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Volumn 12, Issue 21, 1998, Pages 3343-3356

Structure and specificity of nuclear receptor-coactivator interactions

Author keywords

Coactivators; GRIP1; Interaction site; Nuclear receptors; Specificity

Indexed keywords

CELL NUCLEUS RECEPTOR;

EID: 0032213219     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.21.3343     Document Type: Article
Times cited : (840)

References (53)
  • 1
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams, P.D., N.S. Pannu, R.J. Read, and A.T. Brunger. 1997. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. 94: 5018-5023.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 3
    • 0028980918 scopus 로고
    • Expression of the rat α1 thyroid hormone receptor ligand binding domain in Escherichia coli and the use of a ligand-induced conformational change as a method for its purification to homogeneity
    • Apriletti, J.W., J.D. Baxter, K.H. Lau, and B. West. 1995. Expression of the rat α1 thyroid hormone receptor ligand binding domain in Escherichia coli and the use of a ligand-induced conformational change as a method for its purification to homogeneity. Protein Expr. Purif. 6: 363-370.
    • (1995) Protein Expr. Purif. , vol.6 , pp. 363-370
    • Apriletti, J.W.1    Baxter, J.D.2    Lau, K.H.3    West, B.4
  • 4
    • 0028233763 scopus 로고
    • Characterization of the ligand-dependent transactivation domain of thyroid receptor
    • Barettino, D., M.d.M. Vivanco Ruiz, and G. Stunnenberg. 1994. Characterization of the ligand-dependent transactivation domain of thyroid receptor. EMBO J. 13: 3039-3049.
    • (1994) EMBO J. , vol.13 , pp. 3039-3049
    • Barettino, D.1    Vivanco Ruiz, M.D.M.2    Stunnenberg, G.3
  • 5
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXRa
    • Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the ligand-binding domain of the human nuclear receptor RXRa. Nature 375: 377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 7
    • 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., R.J. Lin, R.L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M.L. Privalsky, Y. Nakatani, and R.M. Evans. 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
  • 9
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, No. 4. 1994. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. Sect. D. Biol. Crystallogr. 50: 760-763.
    • (1994) Acta Crystallogr. Sect. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 11
    • 0026600841 scopus 로고
    • Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
    • Danielian, P.S., R. White, J.A. Lees, and M.G. Parker. 1992. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 11: 1025-1033.
    • (1992) EMBO J. , vol.11 , pp. 1025-1033
    • Danielian, P.S.1    White, R.2    Lees, J.A.3    Parker, M.G.4
  • 12
    • 0032230231 scopus 로고    scopus 로고
    • Nuclear receptor binding sites of coactivators GRIP1 and SRC-1 : Multiple motifs with different binding specificities
    • Ding, X.F., C.M. Anderson, H. Ma, H. Hong, R.M. Uht, P.J. Kushner, and M.R. Stallcup. 1998. Nuclear receptor binding sites of coactivators GRIP1 and SRC-1 : multiple motifs with different binding specificities. Mol. Endocrinol. 12: 302-313.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 302-313
    • Ding, X.F.1    Anderson, C.M.2    Ma, H.3    Hong, H.4    Uht, R.M.5    Kushner, P.J.6    Stallcup, M.R.7
  • 13
    • 0027941792 scopus 로고
    • Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: Presence of a conserved autonomous constitutive activation domain and influence of the nature of the response element on AF-2 activity
    • Durand, B., M. Saunders, C. Gaudon, B. Roy, R. Losson, and P. Chambon. 1994. Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: Presence of a conserved autonomous constitutive activation domain and influence of the nature of the response element on AF-2 activity. EMBO J. 13: 5370-5382.
    • (1994) EMBO J. , vol.13 , pp. 5370-5382
    • Durand, B.1    Saunders, M.2    Gaudon, C.3    Roy, B.4    Losson, R.5    Chambon, P.6
  • 16
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in the transcriptional co-activators mediate binding to nuclear receptors
    • Heery, D.M., E. Kalkhoven, S. Hoare, and M.G. Parker. 1997. A signature motif in the transcriptional co-activators mediate binding to nuclear receptors. Nature 387: 733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 17
    • 0030950531 scopus 로고    scopus 로고
    • AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors
    • Henttu, P.M.A., E. Kalkhoven, and M.G. Parker. 1997. AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors. Mol. Cell Biol. 17: 1832-1839.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 1832-1839
    • Henttu, P.M.A.1    Kalkhoven, E.2    Parker, M.G.3
  • 18
    • 0029978605 scopus 로고    scopus 로고
    • GRIP1, a novel mouse protein that serves as a transcriptional co-activator in yeast for the hormone binding domains of steroid receptors
    • Hong, H., K. Kohli, A. Triverdi, D.L. Johnson, and M.R. Stallcup. 1996. GRIP1, a novel mouse protein that serves as a transcriptional co-activator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. 93: 4948-4952.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 4948-4952
    • Hong, H.1    Kohli, K.2    Triverdi, A.3    Johnson, D.L.4    Stallcup, M.R.5
  • 19
    • 0030949836 scopus 로고    scopus 로고
    • GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • Hong, H., K. Kohli, M.J. Garabedian, and M.R. Stallcup. 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell Biol. 17: 2735-2744.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3    Stallcup, M.R.4
  • 20
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., J.Y. Zou, S.W. Cowan, and M. Kjelgaard. 1991. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallographica A47: 110-119.
    • (1991) Acta Crystallographica , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 21
    • 0030980888 scopus 로고    scopus 로고
    • Mutations in the 1,25-dihydroxyvitamin D3 receptor identifying carboxy-terminal amino acids required for the transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor IIb, in vitro
    • Jurutka, P.W., J.C. Hsieh, L.S. Remus, G.K. Whitfield, P.D. Thompson, C.A. Haussler, J.C. Blanco, K. Ozato, and M.R. Haussler. 1997. Mutations in the 1,25-dihydroxyvitamin D3 receptor identifying carboxy-terminal amino acids required for the transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor IIb, 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    Thompson, P.D.5    Haussler, C.A.6    Blanco, J.C.7    Ozato, K.8    Haussler, M.R.9
  • 22
    • 0032472408 scopus 로고    scopus 로고
    • Isoforms of steroid receptor coactivator 1 differ in their ability to potentiate transcription by the oestrogen receptor
    • Kalkhoven, E., J.E. Valentine, D.M. Heery, and M.G. Parker. 1998. Isoforms of steroid receptor coactivator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 17: 232-243.
    • (1998) EMBO J. , vol.17 , pp. 232-243
    • Kalkhoven, E.1    Valentine, J.E.2    Heery, D.M.3    Parker, M.G.4
  • 25
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TIF1α and TIF1β in the epigenetic control of transcription by nuclear receptors
    • Le Douarin, B., A.L. Nielsen, J.M. Gamier, H. Ichinose, F. Jeanmougin, R. Losson, and P. Chambon. 1996. A possible involvement of TIF1α and TIF1β in the epigenetic control of transcription by nuclear receptors. EMBO J. 15: 6701-6715.
    • (1996) EMBO J. , vol.15 , pp. 6701-6715
    • Le Douarin, B.1    Nielsen, A.L.2    Gamier, J.M.3    Ichinose, H.4    Jeanmougin, F.5    Losson, R.6    Chambon, P.7
  • 26
    • 0030872716 scopus 로고    scopus 로고
    • RAC3, a steroid/ nuclear receptor-associated coactivator that is related to SRC-1 and TIF-2
    • Li, H., P.J. Gomes, and J. Don Chen. 1997. RAC3, a steroid/ nuclear receptor-associated coactivator that is related to SRC-1 and TIF-2. Proc. Natl. Acad. Sci. 94: 8479-8484.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 8479-8484
    • Li, H.1    Gomes, P.J.2    Don Chen, J.3
  • 27
    • 0028979005 scopus 로고
    • II31 protein is a transcriptional coactivator of the p53 protein
    • II31 protein is a transcriptional coactivator of the p53 protein. Proc. Natl. Acad. Sci. 92: 5154-5158.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 5154-5158
    • Lu, H.1    Levine, A.J.2
  • 29
    • 0030771215 scopus 로고    scopus 로고
    • Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction
    • Masuyama, H., C.M. Brownfield, R. St-Arnaud, and P.N. MacDonald. 1997. Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction. Mol. Endocrinol. 11: 1507-1517.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1507-1517
    • Masuyama, H.1    Brownfield, C.M.2    St-Arnaud, R.3    MacDonald, P.N.4
  • 30
    • 0031833450 scopus 로고    scopus 로고
    • The nuclear receptor ligand-binding domain: Structure and function
    • Moras, D. and H. Gronemeyer. 1998. The nuclear receptor ligand-binding domain: Structure and function. Curr. Opin. Cell. Biol. 10: 384-391.
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 384-391
    • Moras, D.1    Gronemeyer, H.2
  • 31
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., K.A. Sharp, and B. Honig. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 33
    • 0032549531 scopus 로고    scopus 로고
    • Enhancement of the estrogen receptor transcriptional activity by the coactivator GRIP1 highlights the role of activation function 2 in determining estrogen receptor pharmacology
    • Norris, J.D., D. Fan, M.R. Stallcup, and D.P. McDonnell. 1998. Enhancement of the estrogen receptor transcriptional activity by the coactivator GRIP1 highlights the role of activation function 2 in determining estrogen receptor pharmacology. J. Biol. Chem. 273: 6679-6688.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6679-6688
    • Norris, J.D.1    Fan, D.2    Stallcup, M.R.3    McDonnell, D.P.4
  • 34
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate, S.A., S.Y. Tsai, M.J. Tsai, and B.W. O'Malley. 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
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • ed. C.W. Carter, Jr. and R.M. Sweet Academic Press, New York, NY
    • Otwinowski, Z. and W. Minor. 1997. Processing of x-ray diffraction data collected in oscillation mode. In Macromolecular crystallography, Part A (ed. C.W. Carter, Jr. and R.M. Sweet), pp. 307-326. Academic Press, New York, NY.
    • (1997) Macromolecular Crystallography, Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 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., G.C. Perez-Alvarado, D. Parker, H.J. Dyson, M.R. Montminy, and P.E. Wright. 1997. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions. Cell 91: 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
  • 37
    • 0029643780 scopus 로고
    • Crystal structure of the RARγ ligand-binding domain bound to all-trans retinoic acid
    • Renaud, J.P., N. Rachel, M. Ruff, V. Vivat, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the RARγ ligand-binding domain bound to all-trans retinoic acid. Nature 378: 681-689.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.P.1    Rachel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 38
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B. and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19: 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 39
    • 0030754001 scopus 로고    scopus 로고
    • Mutations in the conserved carboxy-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity
    • Saatcioglu, F., G. Lopez, B.L. West, E. Zandi, W. Feng, H. Lu, A. Esmaili, J.W. Apriletti, P.J. Kushner, J.D. Baxter, and M. Karin. 1997. Mutations in the conserved carboxy-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity. Mol. Cell. Biol. 17: 4687-4695.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4687-4695
    • Saatcioglu, F.1    Lopez, G.2    West, B.L.3    Zandi, E.4    Feng, W.5    Lu, H.6    Esmaili, A.7    Apriletti, J.W.8    Kushner, P.J.9    Baxter, J.D.10    Karin, M.11
  • 40
    • 0030786270 scopus 로고    scopus 로고
    • TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid coactivator-1
    • Takeshita, A., G.R. Cardona, N. Koibuchi, C.S. Suen, and W.W. Chin. 1997. TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid coactivator-1. J. Biol. Chem. 272: 27629-27634.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27629-27634
    • Takeshita, A.1    Cardona, G.R.2    Koibuchi, N.3    Suen, C.S.4    Chin, W.W.5
  • 42
    • 0027996382 scopus 로고
    • Functional analysis of a transactivation domain in the thyroid beta receptor
    • Tone, Y., T.N. Collingwood, M. Adams, and V.K. Chatterjee. 1994. Functional analysis of a transactivation domain in the thyroid beta receptor. J. Biol. Chem. 269: 31157-31161.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31157-31161
    • Tone, Y.1    Collingwood, T.N.2    Adams, M.3    Chatterjee, V.K.4
  • 43
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional coactivator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia, J., D.W. Rose, J. Inostroza, Y. Kamei, S. Westin, C.K. Glass, and M.G. Rosenfeld. 1997. The transcriptional coactivator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387: 677-684.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1    Rose, D.W.2    Inostroza, J.3    Kamei, Y.4    Westin, S.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 44
    • 0030756675 scopus 로고    scopus 로고
    • Induced a helix in the VP16 activation domain upon binding to a human TAF
    • Uesugi, M., O. Nyanguile, H. Lu, A.J. Levine, and G.L. Verdine. 1997. Induced a helix in the VP16 activation domain upon binding to a human TAF. Science 277: 1310-1313.
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 45
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel, J.J., M.J.S. Heine, C. Zechel, P. Chambon, and H. Gronemeyer. 1996. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15: 3667-3675.
    • (1996) EMBO J. , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.S.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 46
    • 0032518944 scopus 로고    scopus 로고
    • The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
    • Voegel, J.J., M.J.S. Heine, M. Tini, V. Vivat, P. Chambon, and H. Gronemeyer. 1998. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways, EMBO J. 17: 507-519.
    • (1998) EMBO J. , vol.17 , pp. 507-519
    • Voegel, J.J.1    Heine, M.J.S.2    Tini, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6
  • 47
    • 0031910827 scopus 로고    scopus 로고
    • The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor
    • Wagner, B.L., J.D. Morris, T.A. Knotts, N. Weigel, and D.P. McDonnell. 1998. The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor. Mol. Cell. Biol. 18: 1369-1378.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1369-1378
    • Wagner, B.L.1    Morris, J.D.2    Knotts, T.A.3    Weigel, N.4    McDonnell, D.P.5
  • 49
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of the progesterone/progesterone receptor complex
    • Williams, S.P. and P.B. Sigler. 1998. Atomic structure of the progesterone/progesterone receptor complex. Nature 393: 392-396.
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 51
    • 0024150160 scopus 로고
    • Ligand regulated nonspecific inactivation of receptor function: A versatile mechanism for signal transduction
    • Yamamoto, K.R., P.J. Godowski, and D. Picard. 1988. Ligand regulated nonspecific inactivation of receptor function: a versatile mechanism for signal transduction. Cold Spring Harb. Symp. Quant. Biol. 53: 803-811.
    • (1988) Cold Spring Harb. Symp. Quant. Biol. , vol.53 , pp. 803-811
    • Yamamoto, K.R.1    Godowski, P.J.2    Picard, D.3
  • 52
    • 0000017176 scopus 로고
    • Combinatorial regulation at a mammalian composite response element
    • ed. S.L. McKnight and K.R. Yamamoto, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Yamamoto, K.R., D. Pearce, J. Thomas, and J.N. Miner. 1992. Combinatorial regulation at a mammalian composite response element. In Transcriptional regulation (ed. S.L. McKnight and K.R. Yamamoto), pp. 1169-1192. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1992) Transcriptional Regulation , pp. 1169-1192
    • Yamamoto, K.R.1    Pearce, D.2    Thomas, J.3    Miner, J.N.4
  • 53
    • 0032230289 scopus 로고    scopus 로고
    • A nuclear receptor corepressor modulates transcriptional activity of antagonist-occupied steroid hormone receptor
    • Zhang, X., M. Jeyakumar, S. Petukhov, and M.K. Bagchi. 1998. A nuclear receptor corepressor modulates transcriptional activity of antagonist-occupied steroid hormone receptor. Mol. Endocrinol. 12: 513-524.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 513-524
    • Zhang, X.1    Jeyakumar, M.2    Petukhov, S.3    Bagchi, M.K.4


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