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Volumn 74, Issue 12, 2009, Pages 877-883

Structural and functional relationships of the steroid hormone receptors' N-terminal transactivation domain

Author keywords

Activation function; Intrinsically disordered protein; Protein folding; Protein:protein interactions; Steroid hormone receptors

Indexed keywords

STEROID RECEPTOR;

EID: 69949131670     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2009.07.012     Document Type: Review
Times cited : (41)

References (89)
  • 1
    • 0034129679 scopus 로고    scopus 로고
    • Steroid hormone receptors: an update
    • Beato M., and Klug J. Steroid hormone receptors: an update. Hum Reprod Update 6 (2000) 225-236
    • (2000) Hum Reprod Update , vol.6 , pp. 225-236
    • Beato, M.1    Klug, J.2
  • 2
    • 0035976638 scopus 로고    scopus 로고
    • Nuclear receptors and lipid physiology: opening the X-files
    • Chawla A., Repa J.J., Evans R.M., and Mangelsdorf D.J. Nuclear receptors and lipid physiology: opening the X-files. Science 294 (2001) 1866-1870
    • (2001) Science , vol.294 , pp. 1866-1870
    • Chawla, A.1    Repa, J.J.2    Evans, R.M.3    Mangelsdorf, D.J.4
  • 3
    • 0141891343 scopus 로고    scopus 로고
    • Unfolding the action of progesterone receptors
    • Li X., and O'Malley B.W. Unfolding the action of progesterone receptors. J Biol Chem 278 (2003) 39261-39264
    • (2003) J Biol Chem , vol.278 , pp. 39261-39264
    • Li, X.1    O'Malley, B.W.2
  • 4
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation
    • Lonard D.M., and O'Malley B.W. Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation. Mol Cell 27 (2007) 691-700
    • (2007) Mol Cell , vol.27 , pp. 691-700
    • Lonard, D.M.1    O'Malley, B.W.2
  • 5
    • 0033054115 scopus 로고    scopus 로고
    • The structure of the nuclear hormone receptors
    • Kumar R., and Thompson E.B. The structure of the nuclear hormone receptors. Steroids 64 (1999) 310-319
    • (1999) Steroids , vol.64 , pp. 310-319
    • Kumar, R.1    Thompson, E.B.2
  • 6
    • 0022393794 scopus 로고
    • Primary structure and expression of a functional human glucocorticoid receptor cDNA
    • Hollenberg S.M., Weinberger C., Ong E.S., Cerelli G., Oro A., Lebo R., et al. Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature 318 (1985) 635-641
    • (1985) Nature , vol.318 , pp. 635-641
    • Hollenberg, S.M.1    Weinberger, C.2    Ong, E.S.3    Cerelli, G.4    Oro, A.5    Lebo, R.6
  • 7
    • 0022653964 scopus 로고
    • Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A
    • Green S., Walter P., Kumar V., Krust A., Bornert J.M., Argos P., et al. Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature 320 (1986) 134-139
    • (1986) Nature , vol.320 , pp. 134-139
    • Green, S.1    Walter, P.2    Kumar, V.3    Krust, A.4    Bornert, J.M.5    Argos, P.6
  • 8
    • 3142624840 scopus 로고    scopus 로고
    • The evolution of the nuclear receptor superfamily
    • Escriva H., Bertrand S., and Laudet V. The evolution of the nuclear receptor superfamily. Essays Biochem 40 (2004) 11-26
    • (2004) Essays Biochem , vol.40 , pp. 11-26
    • Escriva, H.1    Bertrand, S.2    Laudet, V.3
  • 9
    • 0035826690 scopus 로고    scopus 로고
    • Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions
    • Thornton J.W. Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions. Proc Natl Acad Sci U S A 98 (2001) 5671-5676
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5671-5676
    • Thornton, J.W.1
  • 10
    • 0141431993 scopus 로고    scopus 로고
    • Resurrecting the ancestral steroid receptor: ancient origin of estrogen signaling
    • Thornton J.W., Need E., and Crews D. Resurrecting the ancestral steroid receptor: ancient origin of estrogen signaling. Science 301 (2003) 1714-1717
    • (2003) Science , vol.301 , pp. 1714-1717
    • Thornton, J.W.1    Need, E.2    Crews, D.3
  • 11
    • 0023913120 scopus 로고    scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans R.M. The steroid and thyroid hormone receptor superfamily. Science 240 (2003) 889-895
    • (2003) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 12
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato M. Gene regulation by steroid hormones. Cell 56 (1989) 335-344
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 13
    • 0022327612 scopus 로고
    • Steroid receptor regulated transcription of specific genes and gene network
    • Yamamoto K.R. Steroid receptor regulated transcription of specific genes and gene network. Annu Rev Genet 19 (1985) 209-252
    • (1985) Annu Rev Genet , vol.19 , pp. 209-252
    • Yamamoto, K.R.1
  • 14
    • 0028713459 scopus 로고    scopus 로고
    • Function/activity of specific amino acids in glucocorticoid receptors
    • Academic Press, Inc. p. 49-130
    • Simons Jr. S.S. Function/activity of specific amino acids in glucocorticoid receptors. Vitamins and hormones (1999), Academic Press, Inc. p. 49-130
    • (1999) Vitamins and hormones
    • Simons Jr., S.S.1
  • 15
    • 0026600841 scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of the interaction by tamoxifen
    • Danielian P.S., White R., Lees J.A., and Parker M.G. The structural basis of estrogen receptor/coactivator recognition and the antagonism of the interaction by tamoxifen. EMBO J 11 (1992) 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
  • 16
    • 0025957233 scopus 로고
    • Transcriptional activation and nuclear targeting signals of the human androgen receptor
    • Simental J.A., Sar M., Lane M.V., French F.S., and Wilson E.M. Transcriptional activation and nuclear targeting signals of the human androgen receptor. J Biol Chem 266 (1991) 510-518
    • (1991) J Biol Chem , vol.266 , pp. 510-518
    • Simental, J.A.1    Sar, M.2    Lane, M.V.3    French, F.S.4    Wilson, E.M.5
  • 17
    • 0026600841 scopus 로고
    • Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
    • Danielian P.S., White R., Lees J.A., and Parker M.G. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J 11 (1992) 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
  • 18
    • 0030669765 scopus 로고    scopus 로고
    • Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators
    • Ikonen T., Palvimo J.J., and Janne O.A. Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. J Biol Chem 272 (1997) 29821-29828
    • (1997) J Biol Chem , vol.272 , pp. 29821-29828
    • Ikonen, T.1    Palvimo, J.J.2    Janne, O.A.3
  • 19
    • 0034740164 scopus 로고    scopus 로고
    • Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains
    • Metivier R., Penot G., Flouriot G., and Pakdel F. Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains. Mol Endocrinol 15 (2001) 1953-1970
    • (2001) Mol Endocrinol , vol.15 , pp. 1953-1970
    • Metivier, R.1    Penot, G.2    Flouriot, G.3    Pakdel, F.4
  • 20
    • 0029978077 scopus 로고    scopus 로고
    • Human estrogen receptor ligand activity inversion mutants: receptors that interpret antiestrogens as estrogens and estrogens as antiestrogens and discriminate among different antiestrogens
    • Montano M.M., Ekena K., Krueger K.D., Keller A.L., and Katzenellenbogen B.S. Human estrogen receptor ligand activity inversion mutants: receptors that interpret antiestrogens as estrogens and estrogens as antiestrogens and discriminate among different antiestrogens. Mol Endocrinol 10 (1996) 230-242
    • (1996) Mol Endocrinol , vol.10 , pp. 230-242
    • Montano, M.M.1    Ekena, K.2    Krueger, K.D.3    Keller, A.L.4    Katzenellenbogen, B.S.5
  • 21
    • 0029616211 scopus 로고
    • Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor
    • Kraus W.L., McInerney E.M., and Katzenellenbogen B.S. Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor. Proc Natl Acad Sci U S A 92 (1995) 12314-12318
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 12314-12318
    • Kraus, W.L.1    McInerney, E.M.2    Katzenellenbogen, B.S.3
  • 22
    • 0033305373 scopus 로고    scopus 로고
    • Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo
    • Tetel M.J., Giangrande P.H., Leonhardt S.A., McDonnell D.P., and Edwards D.P. Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol Endocrinol 13 (1999) 910-924
    • (1999) Mol Endocrinol , vol.13 , pp. 910-924
    • Tetel, M.J.1    Giangrande, P.H.2    Leonhardt, S.A.3    McDonnell, D.P.4    Edwards, D.P.5
  • 23
    • 0037245786 scopus 로고    scopus 로고
    • Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions
    • Kumar R., and Thompson E.B. Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions. Mol Endocrinol 17 (2003) 1-10
    • (2003) Mol Endocrinol , vol.17 , pp. 1-10
    • Kumar, R.1    Thompson, E.B.2
  • 24
    • 0032784653 scopus 로고    scopus 로고
    • The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription
    • Alen P., Claessens F., Verhoeven G., Rombauts W., and Peeters B. The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription. Mol Cell Biol 19 (1999) 6085-6097
    • (1999) Mol Cell Biol , vol.19 , pp. 6085-6097
    • Alen, P.1    Claessens, F.2    Verhoeven, G.3    Rombauts, W.4    Peeters, B.5
  • 25
    • 0037067766 scopus 로고    scopus 로고
    • Dependence of selective gene activation on the androgen receptor NH2- and COOH-terminal interaction
    • He B., Lee L.W., Minges J.T., and Wilson E.M. Dependence of selective gene activation on the androgen receptor NH2- and COOH-terminal interaction. J Biol Chem 277 (2002) 25631-25639
    • (2002) J Biol Chem , vol.277 , pp. 25631-25639
    • He, B.1    Lee, L.W.2    Minges, J.T.3    Wilson, E.M.4
  • 26
    • 0037020186 scopus 로고    scopus 로고
    • TIF2 mediates the synergy between RARalpha 1 activation functions AF-1 and AF-2
    • Bommer M., Benecke A., Gronemeyer H., and Rochette-Egly C. TIF2 mediates the synergy between RARalpha 1 activation functions AF-1 and AF-2. J Biol Chem 277 (2002) 37961-37966
    • (2002) J Biol Chem , vol.277 , pp. 37961-37966
    • Bommer, M.1    Benecke, A.2    Gronemeyer, H.3    Rochette-Egly, C.4
  • 27
    • 0345650665 scopus 로고    scopus 로고
    • Activation functions 1 and 2 of nuclear receptors: molecular strategies for transcriptional activation
    • Warnmark A., Treuter E., Wright A.P., and Gustafsson J.A. Activation functions 1 and 2 of nuclear receptors: molecular strategies for transcriptional activation. Mol Endocrinol 17 (2003) 1901-1909
    • (2003) Mol Endocrinol , vol.17 , pp. 1901-1909
    • Warnmark, A.1    Treuter, E.2    Wright, A.P.3    Gustafsson, J.A.4
  • 30
    • 12244256087 scopus 로고    scopus 로고
    • A novel estrogen receptor alpha-associated protein, template-activating factor I beta, inhibits acetylation and transactivation
    • Loven M.A., Muster N., Yates J.R., and Nardulli A.M. A novel estrogen receptor alpha-associated protein, template-activating factor I beta, inhibits acetylation and transactivation. Mol Endocrinol 17 (2003) 67-78
    • (2003) Mol Endocrinol , vol.17 , pp. 67-78
    • Loven, M.A.1    Muster, N.2    Yates, J.R.3    Nardulli, A.M.4
  • 31
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: cellular and molecular biology
    • McKenna N.J., Lanz R.B., and O'Malley B.W. Nuclear receptor coregulators: cellular and molecular biology. Endocrine Rev 20 (1999) 321-344
    • (1999) Endocrine Rev , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 33
    • 0033214780 scopus 로고    scopus 로고
    • Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins
    • Hittelman A.B., Burakov D., Iniguez-Lluhi J.A., Freedman L.P., and Garabedian M.J. Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins. EMBO J 18 (1999) 5380-5388
    • (1999) EMBO J , vol.18 , pp. 5380-5388
    • Hittelman, A.B.1    Burakov, D.2    Iniguez-Lluhi, J.A.3    Freedman, L.P.4    Garabedian, M.J.5
  • 37
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum D.M., Wang Y., Williams S.P., and Sigler P.B. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci U S A 95 (1998) 5998-6003
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 38
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams S.P., and Sigler P.B. Atomic structure of progesterone complexed with its receptor. Nature 393 (1998) 392-396
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 39
    • 0034714276 scopus 로고    scopus 로고
    • Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations
    • Matias P.M., Donner P., Coelho R., Thomaz M., Peixoto C., Macedo S., et al. Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations. J Biol Chem 275 (2000) 26164-26171
    • (2000) J Biol Chem , vol.275 , pp. 26164-26171
    • Matias, P.M.1    Donner, P.2    Coelho, R.3    Thomaz, M.4    Peixoto, C.5    Macedo, S.6
  • 40
    • 0038265311 scopus 로고    scopus 로고
    • The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism
    • Kauppi B., Jakob C., Farnegardh M., Yang J., Ahola H., Alarcon M., et al. The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism. J Biol Chem 278 (2003) 22748-22754
    • (2003) J Biol Chem , vol.278 , pp. 22748-22754
    • Kauppi, B.1    Jakob, C.2    Farnegardh, M.3    Yang, J.4    Ahola, H.5    Alarcon, M.6
  • 41
    • 0033198735 scopus 로고    scopus 로고
    • Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist
    • Pike A.C., Brzozowski A.M., Hubbard R.E., Bonn T., Thorsell A.G., Engstrom O., et al. Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist. EMBO J 18 (1999) 4608-4618
    • (1999) EMBO J , vol.18 , pp. 4608-4618
    • Pike, A.C.1    Brzozowski, A.M.2    Hubbard, R.E.3    Bonn, T.4    Thorsell, A.G.5    Engstrom, O.6
  • 43
    • 0025223160 scopus 로고
    • Solution structure of the DNA-binding domain of the oestrogen receptor
    • Schwabe J.W., Neuhaus D., and Rhodes D. Solution structure of the DNA-binding domain of the oestrogen receptor. Nature 348 (1990) 458-461
    • (1990) Nature , vol.348 , pp. 458-461
    • Schwabe, J.W.1    Neuhaus, D.2    Rhodes, D.3
  • 44
    • 0027365669 scopus 로고
    • The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements
    • Schwabe J.W., Chapman L., Finch J.T., and Rhodes D. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 75 (1993) 567-578
    • (1993) Cell , vol.75 , pp. 567-578
    • Schwabe, J.W.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 46
    • 3142760881 scopus 로고    scopus 로고
    • DNA recognition by nuclear receptors
    • Claessens F., and Gewirth D.T. DNA recognition by nuclear receptors. Essays Biochem 40 (2004) 59-72
    • (2004) Essays Biochem , vol.40 , pp. 59-72
    • Claessens, F.1    Gewirth, D.T.2
  • 47
    • 56749130032 scopus 로고    scopus 로고
    • Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA
    • Chandra V., Huang P., Hamuro Y., Raghuram S., Wang Y., Burris T.P., et al. Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. Nature 456 (2008) 350-356
    • (2008) Nature , vol.456 , pp. 350-356
    • Chandra, V.1    Huang, P.2    Hamuro, Y.3    Raghuram, S.4    Wang, Y.5    Burris, T.P.6
  • 48
    • 0344527724 scopus 로고    scopus 로고
    • Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor
    • Baskakov I.V., Kumar R., Srinivasan G., Ji Y.S., Bolen D.W., and Thompson E.B. Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor. J Biol Chem 274 (1999) 10693-10696
    • (1999) J Biol Chem , vol.274 , pp. 10693-10696
    • Baskakov, I.V.1    Kumar, R.2    Srinivasan, G.3    Ji, Y.S.4    Bolen, D.W.5    Thompson, E.B.6
  • 49
    • 0033609855 scopus 로고    scopus 로고
    • Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor
    • Kumar R., Baskakov I.V., Srinivasan G., Bolen D.W., Lee J.C., and Thompson E.B. Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor. J Biol Chem 274 (1999) 24737-24741
    • (1999) J Biol Chem , vol.274 , pp. 24737-24741
    • Kumar, R.1    Baskakov, I.V.2    Srinivasan, G.3    Bolen, D.W.4    Lee, J.C.5    Thompson, E.B.6
  • 50
    • 0035947672 scopus 로고    scopus 로고
    • The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins
    • Kumar R., Lee J.C., Bolen D.W., and Thompson E.B. The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins. J Biol Chem 276 (2001) 18146-18152
    • (2001) J Biol Chem , vol.276 , pp. 18146-18152
    • Kumar, R.1    Lee, J.C.2    Bolen, D.W.3    Thompson, E.B.4
  • 51
    • 34548396816 scopus 로고    scopus 로고
    • Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor
    • Kumar R., Serrette J.M., Khan S.H., Miller A.L., and Thompson E.B. Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor. Arch Biochem Biophys 465 (2007) 452-460
    • (2007) Arch Biochem Biophys , vol.465 , pp. 452-460
    • Kumar, R.1    Serrette, J.M.2    Khan, S.H.3    Miller, A.L.4    Thompson, E.B.5
  • 52
    • 0035824562 scopus 로고    scopus 로고
    • The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties
    • Warnmark A., Wikstrom A., Wright A.P., Gustafsson J.A., and Hard T. The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. J Biol Chem 276 (2001) 45939-45944
    • (2001) J Biol Chem , vol.276 , pp. 45939-45944
    • Warnmark, A.1    Wikstrom, A.2    Wright, A.P.3    Gustafsson, J.A.4    Hard, T.5
  • 53
    • 26444526919 scopus 로고    scopus 로고
    • Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism
    • Wardell S.E., Kwok S.C., Sherman L., Hodges R.S., and Edwards D.P. Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism. Mol Cell Biol 25 (2005) 8792-8808
    • (2005) Mol Cell Biol , vol.25 , pp. 8792-8808
    • Wardell, S.E.1    Kwok, S.C.2    Sherman, L.3    Hodges, R.S.4    Edwards, D.P.5
  • 54
    • 0034629344 scopus 로고    scopus 로고
    • The N-terminal region of the human progesterone A-receptor. Structural analysis and the influence of the DNA binding domain
    • Bain D.L., Franden M.A., McManaman J.L., Takimoto G.S., and Horwitz K.B. The N-terminal region of the human progesterone A-receptor. Structural analysis and the influence of the DNA binding domain. J Biol Chem 275 (2000) 7313-7320
    • (2000) J Biol Chem , vol.275 , pp. 7313-7320
    • Bain, D.L.1    Franden, M.A.2    McManaman, J.L.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 55
    • 27744511919 scopus 로고    scopus 로고
    • Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations
    • Lavery D.N., and McEwan I.J. Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations. Biochem J 391 (2005) 449-464
    • (2005) Biochem J , vol.391 , pp. 449-464
    • Lavery, D.N.1    McEwan, I.J.2
  • 57
    • 0032581008 scopus 로고    scopus 로고
    • Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau1-core activation domain and target factors
    • Almlof T., Wallberg A.E., Gustafsson J.A., and Wright A.P.H. Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau1-core activation domain and target factors. Biochem 37 (1998) 9586-9594
    • (1998) Biochem , vol.37 , pp. 9586-9594
    • Almlof, T.1    Wallberg, A.E.2    Gustafsson, J.A.3    Wright, A.P.H.4
  • 58
    • 0037205522 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation
    • Reid J., Kelly S.M., Watt K., Price N.C., and McEwan I.J. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. J Biol Chem 277 (2002) 20079-20086
    • (2002) J Biol Chem , vol.277 , pp. 20079-20086
    • Reid, J.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 59
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky V.N., Oldfield C.J., and Dunker A.K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18 (2005) 343-384
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 60
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink A.L. Natively unfolded proteins. Curr Opin Struct Biol 15 (2005) 35-41
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 61
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker A.K., Cortese M.S., Romero P., Iakoucheva L.M., and Uversky V.N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 272 (2005) 5129-5148
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 62
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579 (2005) 3346-3354
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 64
    • 38149063767 scopus 로고    scopus 로고
    • Structural disorder promotes assembly of protein complexes
    • Hegyi H., Schad E., and Tompa P. Structural disorder promotes assembly of protein complexes. BMC Struct Biol 7 (2007) 65
    • (2007) BMC Struct Biol , vol.7 , pp. 65
    • Hegyi, H.1    Schad, E.2    Tompa, P.3
  • 65
    • 33744829805 scopus 로고    scopus 로고
    • Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation
    • Minezaki Y., Homma K., Kinjo A.R., and Nishikawa K. Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation. J Mol Biol 359 (2006) 1137-1149
    • (2006) J Mol Biol , vol.359 , pp. 1137-1149
    • Minezaki, Y.1    Homma, K.2    Kinjo, A.R.3    Nishikawa, K.4
  • 66
    • 58249105355 scopus 로고    scopus 로고
    • Role of intrinsically disordered protein regions/domains in transcriptional regulation
    • Garza A.S., Ahmad N., and Kumar R. Role of intrinsically disordered protein regions/domains in transcriptional regulation. Life Sci 84 (2009) 189-193
    • (2009) Life Sci , vol.84 , pp. 189-193
    • Garza, A.S.1    Ahmad, N.2    Kumar, R.3
  • 67
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker A., and Uversky V. Signal transduction via unstructured protein conduits. Nat Chem Biol 4 (2008) 229-230
    • (2008) Nat Chem Biol , vol.4 , pp. 229-230
    • Dunker, A.1    Uversky, V.2
  • 68
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H., and Wright P. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 12 (2002) 54-60
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.1    Wright, P.2
  • 69
    • 52249099866 scopus 로고    scopus 로고
    • Isoform-specific variation in the intrinsic disorder of troponin I
    • Hoffman R., and Sykes B. Isoform-specific variation in the intrinsic disorder of troponin I. Proteins 73 (2008) 338-350
    • (2008) Proteins , vol.73 , pp. 338-350
    • Hoffman, R.1    Sykes, B.2
  • 70
    • 33744829805 scopus 로고    scopus 로고
    • Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation
    • Minezaki Y., Homma K., Kinjo A., and Nishikawa K. Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation. J Mol Biol 359 (2006) 1137-1149
    • (2006) J Mol Biol , vol.359 , pp. 1137-1149
    • Minezaki, Y.1    Homma, K.2    Kinjo, A.3    Nishikawa, K.4
  • 71
    • 9344227341 scopus 로고    scopus 로고
    • TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain
    • Kumar R., Volk D., Li J., Lee J., Gorenstein D., and Thompson E. TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain. Proc Natl Acad Sci U S A 101 (2004) 16425-16430
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16425-16430
    • Kumar, R.1    Volk, D.2    Li, J.3    Lee, J.4    Gorenstein, D.5    Thompson, E.6
  • 72
    • 9644252804 scopus 로고    scopus 로고
    • Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions?
    • Mark W., Liao J., Lu Y., Ayed A., Laister R., Szymczyna B., et al. Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions?. J Mol Biol 345 (2005) 275-287
    • (2005) J Mol Biol , vol.345 , pp. 275-287
    • Mark, W.1    Liao, J.2    Lu, Y.3    Ayed, A.4    Laister, R.5    Szymczyna, B.6
  • 73
    • 1542743970 scopus 로고    scopus 로고
    • Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF
    • Kumar R., Betney R., Li J., Thompson E., and McEwan I. Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. Biochem 43 (2004) 3008-3013
    • (2004) Biochem , vol.43 , pp. 3008-3013
    • Kumar, R.1    Betney, R.2    Li, J.3    Thompson, E.4    McEwan, I.5
  • 74
    • 0029865110 scopus 로고    scopus 로고
    • Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors
    • Shen F., Triezenberg S., Hensley P., Porter D., and Knutson J. Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. J Biol Chem 271 (1996) 4827-4837
    • (1996) J Biol Chem , vol.271 , pp. 4827-4837
    • Shen, F.1    Triezenberg, S.2    Hensley, P.3    Porter, D.4    Knutson, J.5
  • 75
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: the fly-casting mechanism
    • Shoemaker B., Portman J., and Wolynes P. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci U S A 97 (2000) 8868-8873
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8868-8873
    • Shoemaker, B.1    Portman, J.2    Wolynes, P.3
  • 76
    • 34447558571 scopus 로고    scopus 로고
    • Intrinsic disorder in yeast transcriptional regulatory network
    • Singh G., and Dash D. Intrinsic disorder in yeast transcriptional regulatory network. Proteins 68 (2007) 602-605
    • (2007) Proteins , vol.68 , pp. 602-605
    • Singh, G.1    Dash, D.2
  • 77
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker B.A., Portman J.J., and Wolynes P.J. Speeding molecular recognition by using the folding funnel: The fly-casting mechanism. Proc Natl Acad Sci U S A 97 (2000) 8868-8873
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.J.3
  • 78
    • 0029740873 scopus 로고    scopus 로고
    • Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding
    • McEwan I., Dahlman-Wright K., Ford J., and Wright A. Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. Biochemistry 35 (1996) 9584-9593
    • (1996) Biochemistry , vol.35 , pp. 9584-9593
    • McEwan, I.1    Dahlman-Wright, K.2    Ford, J.3    Wright, A.4
  • 79
    • 0037154116 scopus 로고    scopus 로고
    • Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1)
    • Bienkiewicz E., Adkins J., and Lumb K. Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). Biochemistry 41 (2002) 752-759
    • (2002) Biochemistry , vol.41 , pp. 752-759
    • Bienkiewicz, E.1    Adkins, J.2    Lumb, K.3
  • 81
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11 (2002) 739-756
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.1
  • 82
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H., and Wright P. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6 (2005) 197-208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.1    Wright, P.2
  • 83
    • 0028073682 scopus 로고
    • A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform
    • Sartorius C.A., Melville M.Y., Hovland A.R., Tung L., Takimoto G.S., and Horwitz K.B. A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform. Mol Endocrinol 8 (1994) 1347-1360
    • (1994) Mol Endocrinol , vol.8 , pp. 1347-1360
    • Sartorius, C.A.1    Melville, M.Y.2    Hovland, A.R.3    Tung, L.4    Takimoto, G.S.5    Horwitz, K.B.6
  • 84
    • 33744492845 scopus 로고    scopus 로고
    • Activation function 1 of glucocorticoid receptor binds TATA-binding protein in vitro and in vivo
    • Copik A.J., Webb M.S., Miller A.L., Wang Y., Kumar R., and Thompson E.B. Activation function 1 of glucocorticoid receptor binds TATA-binding protein in vitro and in vivo. Mol Endocrinol 20 (2006) 1218-1230
    • (2006) Mol Endocrinol , vol.20 , pp. 1218-1230
    • Copik, A.J.1    Webb, M.S.2    Miller, A.L.3    Wang, Y.4    Kumar, R.5    Thompson, E.B.6
  • 85
    • 0037008749 scopus 로고    scopus 로고
    • Glucocorticoid receptor domain requirements for chromatin remodeling and transcriptional activation of the mouse mammary tumor virus promoter in different nucleoprotein contexts
    • Keeton E.K., Fletcher T.M., Baumann C.T., Hager G.L., and Smith C.L. Glucocorticoid receptor domain requirements for chromatin remodeling and transcriptional activation of the mouse mammary tumor virus promoter in different nucleoprotein contexts. J Biol Chem 277 (2002) 28247-28257
    • (2002) J Biol Chem , vol.277 , pp. 28247-28257
    • Keeton, E.K.1    Fletcher, T.M.2    Baumann, C.T.3    Hager, G.L.4    Smith, C.L.5
  • 86
  • 87
    • 0031473542 scopus 로고    scopus 로고
    • Mechanistic aspects of estrogen receptor activation probed with constitutively active estrogen receptors: correlations with DNA and coregulator interactions and receptor conformational changes
    • Lazennec G., Ediger T.R., Petz L.N., Nardulli A.M., and Katzenellenbogen B.S. Mechanistic aspects of estrogen receptor activation probed with constitutively active estrogen receptors: correlations with DNA and coregulator interactions and receptor conformational changes. Mol Endocrinol 11 (1997) 1375-1386
    • (1997) Mol Endocrinol , vol.11 , pp. 1375-1386
    • Lazennec, G.1    Ediger, T.R.2    Petz, L.N.3    Nardulli, A.M.4    Katzenellenbogen, B.S.5
  • 88
    • 34249667205 scopus 로고    scopus 로고
    • Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors
    • McEwan I.J., Lavery D., Fischer K., and Watt K. Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors. Nucl Recept Signal 5 (2007) e001
    • (2007) Nucl Recept Signal , vol.5
    • McEwan, I.J.1    Lavery, D.2    Fischer, K.3    Watt, K.4
  • 89
    • 0034161321 scopus 로고    scopus 로고
    • NPS@: Network protein sequence analysis
    • Combet C., Blanchet C., Geourjon C., and Deléage G. NPS@: Network protein sequence analysis. TIBS 25 3 [291] (2000) 147-150
    • (2000) TIBS , vol.25 , Issue.3 291 , pp. 147-150
    • Combet, C.1    Blanchet, C.2    Geourjon, C.3    Deléage, G.4


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