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Volumn 17, Issue 9, 2003, Pages 1704-1714

Helix 1/8 interactions influence the activity of nuclear receptor ligand-binding domains

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; LIGAND; NERVE GROWTH FACTOR BETA SUBUNIT; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA;

EID: 0042334874     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2003-0001     Document Type: Article
Times cited : (10)

References (29)
  • 1
    • 0035976638 scopus 로고    scopus 로고
    • Nuclear receptors and lipid physiology: Opening the X-files
    • Chawla A, Repa JJ, Evans RM, Mangelsdorf DJ 2001 Nuclear receptors and lipid physiology: opening the X-files. Science 294:1866-1870
    • (2001) Science , vol.294 , pp. 1866-1870
    • Chawla, A.1    Repa, J.J.2    Evans, R.M.3    Mangelsdorf, D.J.4
  • 3
    • 0035813090 scopus 로고    scopus 로고
    • Coregulator codes of transcriptional regulation by nuclear receptors
    • Rosenfeld MG, Glass CK 2001 Coregulator codes of transcriptional regulation by nuclear receptors. J Biol Chem 276:36865-36868
    • (2001) J Biol Chem , vol.276 , pp. 36865-36868
    • Rosenfeld, M.G.1    Glass, C.K.2
  • 5
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D 1995 Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. 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
  • 6
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis retinoic acid
    • Egea PF, Mitschler A, Rochel N, Ruff M, Chambon P, Moras D 2000 Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J 19:2592-601
    • (2000) EMBO J , vol.19 , pp. 2592-2601
    • Egea, P.F.1    Mitschler, A.2    Rochel, N.3    Ruff, M.4    Chambon, P.5    Moras, D.6
  • 10
    • 0022507916 scopus 로고
    • Comparison of the physicochemical properties of uterine nuclear estrogen receptors bound to estradiol or 4-hydroxytamoxifen
    • Attardi B, Happe HK 1986 Comparison of the physicochemical properties of uterine nuclear estrogen receptors bound to estradiol or 4-hydroxytamoxifen. Endocrinology 119:904-915
    • (1986) Endocrinology , vol.119 , pp. 904-915
    • Attardi, B.1    Happe, H.K.2
  • 11
    • 0030787737 scopus 로고    scopus 로고
    • Conformational studies of human vitamin-D receptor by antipeptide antibodies, partial proteolytic digestion and ligand binding
    • Vaisanen S, Juntunen K, Itkonen A, Vihko P, Maenpaa PH 1997 Conformational studies of human vitamin-D receptor by antipeptide antibodies, partial proteolytic digestion and ligand binding. Eur J Biochem 248:156-162
    • (1997) Eur J Biochem , vol.248 , pp. 156-162
    • Vaisanen, S.1    Juntunen, K.2    Itkonen, A.3    Vihko, P.4    Maenpaa, P.H.5
  • 13
    • 0029932761 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the human mineralocorticoid receptor occurs within its hetero-oligomeric structure
    • Couette B, Fagart J, Jalaguier S, Lombes M, Souque A, Rafestin-Oblin ME 1996 Ligand-induced conformational change in the human mineralocorticoid receptor occurs within its hetero-oligomeric structure. Biochem J 315:421-427
    • (1996) Biochem J , vol.315 , pp. 421-427
    • Couette, B.1    Fagart, J.2    Jalaguier, S.3    Lombes, M.4    Souque, A.5    Rafestin-Oblin, M.E.6
  • 14
    • 0028891989 scopus 로고
    • Ligand-induced conformational alterations of the androgen receptor analyzed by limited trypsinization. Studies on the mechanism of antiandrogen action
    • Kuil CW, Berrevoets CA, Mulder E 1995 Ligand-induced conformational alterations of the androgen receptor analyzed by limited trypsinization. Studies on the mechanism of antiandrogen action. J Biol Chem 270:27569-27576
    • (1995) J Biol Chem , vol.270 , pp. 27569-27576
    • Kuil, C.W.1    Berrevoets, C.A.2    Mulder, E.3
  • 15
    • 0028862855 scopus 로고
    • Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis
    • Seielstad DA, Carlson KE, Kushner PJ, Greene GL, Katzenellenbogen JA 1995 Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis. Biochemistry 34:12605-12615
    • (1995) Biochemistry , vol.34 , pp. 12605-12615
    • Seielstad, D.A.1    Carlson, K.E.2    Kushner, P.J.3    Greene, G.L.4    Katzenellenbogen, J.A.5
  • 16
    • 0035810957 scopus 로고    scopus 로고
    • Increase in the stability and helical content of estrogen receptor α in the presence of the estrogen response element: Analysis by circular dichroism spectroscopy
    • Greenfield N, Vijayanathan V, Thomas TJ, Gallo MA, Thomas T 2001 Increase in the stability and helical content of estrogen receptor α in the presence of the estrogen response element: analysis by circular dichroism spectroscopy. Biochemistry 40:6646-6652
    • (2001) Biochemistry , vol.40 , pp. 6646-6652
    • Greenfield, N.1    Vijayanathan, V.2    Thomas, T.J.3    Gallo, M.A.4    Thomas, T.5
  • 17
    • 0035431321 scopus 로고    scopus 로고
    • Structure of the PPARα and -γ ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family
    • Camb
    • Cronet P, Petersen JF, Folmer R, Blomberg N, Sjoblom K, Karlsson U, Lindstedt EL, Bamberg K 2001 Structure of the PPARα and -γ ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure (Camb) 9:699-706
    • (2001) Structure , vol.9 , pp. 699-706
    • Cronet, P.1    Petersen, J.F.2    Folmer, R.3    Blomberg, N.4    Sjoblom, K.5    Karlsson, U.6    Lindstedt, E.L.7    Bamberg, K.8
  • 18
    • 0034724560 scopus 로고    scopus 로고
    • Ligand-induced stabilization of PPARγ monitored by NMR spectroscopy: Implications for nuclear receptor activation
    • Johnson BA, Wilson EM, Li Y, Moller DE, Smith RG, Zhou G2000 Ligand-induced stabilization of PPARγ monitored by NMR spectroscopy: implications for nuclear receptor activation. J Mol Biol 298:187-194
    • (2000) J Mol Biol , vol.298 , pp. 187-194
    • Johnson, B.A.1    Wilson, E.M.2    Li, Y.3    Moller, D.E.4    Smith, R.G.5    Zhou, G.6
  • 19
    • 0033637850 scopus 로고    scopus 로고
    • Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding
    • Pissios P, Tzameli I, Kushner P, Moore DD 2000 Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding. Mol Cell 6:245-253
    • (2000) Mol Cell , vol.6 , pp. 245-253
    • Pissios, P.1    Tzameli, I.2    Kushner, P.3    Moore, D.D.4
  • 20
    • 0034986245 scopus 로고    scopus 로고
    • New insights into receptor ligand binding domains from a novel assembly assay
    • Pissios P, Tzameli I, Moore DD 2001 New insights into receptor ligand binding domains from a novel assembly assay. J Steroid Biochem Mol Biol 76:3-7
    • (2001) J Steroid Biochem Mol Biol , vol.76 , pp. 3-7
    • Pissios, P.1    Tzameli, I.2    Moore, D.D.3
  • 21
    • 0035091701 scopus 로고    scopus 로고
    • Comprehensive messenger ribonucleic acid profiling reveals that peroxisome proliferator-activated receptor γ activation has coordinate effects on gene expression in multiple insulin-sensitive tissues
    • Way JM, Harrington WW, Brown KK, Gottschalk WK, Sundseth SS, Mansfield TA, Ramachandran RK, Willson TM, Kliewer SA 2001 Comprehensive messenger ribonucleic acid profiling reveals that peroxisome proliferator-activated receptor γ activation has coordinate effects on gene expression in multiple insulin-sensitive tissues. Endocrinology 142:1269-1277
    • (2001) Endocrinology , vol.142 , pp. 1269-1277
    • Way, J.M.1    Harrington, W.W.2    Brown, K.K.3    Gottschalk, W.K.4    Sundseth, S.S.5    Mansfield, T.A.6    Ramachandran, R.K.7    Willson, T.M.8    Kliewer, S.A.9
  • 23
    • 0032514771 scopus 로고    scopus 로고
    • Trifluoroethanol promotes helix formation by destabilizing backbone exposure: Desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding
    • Kentsis A, Sosnick TR 1998 Trifluoroethanol promotes helix formation by destabilizing backbone exposure: desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry 37:14613-14622
    • (1998) Biochemistry , vol.37 , pp. 14613-14622
    • Kentsis, A.1    Sosnick, T.R.2
  • 24
    • 0032702675 scopus 로고    scopus 로고
    • A 13-amino acid amphipathic α-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A
    • Eilers AL, Billin AN, Liu J, Ayer DE 1999 A 13-amino acid amphipathic α-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A. J Biol Chem 274:32750-32756
    • (1999) J Biol Chem , vol.274 , pp. 32750-32756
    • Eilers, A.L.1    Billin, A.N.2    Liu, J.3    Ayer, D.E.4
  • 25
    • 0033696968 scopus 로고    scopus 로고
    • Solution structure of the interacting domains of the Mad-Sin3 complex: Implications for recruitment of a chromatin-modifying complex
    • Brubaker K, Cowley SM, Huang K, Loo L, Yochum GS, Ayer DE, Eisenman RN, Radhakrishnan I 2000 Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex. Cell 103:655-665
    • (2000) Cell , vol.103 , pp. 655-665
    • Brubaker, K.1    Cowley, S.M.2    Huang, K.3    Loo, L.4    Yochum, G.S.5    Ayer, D.E.6    Eisenman, R.N.7    Radhakrishnan, I.8
  • 29
    • 0019871847 scopus 로고
    • Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution
    • Wu CS, Ikeda K, Yang JT 1981 Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry 20:566-570
    • (1981) Biochemistry , vol.20 , pp. 566-570
    • Wu, C.S.1    Ikeda, K.2    Yang, J.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.