
  • 36
    • 0024744568 scopus 로고
    • Mutations in glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities
    • Schena M, Freedman LP, Yamamoto KR (1989) Mutations in glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities. Genes Dev 3: 1590-1601
    • (1989) Genes Dev , vol.3 , pp. 1590-1601
    • Schena, M.1    Freedman, L.P.2    Yamamoto, K.R.3
  • 37
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL (1998) The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 23: 927-937
    • (1998) Cell , vol.23 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 41
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L, White J, Brou C, Tasset D, Webster N, Scheer E, Chambon P (1989) The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 3: 477-487
    • (1989) Cell , vol.3 , pp. 477-487
    • Tora, L.1    White, J.2    Brou, C.3    Tasset, D.4    Webster, N.5    Scheer, E.6    Chambon, P.7
  • 42
    • 0028831207 scopus 로고
    • The Pan basic helix-loop-helix proteins are required for insulin gene expression
    • Vierra CA, Nelson C (1995) The Pan basic helix-loop-helix proteins are required for insulin gene expression. Mol Endocrinol 9: 64-71
    • (1995) Mol Endocrinol , vol.9 , pp. 64-71
    • Vierra, C.A.1    Nelson, C.2
  • 43
  • 47
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kijima M, Akita M, Beppu T (1990) Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 5: 17174-17179
    • (1990) J Biol Chem , vol.5 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4


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