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Volumn 11, Issue 2, 2011, Pages 133-147

Induced Fit Simulations on Nuclear Receptors

Author keywords

Allosteric effect; Closed agonistic conformation; Helix H12 positioning; Ligand Binding Domain; Micro and macroscopic flexibility; Nuclear Receptor Superfamily; Open antagonistic conformation

Indexed keywords

4 HYDROXYTAMOXIFEN; ALDOSTERONE; ALITRETINOIN; AMINO ACID; ANDROGEN RECEPTOR; ANDROSTANOLONE; ANTINEOPLASTIC AGENT; ASOPRISNIL; BICULATAMIDE; BMS 614; CYPROTERONE ACETATE; DEACYLCORTIVAZOL; DEXAMETHASONE; EM 5477; ESTRADIOL; ESTROGEN; GLUCOCORTICOID RECEPTOR; HYDROXYFLUTAMIDE; MIFEPRISTONE; MOMETASONE FUROATE; NORETHISTERONE; PEROXISOME PROLIFERATOR; PHENYLPYRAZOLOGLUCOCORTICOID CORTIVAZOL; PROGESTERONE; RALOXIFENE; SPIRONOLACTONE; STEROID; TESTOSTERONE; UNCLASSIFIED DRUG; VITAMIN D RECEPTOR; WAY 244;

EID: 78649878888     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802611794863526     Document Type: Article
Times cited : (7)

References (88)
  • 1
    • 8844262660 scopus 로고    scopus 로고
    • Principles formodulation of the nuclear receptor superfamily
    • Gronemeyer, H.; Gustafsson, J.-Å.; Laudet, V. Principles formodulation of the nuclear receptor superfamily. Nature, 2004, 3, 950-964.
    • (2004) Nature , vol.3 , pp. 950-964
    • Gronemeyer, H.1    Gustafsson, J.-A.2    Laudet, V.3
  • 3
    • 0034306499 scopus 로고    scopus 로고
    • Nuclear receptorligand-binding domains: Three-dimensional structures, molecularinteractions and pharmacological implications
    • Bourguet, W.; Germain, P.; Gronemeyer, H.; Nuclear receptorligand-binding domains: three-dimensional structures, molecularinteractions and pharmacological implications. TiPS, 2000, 21, 381-388.
    • (2000) TiPS , vol.21 , pp. 381-388
    • Bourguet, W.1    Germain, P.2    Gronemeyer, H.3
  • 5
    • 0020594051 scopus 로고
    • Assessment of structural similarities in chick oviduct progesterone receptorsubunits by partial proteolysis of photoaffinity-labeled proteins
    • Birnbaumer, M.; Schrader, W. T.; O'Malley, B. W. Assessment of structural similarities in chick oviduct progesterone receptorsubunits by partial proteolysis of photoaffinity-labeled proteins. J.Biol. Chem., 1983, 258, 7331-7337.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7331-7337
    • Birnbaumer, M.1    Schrader, W.T.2    O'Malley, B.W.3
  • 6
    • 0021246674 scopus 로고
    • Characterization of the puried activated glucocorticoidreceptor from ratliver cytosol
    • Wrange, O.; Okret, S.; Radojcic, M.; Carlstedt-Duke, J.; Gustafsson, J. A. Characterization of the puried activated glucocorticoidreceptor from ratliver cytosol. J. Biol. Chem., 1984, 259, 4534-4541.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4534-4541
    • Wrange, O.1    Okret, S.2    Radojcic, M.3    Carlstedt-Duke, J.4    Gustafsson, J.A.5
  • 7
    • 34249667205 scopus 로고    scopus 로고
    • Natural disorderedsequences in the aminoterminal domain of nuclear receptors: Lessonsfrom the and rogen and glucocorticoid receptors
    • McEwan, I.J.; Lavery, D.; Fischer, K.; Watt, K. Natural disorderedsequences in the aminoterminal domain of nuclear receptors: lessonsfrom the and rogen and glucocorticoid receptors. Nucl. ReceptorSignal., 2007, 5, 1-6.
    • (2007) Nucl. ReceptorSignal. , vol.5 , pp. 1-6
    • McEwan, I.J.1    Lavery, D.2    Fischer, K.3    Watt, K.4
  • 8
    • 1542743970 scopus 로고    scopus 로고
    • Induced α-helix structure in AF1 of the and rogen receptor uponbinding transcription factor TFIIF
    • Kumar, R.; Betney, R.; Li, J.; Thompson, E. B.; McEwan, I. J.Induced α-helix structure in AF1 of the and rogen receptor uponbinding transcription factor TFIIF. Biochemistry, 2004, 43, 3008-3013.
    • (2004) Biochemistry , vol.43 , pp. 3008-3013
    • Kumar, R.1    Betney, R.2    Li, J.3    Thompson, E.B.4    McEwan, I.J.5
  • 9
    • 21344441515 scopus 로고    scopus 로고
    • Intra-domain communication between theN-terminal and DNA-binding domains of the and rogen receptor: Modulation of and rogen response element DNA binding
    • Brodie, J.; McEwan, I. J. Intra-domain communication between theN-terminal and DNA-binding domains of the and rogen receptor: modulation of and rogen response element DNA binding. J. Mol.Endocrinol., 2005, 34, 3008-3013.
    • (2005) J. Mol.Endocrinol. , vol.34 , pp. 3008-3013
    • Brodie, J.1    McEwan, I.J.2
  • 12
    • 0027770574 scopus 로고
    • Refined solution structure of the glucocorticoid receptor DNAbindingdomain
    • Baumann, H.; Paulsen, K.; Kovacs, H.; Berglund, H.; Wright A. P.Refined solution structure of the glucocorticoid receptor DNAbindingdomain. Biochemistry, 1993, 32, 13463-13471.
    • (1993) Biochemistry , vol.32 , pp. 13463-13471
    • Baumann, H.1    Paulsen, K.2    Kovacs, H.3    Berglund, H.4    Wright, A.P.5
  • 13
    • 0035369335 scopus 로고    scopus 로고
    • Nuclear-receptor interactions onDNA-response elements
    • Khorasanizadeh, S.; Rastinejad, F. Nuclear-receptor interactions onDNA-response elements. Trends Biochem. Sci., 2001, 26, 384-390.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 384-390
    • Khorasanizadeh, S.1    Rastinejad, F.2
  • 14
    • 43149125406 scopus 로고    scopus 로고
    • Structural basis for the nuclear import of the human and rogenreceptor
    • Cutress, M. L.; Whitaker, H. C.; Mills, I. G.; Stewart, M.; Neal, D.E. Structural basis for the nuclear import of the human and rogenreceptor. J. Cell Sci., 2008, 121, 957-968.
    • (2008) J. Cell Sci. , vol.121 , pp. 957-968
    • Cutress, M.L.1    Whitaker, H.C.2    Mills, I.G.3    Stewart, M.4    Neal, D.E.5
  • 15
    • 0029012163 scopus 로고
    • Crystal structure of the ligand binding domain of the human nucelarrecptor RXR-α
    • Bourguet, W.; Ruff, M.; Chambon, P.; Gronemeyer, H.; Moras, D.Crystal structure of the ligand binding domain of the human nucelarrecptor RXR-α. Nature, 1995, 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
  • 16
    • 34548496025 scopus 로고    scopus 로고
    • Modulation of and rogen receptor activation function 2by testosterone and dihydrotestosterone
    • Askew, E. B.; Gampe, Jr., R.T.; Stanley, T. B.; Faggart, J. L.; Wilson, E. M. Modulation of and rogen receptor activation function 2by testosterone and dihydrotestosterone. J. Biol. Chem., 2007, 282, 25801-15816.
    • (2007) J. Biol. Chem. , vol.282 , pp. 25801-15816
    • Askew, E.B.1    Gampe Jr., R.T.2    Stanley, T.B.3    Faggart, J.L.4    Wilson, E.M.5
  • 17
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans, R. M. The steroid and thyroid hormone receptor superfamily.Sciene, 1988, 240, 889-895.
    • (1988) Sciene , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 20
    • 0000680876 scopus 로고    scopus 로고
    • Nuclear Receptor Nomenclature Committee: A unified nomenclaturesystem for nuclear receptor superfamily
    • Nuclear Receptor Nomenclature Committee: A unified nomenclaturesystem for nuclear receptor superfamily. Cell., 1999, 97, 161-163.
    • (1999) Cell. , vol.97 , pp. 161-163
  • 21
    • 0030801841 scopus 로고    scopus 로고
    • Differential ligand activation of estrogen receptors ER alphaand ER beta at AP1 sites
    • Paech, K.; Webb, P.; Kuiper, G. G. J. M., Nilsson, S.; Gustafsson, J.-Å. Differential ligand activation of estrogen receptors ER alphaand ER beta at AP1 sites. Science, 1997, 277, 1508-1510.
    • (1997) Science , vol.277 , pp. 1508-1510
    • Paech, K.1    Webb, P.2    Kuiper, G.G.J.M.3    Nilsson, S.4    Gustafsson, J.-A.5
  • 22
    • 0029115972 scopus 로고
    • Correlationof retinoid binding affinity to retinoic acid receptor α withretinoid inhibition of growth of estrogen receptor-positive MCF-7mammary carcinoma cells
    • Dawson, M. I.; Chao, W.R.; Pine, P.; Jong, L.; Hobbs, P. D. Correlationof retinoid binding affinity to retinoic acid receptor α withretinoid inhibition of growth of estrogen receptor-positive MCF-7mammary carcinoma cells. Cancer Res., 1995, 55, 4446-4451.
    • (1995) Cancer Res. , vol.55 , pp. 4446-4451
    • Dawson, M.I.1    Chao, W.R.2    Pine, P.3    Jong, L.4    Hobbs, P.D.5
  • 23
    • 0029562846 scopus 로고    scopus 로고
    • Synthesis, structure-affinity relationships, and biological activitiesof ligand binding to retinoic acid receptors subtypes
    • Charpentier, B.; Bernardon, J. M.; Eustache, J.; Millois, C.; Martin, B. Synthesis, structure-affinity relationships, and biological activitiesof ligand binding to retinoic acid receptors subtypes. J. Med.Chem., 1998, 38, 4993-5006.
    • (1998) J. Med.Chem. , vol.38 , pp. 4993-5006
    • Charpentier, B.1    Bernardon, J.M.2    Eustache, J.3    Millois, C.4    Martin, B.5
  • 24
    • 0029894589 scopus 로고    scopus 로고
    • Celltypeand promoter-context dependent retinoic acid receptor (RAR)redundancies for RAR beta 2 and Hoxa-1 activation in F9 and P19cells can be artefactually generated by gene knockouts
    • Taneja, R.; Roy, B.; Plassat, J. L.; Zusi, C, F.; Ostrowski, J. Celltypeand promoter-context dependent retinoic acid receptor (RAR)redundancies for RAR beta 2 and Hoxa-1 activation in F9 and P19cells can be artefactually generated by gene knockouts. Proc. Natl.Acad. Sci. USA, 1996, 93, 6197-6202.
    • (1996) Proc. Natl.Acad. Sci. USA , vol.93 , pp. 6197-6202
    • Taneja, R.1    Roy, B.2    Plassat, J.L.3    Zusi, C.F.4    Ostrowski, J.5
  • 26
    • 0033253070 scopus 로고    scopus 로고
    • Steroid hormone receptors: Evolution, ligands and molecular basisof biologic function
    • Whitfield, G. K.; Jurutka, P. W.; Haussler, C. A.; Haussler, M. R.Steroid hormone receptors: evolution, ligands and molecular basisof biologic function. J. Cell. Biochem. Suppl., 1999, 32/33, 110-122.
    • (1999) J. Cell. Biochem. Suppl. , vol.32-33 , pp. 110-122
    • Whitfield, G.K.1    Jurutka, P.W.2    Haussler, C.A.3    Haussler, M.R.4
  • 27
    • 0034733912 scopus 로고    scopus 로고
    • Ligand-protein interactionsin nuclear receptors of hormones
    • Egea, P. F.; Klaholz, B. P.; Moras, D. Ligand-protein interactionsin nuclear receptors of hormones. FEBS Lett., 2000, 476, 62-67.
    • (2000) FEBS Lett. , vol.476 , pp. 62-67
    • Egea, P.F.1    Klaholz, B.P.2    Moras, D.3
  • 30
    • 0032446607 scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interactionby tamoxifen
    • Shiau, A. K.; Barstad, D.; Loria, P. M.; Cheng, L.; Kushner, P. J.; Agard, D.A.; Greene, G.L. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interactionby tamoxifen. Cell, 1995, 95, 927-937.
    • (1995) Cell , vol.95 , 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
  • 32
    • 19344376991 scopus 로고    scopus 로고
    • Recognition and Accommodation at the Androgen ReceptorCoactivator Binding Interface
    • Hur, E.; Pfaff, S. J.; Payne, E. S.; Grøn, H.; Buehrer, B. M.; Fletterick, R. J. Recognition and Accommodation at the Androgen ReceptorCoactivator Binding Interface. PLoS Biol., 2004, 2, 1303-1312.
    • (2004) PLoS Biol. , vol.2 , pp. 1303-1312
    • Hur, E.1    Pfaff, S.J.2    Payne, E.S.3    Grøn, H.4    Buehrer, B.M.5    Fletterick, R.J.6
  • 33
    • 85036720923 scopus 로고    scopus 로고
    • www.pdb.org
  • 34
    • 18044365802 scopus 로고    scopus 로고
    • Conformational adaptation of nuclear receptorligand binding domains to agonists: Potential for novel approachesto ligand design
    • Togashi, M.; Borngraeber, S.; Sandler, B.; Fletterick, R. J.; Webb, P.; Baxter, J. D. Conformational adaptation of nuclear receptorligand binding domains to agonists: Potential for novel approachesto ligand design. J. Steroid Biochem. Mol. Biol., 2005, 93, 127-137.
    • (2005) J. Steroid Biochem. Mol. Biol. , vol.93 , pp. 127-137
    • Togashi, M.1    Borngraeber, S.2    Sandler, B.3    Fletterick, R.J.4    Webb, P.5    Baxter, J.D.6
  • 36
    • 18044386870 scopus 로고    scopus 로고
    • Ligand control of coregulator recruitmentof nuclear receptor
    • Nettless, K. W.; Greene, G. L. Ligand control of coregulator recruitmentof nuclear receptor. Annu. Rev. Physiol., 2004.
    • (2004) Annu. Rev. Physiol.
    • Nettless, K.W.1    Greene, G.L.2
  • 39
    • 67349237917 scopus 로고    scopus 로고
    • Mechanism of and rogen receptor action
    • Kenny, P.W. Mechanism of and rogen receptor action. Maturitas, 2009, 63, 142-148.
    • (2009) Maturitas , vol.63 , pp. 142-148
    • Kenny, P.W.1
  • 40
    • 2342558431 scopus 로고    scopus 로고
    • Androgen receptor in prostate cancer
    • Heinlein, C. A.; Chang, C. Androgen receptor in prostate cancer.Endocr. Rev., 2004, 25, 276-308.
    • (2004) Endocr. Rev. , vol.25 , pp. 276-308
    • Heinlein, C.A.1    Chang, C.2
  • 42
    • 0013794946 scopus 로고
    • Two principles in endocrine therapy of cancers: Hormonedeprival and hormone interference
    • Huggins C. Two principles in endocrine therapy of cancers: hormonedeprival and hormone interference. Cancer Res., 1965, 25, 1163-1167.
    • (1965) Cancer Res. , vol.25 , pp. 1163-1167
    • Huggins, C.1
  • 43
    • 0033988067 scopus 로고    scopus 로고
    • Endocrine treatment in prostate cancer
    • Denis, L. J.; Griffiths, K. Endocrine treatment in prostate cancer.Semin. Surg. Oncol., 2000, 18, 52-74.
    • (2000) Semin. Surg. Oncol. , vol.18 , pp. 52-74
    • Denis, L.J.1    Griffiths, K.2
  • 46
    • 24744458589 scopus 로고    scopus 로고
    • Impact of induced fiton ligand binding to the and rogen receptor: A multidimensionalqsar study to predict endocrine-disrupting effects of environmentalchemicals
    • Lill, M. A.; Winiger, F.; Vedani, A.; Ernst, B. Impact of induced fiton ligand binding to the and rogen receptor: a multidimensionalqsar study to predict endocrine-disrupting effects of environmentalchemicals. J. Med. Chem., 2005, 48, 5666-5674.
    • (2005) J. Med. Chem. , vol.48 , pp. 5666-5674
    • Lill, M.A.1    Winiger, F.2    Vedani, A.3    Ernst, B.4
  • 47
    • 35648970526 scopus 로고    scopus 로고
    • Structural characterization of the humanandrogen receptor ligand-binding domain complexed withEM5744, a rationally designed steroidal ligand bearing a bulkychain directed toward helix 12
    • Cantin, L.; Faucher, F.; Couture, J.-F.; Pereira de Jesus-Tran, K.; Legrand, P.; Ciobanu, L. C.; Frechette, Y.; Labrecque, R.; Singh, S.M.; Labrie, F.; Breton, R. Structural characterization of the humanandrogen receptor ligand-binding domain complexed withEM5744, a rationally designed steroidal ligand bearing a bulkychain directed toward helix 12. J. Biol. Chem., 2007, 282, 30910-30919.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30910-30919
    • Cantin, L.1    Faucher, F.2    Couture, J.-F.3    Pereira de Jesus-Tran, K.4    Legrand, P.5    Ciobanu, L.C.6    Frechette, Y.7    Labrecque, R.8    Singh, S.M.9    Labrie, F.10    Breton, R.11
  • 48
    • 27844611242 scopus 로고    scopus 로고
    • Structuralbasis for accommodation of nonsteroidal ligands in the and rogenreceptor
    • Bohl, C. E.; Miller, D. D.; Chen, J.; Bell, C. E.; Dalton, J. T. Structuralbasis for accommodation of nonsteroidal ligands in the and rogenreceptor. J. Biol. Chem., 2005, 280, 37747-37754.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37747-37754
    • Bohl, C.E.1    Miller, D.D.2    Chen, J.3    Bell, C.E.4    Dalton, J.T.5
  • 49
    • 33646138016 scopus 로고    scopus 로고
    • Comparison of crystal structures of humanandrogen receptor ligand-binding domain complexed with variousagonists reveals molecular determinants responsible for binding affinity
    • Pereira de Jesus-Tran, K.; Cote, P. L.; Cantin, L.; Blanchet, J.; Labrie, F.; Breton, R. Comparison of crystal structures of humanandrogen receptor ligand-binding domain complexed with variousagonists reveals molecular determinants responsible for binding affinity.Protein Sci., 2006, 15, 987-999.
    • (2006) Protein Sci. , vol.15 , pp. 987-999
    • Pereira de Jesus-Tran, K.1    Cote, P.L.2    Cantin, L.3    Blanchet, J.4    Labrie, F.5    Breton, R.6
  • 50
    • 34250365377 scopus 로고    scopus 로고
    • Crystalstructure of the t877a human and rogen receptor ligand-binding domaincomplexed to cyproterone acetate provides insight for ligandinduced conformational changes and structure-based drug design
    • Bohl, C. E.; Wu, Z.; Miller, D. D.; Bell, C. E.; Dalton, J. T. Crystalstructure of the t877a human and rogen receptor ligand-binding domaincomplexed to cyproterone acetate provides insight for ligandinduced conformational changes and structure-based drug design.J. Biol. Chem., 2008, 282, 13648-13655.
    • (2008) J. Biol. Chem. , vol.282 , pp. 13648-13655
    • Bohl, C.E.1    Wu, Z.2    Miller, D.D.3    Bell, C.E.4    Dalton, J.T.5
  • 51
    • 55949119492 scopus 로고    scopus 로고
    • Molecular basis of agonicity and antagonicity in the and rogen receptor studiedby moleculardynamics simulations
    • Bisson, W. H.; Abagyan, R.; Cavasotto, C. N. Molecular basis of agonicity and antagonicity in the and rogen receptor studiedby moleculardynamics simulations. J. Mol. Graph. Model., 2008, 27, 452-458.
    • (2008) J. Mol. Graph. Model. , vol.27 , pp. 452-458
    • Bisson, W.H.1    Abagyan, R.2    Cavasotto, C.N.3
  • 52
    • 0028891989 scopus 로고
    • Ligand-induced conformationalalterations of the and rogen receptor analyzed by limitedtrypsinization
    • Kuil, C. W.; Berrevoets, C. A.; Mulder, E. Ligand-induced conformationalalterations of the and rogen receptor analyzed by limitedtrypsinization. J. Biol. Chem., 1995, 270, 27569-27576.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27569-27576
    • Kuil, C.W.1    Berrevoets, C.A.2    Mulder, E.3
  • 53
    • 0028181765 scopus 로고
    • Agonists, but not antagonists, alter the conformation of the hormone-binding domain of androgen receptor
    • Kallio, P. J.; Janne, O. A.; Palvimo, J. J. Agonists, but not antagonists, alter the conformation of the hormone-binding domain of androgen receptor. Endocrinology, 1994, 134, 998-1001.
    • (1994) Endocrinology , vol.134 , pp. 998-1001
    • Kallio, P.J.1    Janne, O.A.2    Palvimo, J.J.3
  • 54
    • 0028283503 scopus 로고
    • Molecular mechanism of action of steroid/thyroid receptor superfamily members
    • Tsai, M.-J.; O'Malley, B. W. Molecular mechanism of action of steroid/thyroid receptor superfamily members. Annu. Rev., 1994, 63, 451-486.
    • (1994) Annu. Rev. , vol.63 , pp. 451-486
    • Tsai, M.-J.1    O'Malley, B.W.2
  • 55
    • 24744458589 scopus 로고    scopus 로고
    • Impact of induced fiton ligand binding to the and rogen receptor: A multidimensionalqsar study to predict endocrine-disrupting effects of environmentalchemicals
    • Lill, M. A.; Winiger, F.; Vedani, A.; Ernst. B. Impact of induced fiton ligand binding to the and rogen receptor: a multidimensionalqsar study to predict endocrine-disrupting effects of environmentalchemicals. J. Med. Chem., 2005, 48, 5666-5674.
    • (2005) J. Med. Chem. , vol.48 , pp. 5666-5674
    • Lill, M.A.1    Winiger, F.2    Vedani, A.3    Ernst, B.4
  • 56
    • 18144399332 scopus 로고    scopus 로고
    • The human glucocorticoid receptor: Onegene, multiple proteins and diverse responses
    • Zhou, J.; Cidlowski, J. A. The human glucocorticoid receptor: Onegene, multiple proteins and diverse responses. Steroids, 2005, 70, 407-417.
    • (2005) Steroids , vol.70 , pp. 407-417
    • Zhou, J.1    Cidlowski, J.A.2
  • 58
    • 1642416888 scopus 로고    scopus 로고
    • Glucocorticoid actionnetworks-anintroduction to systems biology
    • Chrousos, G. P., Charmandari, E.; Kino, T. Glucocorticoid actionnetworks-anintroduction to systems biology. J. Clin. Endocrinol.Metab., 2004, 89, 563-564.
    • (2004) J. Clin. Endocrinol.Metab. , vol.89 , pp. 563-564
    • Chrousos, G.P.1    Charmandari, E.2    Kino, T.3
  • 59
    • 3843071883 scopus 로고    scopus 로고
    • The glucocorticoid receptor gene, longevity, and the complexdisorders of Western societies
    • Chrousos, G. P. The glucocorticoid receptor gene, longevity, and the complexdisorders of Western societies. Am. J. Med., 2004, 117, 204-207.
    • (2004) Am. J. Med. , vol.117 , pp. 204-207
    • Chrousos, G.P.1
  • 62
    • 8444227037 scopus 로고    scopus 로고
    • Selectivemodulation of glucocorticoid receptor function toward developmentof novel antiinflammation: Lessons from a phenylpyrazolosteroidcortivazol
    • Tanaka, H.; Yoshikawa, N.; Shimizu, N.; Morimoto, C. Selectivemodulation of glucocorticoid receptor function toward developmentof novel antiinflammation: lessons from a phenylpyrazolosteroidcortivazol. Mod. Rheumatol., 2004, 14, 347-355.
    • (2004) Mod. Rheumatol. , vol.14 , pp. 347-355
    • Tanaka, H.1    Yoshikawa, N.2    Shimizu, N.3    Morimoto, C.4
  • 63
    • 0038320627 scopus 로고    scopus 로고
    • Glucocorticoids: New mechanisms and future agents
    • Adcock, I. M. Glucocorticoids: new mechanisms and future agents.Curr. Allergy Asthma Rep., 2003, 3, 249-257.
    • (2003) Curr. Allergy Asthma Rep. , vol.3 , pp. 249-257
    • Adcock, I.M.1
  • 65
    • 0021895459 scopus 로고    scopus 로고
    • [3H] cortivazol: A unique high affinity ligand for the glucocorticoidreceptor
    • Schlechte, J. A.; Simons, Jr. S. S.; Lewis, D. A.; Thompson, E. B. [3H] cortivazol: a unique high affinity ligand for the glucocorticoidreceptor. Endocrinology, 1998, 117, 1355-1362.
    • (1998) Endocrinology , vol.117 , pp. 1355-1362
    • Schlechte, J.A.1    Simons Jr., S.S.2    Lewis, D.A.3    Thompson, E.B.4
  • 67
    • 0018789810 scopus 로고
    • Antiinflammatorypyrazolo-steroids: Potent glucocorticoids containingbulky A-ring substituents and no C3-carbonyl
    • Simons, S. S. Jr.; Thompson, E. B.; Johnson, D. F. Antiinflammatorypyrazolo-steroids: potent glucocorticoids containingbulky A-ring substituents and no C3-carbonyl. Biochem. Biophys.Res. Commun., 1979, 86, 792-800.
    • (1979) Biochem. Biophys.Res. Commun. , vol.86 , pp. 792-800
    • Simons Jr., S.S.1    Thompson, E.B.2    Johnson, D.F.3
  • 68
    • 0024507978 scopus 로고
    • Interactions of thephenylpyrazolo steroid cortivazol with glucocorticoid receptors insteroidsensitive and -resistant human leukemic cells
    • Thompson, E. B.; Srivastava, D.; Johnson, B. H. Interactions of thephenylpyrazolo steroid cortivazol with glucocorticoid receptors insteroidsensitive and -resistant human leukemic cells. Cancer Res., 1989, 49, 2253-2258.
    • (1989) Cancer Res. , vol.49 , pp. 2253-2258
    • Thompson, E.B.1    Srivastava, D.2    Johnson, B.H.3
  • 70
    • 55949116957 scopus 로고    scopus 로고
    • Induced-fit docking of mometasone furoate and further evidence for glucocorticoid receptor17α pocket flexibility
    • Wanga, H.; Aslanian, R.; Madison, V. S. Induced-fit docking of mometasone furoate and further evidence for glucocorticoid receptor17α pocket flexibility. J. Mol. Graph. Model., 2008, 27, 512-521.
    • (2008) J. Mol. Graph. Model. , vol.27 , pp. 512-521
    • Wanga, H.1    Aslanian, R.2    Madison, V.S.3
  • 71
    • 0037764882 scopus 로고    scopus 로고
    • Glucocorticoid receptor interactionswith glucocorticoids: Evaluation by molecular modeling and functionalanalysis of glucocorticoid receptor mutants
    • Hammer, S.; Spika, I.; Sippl, W.; Jessen, G.; Kleuser, B.; Höltje, H.-D.; Schäfer-Korting, M. Glucocorticoid receptor interactionswith glucocorticoids: evaluation by molecular modeling and functionalanalysis of glucocorticoid receptor mutants. Steroids. 2003, 68, 329-339.
    • (2003) Steroids , vol.68 , pp. 329-339
    • Hammer, S.1    Spika, I.2    Sippl, W.3    Jessen, G.4    Kleuser, B.5    Höltje, H.-D.6    Schäfer-Korting, M.7
  • 73
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographiccomparison of the estrogen and progesterone receptor'sligand binding domains
    • Tanenbaum, D. M.; Wang, Y.; Williams, S. P.; Sigler, P. B. Crystallographiccomparison of the estrogen and progesterone receptor'sligand binding domains. Proc. Natl. Acad. Sci USA, 1998, 95, 5998-6003.
    • (1998) Proc. Natl. Acad. Sci USA , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 75
    • 0033775525 scopus 로고    scopus 로고
    • Molecular mechanisms of selectiveestrogen receptor modulator (SERM) action
    • Dutertre, M.; Smith, C. L. Molecular mechanisms of selectiveestrogen receptor modulator (SERM) action. J. Pharmacol. Exp.Ther., 2000, 295, 431-437.
    • (2000) J. Pharmacol. Exp.Ther. , vol.295 , pp. 431-437
    • Dutertre, M.1    Smith, C.L.2
  • 76
    • 0027495966 scopus 로고
    • Ligand-mediated modulation of estrogen receptor conformation by estradiolanalogs
    • Schwartz, J. A.; Skafar, D. F. Ligand-mediated modulation of estrogen receptor conformation by estradiolanalogs. Biochemistry., 1993, 32, 10109-10115.
    • (1993) Biochemistry. , vol.32 , pp. 10109-10115
    • Schwartz, J.A.1    Skafar, D.F.2
  • 78
    • 41549111672 scopus 로고    scopus 로고
    • Insights intoligand selectivity in estrogen receptor isoforms: Molecular dynamicssimulations and binding free energy calculations
    • Zeng, J.; Li, W.; Zhao, Y.; Liu, G.; Tang, Y.; Jiang, H. Insights intoligand selectivity in estrogen receptor isoforms: molecular dynamicssimulations and binding free energy calculations. J. Phys.Chem. B, 2008, 112, 2719-2726.
    • (2008) J. Phys.Chem. B , vol.112 , pp. 2719-2726
    • Zeng, J.1    Li, W.2    Zhao, Y.3    Liu, G.4    Tang, Y.5    Jiang, H.6
  • 80
    • 33847114057 scopus 로고    scopus 로고
    • Conformational dynamics of the estrogen receptor r: Molecular dynamics simulations of the influenceof binding site structure on protein dynamics
    • Celik, L.; Lund, J. D. D.; Schiøtt, B. Conformational dynamics of the estrogen receptor r: molecular dynamics simulations of the influenceof binding site structure on protein dynamics. Biochemistry, 2007, 46, 1743-1758.
    • (2007) Biochemistry , vol.46 , pp. 1743-1758
    • Celik, L.1    Lund, J.D.D.2    Schiøtt, B.3
  • 81
    • 46149089650 scopus 로고    scopus 로고
    • Preliminary moleculardynamic simulations of the estrogen receptor alpha ligand bindingdomain from antagonist to apo
    • McGee, T. D.; Edwards, J.; Roitberg, A. E. Preliminary moleculardynamic simulations of the estrogen receptor alpha ligand bindingdomain from antagonist to apo. Int. J. Environ. Res. Public, 2008, 5, 111-114.
    • (2008) Int. J. Environ. Res. Public , vol.5 , pp. 111-114
    • McGee, T.D.1    Edwards, J.2    Roitberg, A.E.3
  • 85
    • 67749148919 scopus 로고    scopus 로고
    • The x-raystructure of ru486 bound to the progesterone receptor in a destabilizedagonistic conformation
    • Raaijmakers, H.; Versteegh, J. E.; Uitdehaag, J. C. M. The x-raystructure of ru486 bound to the progesterone receptor in a destabilizedagonistic conformation. J. Biol. Chem., 2009, 284, 19572-19579.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19572-19579
    • Raaijmakers, H.1    Versteegh, J.E.2    Uitdehaag, J.C.M.3
  • 86
    • 0032924018 scopus 로고    scopus 로고
    • Investigation of the bindinginteractions of progesterone using muteins of the human progesteronereceptor ligand binding domain designed on the basis of athree-dimensional protein model
    • Letz, M.; Bringmann, P.; Mann, M.; Mueller-Fahrnow, A.; Reipert, D.; Scholz, P.; Wurtz, J. M.; Egner, U. Investigation of the bindinginteractions of progesterone using muteins of the human progesteronereceptor ligand binding domain designed on the basis of athree-dimensional protein model. Biochim. Biophy. Acta, 1999, 1429, 391-400.
    • (1999) Biochim. Biophy. Acta , vol.1429 , pp. 391-400
    • Letz, M.1    Bringmann, P.2    Mann, M.3    Mueller-Fahrnow, A.4    Reipert, D.5    Scholz, P.6    Wurtz, J.M.7    Egner, U.8


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