메뉴 건너뛰기




Volumn 6, Issue 10, 2007, Pages 811-820

Design of selective nuclear receptor modulators: RAR and RXR as a case study

Author keywords

[No Author keywords available]

Indexed keywords

14 HYDROXY 4,14 RETRORETINOL; 4 (5,6,7,8 TETRAHYDRO 5,5,8,8 TETRAMETHYL 2 ANTHRYL)BENZOIC ACID; 4 (5,6,7,8 TETRAHYDRO 5,5,8,8 TETRAMETHYL 2 NAPHTHALENYL) 2 NAPHTHALENE CARBOXYLIC ACID; 4 [2 (5,6,7,8 TETRAHYDRO 5,5,8,8 TETRAMETHYL 2 NAPHTHYL) 1,3 DIOXOLAN 2 YL]BENZOIC ACID; 4 [2 [5,5 DIMETHYL 8 (2 PHENYLETHYNYL) 5,6 DIHYDRONAPHTHALEN 2 YL]ETHEN 1 YL]BENZOIC ACID; 4 [2 [5,6 DIHYDRO 5,5 DIMETHYL 8 (4 METHYLPHENYL) 2 NAPHTHYL]ETHYNYL]BENZOIC ACID; 4 AMINO 2 (BUTYRYLAMINO)PHENYLRETINAMIDE; 6 [3 (1 ADAMANTYL) 4 HYDROXYPHENYL] 2 NAPHTHOIC ACID; ACYCLIC RETINOID; AGN 193918; ALITRETINOIN; AMINOAROTINOID; ANHYDRORETINOL; ANTINEOPLASTIC AGENT; BEXAROTENE; BMS 204493; CD 2674; FENRETINIDE; MOFAROTENE; MX 781; NIK 333; RETINOIC ACID; RETINOIC ACID RECEPTOR; RETINOIC ACID RECEPTOR MODULATOR; RETINOIC ACID RECEPTOR STIMULATING AGENT; RETINOID DERIVATIVE; RETINOID X RECEPTOR; RETINOID X RECEPTOR BLOCKING AGENT; RETINOID X RECEPTOR MODULATOR; RETINOID X RECEPTOR STIMULATING AGENT; REXINOID; RO 13 7419; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 34848862778     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd2398     Document Type: Review
Times cited : (237)

References (59)
  • 2
    • 8844262660 scopus 로고    scopus 로고
    • Principles for modulation of the nuclear receptor superfamily
    • Gronemeyer, H., Gustafsson, J, A. & Laudet, V. Principles for modulation of the nuclear receptor superfamily. Nature Rev. Drug Disc. 3 950-964 (2004).
    • (2004) Nature Rev. Drug Disc , vol.3 , pp. 950-964
    • Gronemeyer, H.1    Gustafsson, J.A.2    Laudet, V.3
  • 3
    • 33144488245 scopus 로고    scopus 로고
    • Function of retinoid nuclear receptors: Lessons from genetic and pharmacological dissections of the retinoic acid signalling pathway during mouse embryogenesis
    • Mark, M., Ghyselinck, N. B. & Chambon, P. Function of retinoid nuclear receptors: Lessons from genetic and pharmacological dissections of the retinoic acid signalling pathway during mouse embryogenesis. Annu. Rev. Pharmacol. Taxicol. 46, 451-480 (2005).
    • (2005) Annu. Rev. Pharmacol. Taxicol , vol.46 , pp. 451-480
    • Mark, M.1    Ghyselinck, N.B.2    Chambon, P.3
  • 4
    • 2942621879 scopus 로고    scopus 로고
    • In vivo activation of PPAR target genes by RXR, homodimers
    • Upenberg, A. et al. In vivo activation of PPAR target genes by RXR, homodimers. EMBO J. 23, 2083-2091 (2004).
    • (2004) EMBO J , vol.23 , pp. 2083-2091
    • Upenberg, A.1
  • 5
    • 0034672081 scopus 로고    scopus 로고
    • Docosahexaenoic acid, a ligand for the retinoid X receptor in mouse brain
    • de Urquiza, A. M. et al. Docosahexaenoic acid, a ligand for the retinoid X receptor in mouse brain. Science 290, 2140-2144 (2000).
    • (2000) Science , vol.290 , pp. 2140-2144
    • de Urquiza, A.M.1
  • 6
    • 4043140077 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids including docosahexaenoic and arachidonic acid bind to the retinoid X receptor α ligand-binding domain
    • Lengqvist, J. et al. Polyunsaturated fatty acids including docosahexaenoic and arachidonic acid bind to the retinoid X receptor α ligand-binding domain. Mol. Cell. Proteomics 3, 692-703 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 692-703
    • Lengqvist, J.1
  • 7
    • 0036897019 scopus 로고    scopus 로고
    • Selective retinoids and rexinoids in cancer therapy and chemo-prevention
    • Zusi, F. C., Lorenzi, M. V. & Vivat-Hannah, V. Selective retinoids and rexinoids in cancer therapy and chemo-prevention. Drug Discov. Today 7, 1165-1174 (2002).
    • (2002) Drug Discov. Today , vol.7 , pp. 1165-1174
    • Zusi, F.C.1    Lorenzi, M.V.2    Vivat-Hannah, V.3
  • 8
    • 2442608526 scopus 로고    scopus 로고
    • Synthetic retinoids and their nuclear, receptors
    • Dawson, M. I. Synthetic retinoids and their nuclear, receptors. Curr. Med. Chem. Anticancer Agents 4, 199-230 (2004).
    • (2004) Curr. Med. Chem. Anticancer Agents , vol.4 , pp. 199-230
    • Dawson, M.I.1
  • 9
    • 0034306499 scopus 로고    scopus 로고
    • Nuclear receptor ligand-binding domains: Three-dimensional structures, molecular interactions and pharmacological implications
    • Bourguet, W., Cermain, P. & Gronemeyer, H. Nuclear receptor ligand-binding domains: Three-dimensional structures, molecular interactions and pharmacological implications. Trends Pharmacol. Sci. 21, 381-388 (2000).
    • (2000) Trends Pharmacol. Sci , vol.21 , pp. 381-388
    • Bourguet, W.1    Cermain, P.2    Gronemeyer, H.3
  • 10
    • 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. & Maras, D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375, 377-382 (1995).
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Maras, D.5
  • 11
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis retinoic acid
    • Egea, P. F. et al. Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J. 19, 2592-2601 (2000).
    • (2000) EMBO J , vol.19 , pp. 2592-2601
    • Egea, P.F.1
  • 12
    • 0030056997 scopus 로고    scopus 로고
    • A canonical structure for the ligand-binding domain of nuclear receptors
    • Wurtz, J. M. et al. A canonical structure for the ligand-binding domain of nuclear receptors. Nature Struct. Biol. 3, 87-94 (1996).
    • (1996) Nature Struct. Biol , vol.3 , pp. 87-94
    • Wurtz, J.M.1
  • 13
    • 0036515648 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Multiple modes of modification
    • Hermanson, O., Glass, C. K. & Rosenfeld, M. G. Nuclear receptor coregulators: Multiple modes of modification. Trends Endocrinol. Metab. 13, 55-60 (2002).
    • (2002) Trends Endocrinol. Metab , vol.13 , pp. 55-60
    • Hermanson, O.1    Glass, C.K.2    Rosenfeld, M.G.3
  • 14
    • 1442351143 scopus 로고    scopus 로고
    • Coregulator function: A key to understanding tissue specificity of selective receptor modulators
    • Smith, C. L. & O'Malley, B. W. Coregulator function: A key to understanding tissue specificity of selective receptor modulators. Endocr. Rev. 25, 45-71 (2004).
    • (2004) Endocr. Rev , vol.25 , pp. 45-71
    • Smith, C.L.1    O'Malley, B.W.2
  • 15
    • 18844373937 scopus 로고    scopus 로고
    • Transcriptional regulation by steroid receptor coactivator phosphorylation
    • Wu, R. C., Smith, C. L. & O'Malley, B. W. Transcriptional regulation by steroid receptor coactivator phosphorylation. Endocr. Rev. 26 393-399 (2005).
    • (2005) Endocr. Rev , vol.26 , pp. 393-399
    • Wu, R.C.1    Smith, C.L.2    O'Malley, B.W.3
  • 16
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • Bourguet, W. et al. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol. Cell 5, 289-298 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 289-298
    • Bourguet, W.1
  • 17
    • 0030865548 scopus 로고    scopus 로고
    • A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers
    • Vivat, V. et al. A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers. EMBO J. 16, 5697-5709 (1997).
    • (1997) EMBO J , vol.16 , pp. 5697-5709
    • Vivat, V.1
  • 18
    • 0142027868 scopus 로고    scopus 로고
    • Separation of retinoid X receptor homo- and heterodimerization functions
    • Vivat-Hannah, V., Bourguet, W., Gottardis, M. & Gronemeyer, H. Separation of retinoid X receptor homo- and heterodimerization functions. Mol. Cell. Biol. 23, 7678-7688 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7678-7688
    • Vivat-Hannah, V.1    Bourguet, W.2    Gottardis, M.3    Gronemeyer, H.4
  • 19
    • 0037050017 scopus 로고    scopus 로고
    • Coregulator recruitment and the mechanism of retinoic acid receptor synergy
    • Germain, P., Iyer, J., Zechel, C. & Gronemeyer, H. Coregulator recruitment and the mechanism of retinoic acid receptor synergy. Nature 415, 187-192 (2002).
    • (2002) Nature , vol.415 , pp. 187-192
    • Germain, P.1    Iyer, J.2    Zechel, C.3    Gronemeyer, H.4
  • 20
    • 0033681001 scopus 로고    scopus 로고
    • Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors
    • Gampe, R. T. Jr et al. Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol. Cell 5, 545-555 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 545-555
    • Gampe Jr, R.T.1
  • 21
    • 2442560527 scopus 로고    scopus 로고
    • Signature of the oligomeric behaviour of nuclear receptors at the sequence and structural level
    • 423-429
    • Brelivet, Y., Kammerer, S., Rachel, N., Poch, O. & Moras, D. Signature of the oligomeric behaviour of nuclear receptors at the sequence and structural level. EMBO Rep. 5, 423-429 (2004).
    • (2004) EMBO Rep , vol.5
    • Brelivet, Y.1    Kammerer, S.2    Rachel, N.3    Poch, O.4    Moras, D.5
  • 22
    • 1642304065 scopus 로고    scopus 로고
    • Structural determinants of allosteric ligand activation in RXR heterodimers
    • Shulman, A. I., Larson, C., Mangelsdorf, D. J. & Ranganathan, R. Structural determinants of allosteric ligand activation in RXR heterodimers. Cell 116, 417-429 (2004).
    • (2004) Cell , vol.116 , pp. 417-429
    • Shulman, A.I.1    Larson, C.2    Mangelsdorf, D.J.3    Ranganathan, R.4
  • 23
    • 1242294391 scopus 로고    scopus 로고
    • Allosteric control of ligand selectivity between estrogen receptors α and β: Implications for other nuclear receptors
    • Nettles, K. W. et al. Allosteric control of ligand selectivity between estrogen receptors α and β: Implications for other nuclear receptors. Mol. Cell 13, 317-327 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 317-327
    • Nettles, K.W.1
  • 24
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda, A. & Pascual, A. Nuclear hormone receptors and gene expression. Physiol. Rev. 81, 1269-1304 (2001).
    • (2001) Physiol. Rev , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 25
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna, N. J. & O'Malley, B. W. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108, 465-474 (2002).
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 26
    • 0034705595 scopus 로고    scopus 로고
    • Recruitment of nuclear receptor corepressor and coactivator to the retinoic acid receptor by retinoid ligands. Influence of DNA-heterodimer interactions
    • Klein, E. S., Wang, J. W., Khalifa, B., Gavigan. S. A. & Chandraratna, R. A. Recruitment of nuclear receptor corepressor and coactivator to the retinoic acid receptor by retinoid ligands. Influence of DNA-heterodimer interactions. J. Biol. Chem. 275, 19401-19408 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 19401-19408
    • Klein, E.S.1    Wang, J.W.2    Khalifa, B.3    Gavigan, S.A.4    Chandraratna, R.A.5
  • 27
    • 0019189707 scopus 로고
    • Arotinoids: A new class of highly active retinoids
    • Loeliger, P., Bollag, W. & Mayer, H. Arotinoids: A new class of highly active retinoids. Eur. J. Med. Chem. 15, 9-15 (1980).
    • (1980) Eur. J. Med. Chem , vol.15 , pp. 9-15
    • Loeliger, P.1    Bollag, W.2    Mayer, H.3
  • 29
    • 8844273694 scopus 로고    scopus 로고
    • Rational design of RAR-selective ligands revealed by RARβ crystal stucture
    • 877-882
    • Germain, P. et al. Rational design of RAR-selective ligands revealed by RARβ crystal stucture. EMBO Rep. 5, 877-882 (2004).
    • (2004) EMBO Rep , vol.5
    • Germain, P.1
  • 30
    • 0029811878 scopus 로고    scopus 로고
    • Identification and functional separation of retinoic acid receptor neutral antagonists and inverse agonists
    • Klein, E. S. et al. Identification and functional separation of retinoic acid receptor neutral antagonists and inverse agonists. J. Biol. Chem. 271, 22692-22696 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 22692-22696
    • Klein, E.S.1
  • 31
    • 0031892525 scopus 로고    scopus 로고
    • Conformational adaptation of agonists to the human nuclear receptor RARγ
    • Klaholz, B. P. et al. Conformational adaptation of agonists to the human nuclear receptor RARγ. Nature Struct. Biol. 5, 199-202 (1998).
    • (1998) Nature Struct. Biol , vol.5 , pp. 199-202
    • Klaholz, B.P.1
  • 32
    • 0029044946 scopus 로고
    • Activation of mammalian retinoid X receptors by the insect growth regulator methoprene
    • Harmon, M. A., Boehm, M. F., Heyman, R. A. & Mangelsdorf, D. J. Activation of mammalian retinoid X receptors by the insect growth regulator methoprene. Proc. Natl Acad. Sci. USA 92, 6157-6160 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6157-6160
    • Harmon, M.A.1    Boehm, M.F.2    Heyman, R.A.3    Mangelsdorf, D.J.4
  • 33
    • 9344249538 scopus 로고    scopus 로고
    • Phytol metabolites are circulating dietary factors that activate the nuclear receptor RXR
    • Kitareewan, S. et al. Phytol metabolites are circulating dietary factors that activate the nuclear receptor RXR. Mol. Cell. Biol. 7, 1153-1166 (1996).
    • (1996) Mol. Cell. Biol , vol.7 , pp. 1153-1166
    • Kitareewan, S.1
  • 34
    • 0029664544 scopus 로고    scopus 로고
    • Phytanic acid is a retinoid X receptor ligand
    • LeMotte, P. K., Keidek, S. & Apfel, C. M. Phytanic acid is a retinoid X receptor ligand. Eur. J. Biochem. 236, 328-333 (1996).
    • (1996) Eur. J. Biochem , vol.236 , pp. 328-333
    • LeMotte, P.K.1    Keidek, S.2    Apfel, C.M.3
  • 35
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis-retinoic acid
    • Egea, P. F. et al. Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis-retinoic acid. EMBO J. 19, 2592-2601 (2000).
    • (2000) EMBO J , vol.19 , pp. 2592-2601
    • Egea, P.F.1
  • 36
    • 0036251738 scopus 로고    scopus 로고
    • Molecular recognition of agonist ligands by RXRs
    • Egea, P. F., Mitschler, A. & Maras, D. Molecular recognition of agonist ligands by RXRs. Mol. Endocrinol. 16, 987-997 (2002).
    • (2002) Mol. Endocrinol , vol.16 , pp. 987-997
    • Egea, P.F.1    Mitschler, A.2    Maras, D.3
  • 37
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ
    • Nolte, R. T. et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature 395 137-143 (1998).
    • (1998) Nature , vol.395 , pp. 137-143
    • Nolte, R.T.1
  • 38
    • 0032553542 scopus 로고    scopus 로고
    • Crystal structure of the ligand binding domain of the human nuclear receptor PPARγ
    • Uppenberg, J. et al. Crystal structure of the ligand binding domain of the human nuclear receptor PPARγ. J. Biol. Chem. 273 31108-31112 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 31108-31112
    • Uppenberg, J.1
  • 39
    • 0033105510 scopus 로고    scopus 로고
    • Molecular recognition of fatty acids by peroxisome proliferator- activated receptors
    • Xu, H. E. et al. Molecular recognition of fatty acids by peroxisome proliferator- activated receptors. Mol. Cell 3, 397-403 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 397-403
    • Xu, H.E.1
  • 40
    • 0036187372 scopus 로고    scopus 로고
    • Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3
    • Greschik, H. et al. Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell 9, 303-313 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 303-313
    • Greschik, H.1
  • 41
    • 10344247702 scopus 로고    scopus 로고
    • Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor α (ERRα): Crystal structure of ERRα ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1 α
    • Kallen, J. et al. Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor α (ERRα): Crystal structure of ERRα ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1 α. J. Biol. Chem. 279, 49330-49337 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 49330-49337
    • Kallen, J.1
  • 42
    • 33846021285 scopus 로고    scopus 로고
    • X-ray crystal structures of the estrogen-related receptor-γ ligand binding domain in three functional states reveal the molecular basis of small molecule regulation
    • Wang, L. et al. X-ray crystal structures of the estrogen-related receptor-γ ligand binding domain in three functional states reveal the molecular basis of small molecule regulation. J. Biol. Chem. 281, 37773-37781 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 37773-37781
    • Wang, L.1
  • 43
    • 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, D. D. Dynamic stabilization of nuclear receptor ligand binding domains by hormone or corepressor binding. Mol. Cell 6, 245-253 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 245-253
    • Pissios, P.1    Tzameli, I.2    Kushner, P.3    Moore, D.D.4
  • 44
    • 0348110368 scopus 로고    scopus 로고
    • Molecular sensors of estrogen receptor conformations and dynamics
    • Tamrazi, A., Carlson, K. E. & Katzenellenbogen, J. A. Molecular sensors of estrogen receptor conformations and dynamics. Mol. Endocrinol. 17, 2593-2602 (2003).
    • (2003) Mol. Endocrinol , vol.17 , pp. 2593-2602
    • Tamrazi, A.1    Carlson, K.E.2    Katzenellenbogen, J.A.3
  • 45
    • 0037317303 scopus 로고    scopus 로고
    • A dynamic mechanism of nuclear receptor activation and its perturbation in a human disease
    • Kallenberger, B. C., Love, J. D., Chatterjee, V. K. & Schwabe, J. W. A dynamic mechanism of nuclear receptor activation and its perturbation in a human disease. Nature Struct. Biol. 10, 136-140 (2003).
    • (2003) Nature Struct. Biol , vol.10 , pp. 136-140
    • Kallenberger, B.C.1    Love, J.D.2    Chatterjee, V.K.3    Schwabe, J.W.4
  • 46
    • 0034724560 scopus 로고    scopus 로고
    • Ligand-induced stabilization of PPARγ monitored by NMR spectroscopy: Implications for nuclear receptor activation
    • Johnson, B. A. et al. Ligand-induced stabilization of PPARγ monitored by NMR spectroscopy: Implications for nuclear receptor activation. J. Mol. Biol. 298, 187-194 (2000).
    • (2000) J. Mol. Biol , vol.298 , pp. 187-194
    • Johnson, B.A.1
  • 47
    • 0028087742 scopus 로고
    • Synthesis and structure-activity relationships of novel retinold X receptor-selective retinoids
    • Boehm, M. F. et al. Synthesis and structure-activity relationships of novel retinold X receptor-selective retinoids. J. Med. Chem. 37, 2930-2941 (1994).
    • (1994) J. Med. Chem , vol.37 , pp. 2930-2941
    • Boehm, M.F.1
  • 49
    • 0033179675 scopus 로고    scopus 로고
    • Structural basis for engineering of retinoic acid receptor isotype-selective agonists and antagonists
    • Gèhin, M. et al. Structural basis for engineering of retinoic acid receptor isotype-selective agonists and antagonists. Chem. Biol. 6, 519-529 (1999).
    • (1999) Chem. Biol , vol.6 , pp. 519-529
    • Gèhin, M.1
  • 50
    • 0037020734 scopus 로고    scopus 로고
    • Synthesis and biological activity of retinoic acid receptor-α specific amides
    • Beard, R. L. et al. Synthesis and biological activity of retinoic acid receptor-α specific amides, Bioorg. Med. Chem. Lett. 12 3145-3148 (2002).
    • (2002) Bioorg. Med. Chem. Lett , vol.12 , pp. 3145-3148
    • Beard, R.L.1
  • 51
    • 0030875103 scopus 로고    scopus 로고
    • Identification of highly potent retinoic acid receptor α-selective antagonists
    • Teng, M. et al. Identification of highly potent retinoic acid receptor α-selective antagonists. J. Med. Chem. 40, 2445-2451 (1997).
    • (1997) J. Med. Chem , vol.40 , pp. 2445-2451
    • Teng, M.1
  • 52
    • 0032488839 scopus 로고    scopus 로고
    • Serine 232 and methionine 272 define the ligand binding pocket in retinoic acid receptor subtypes
    • Ostrowski, J. et al. Serine 232 and methionine 272 define the ligand binding pocket in retinoic acid receptor subtypes. J. Biol. Chem. 273, 3490-3495 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 3490-3495
    • Ostrowski, J.1
  • 53
    • 0004439249 scopus 로고    scopus 로고
    • Structural modifications of 6-naphthalene-2-carboxylate retinoids
    • Yu. K-L. et al. Structural modifications of 6-naphthalene-2-carboxylate retinoids Bioarg. Med. Chem. Lett. 6, 2865-2870 (1996).
    • (1996) Bioarg. Med. Chem. Lett , vol.6 , pp. 2865-2870
    • Yu, K.-L.1
  • 54
    • 0034622982 scopus 로고    scopus 로고
    • Structural basis for isotype selectivity of the human retinoic acid nuclear receptor
    • Klaholz, B. P., Mitschler A. & Moras, D. Structural basis for isotype selectivity of the human retinoic acid nuclear receptor. J. Mol. Biol. 302, 155-170 (2000).
    • (2000) J. Mol. Biol , vol.302 , pp. 155-170
    • Klaholz, B.P.1    Mitschler, A.2    Moras, D.3
  • 55
    • 0034612290 scopus 로고    scopus 로고
    • Enantiomer discrimination illustrated by high-resolution crystal structures of the human nuclear receptor hRARγ
    • Klaholz, B. P., Mitschler, A., Belema, M., Zusi, C. & Maras, D. Enantiomer discrimination illustrated by high-resolution crystal structures of the human nuclear receptor hRARγ. Proc. Natl. Acad. Sci. USA 97, 6322-6327 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6322-6327
    • Klaholz, B.P.1    Mitschler, A.2    Belema, M.3    Zusi, C.4    Maras, D.5
  • 56
    • 0029562846 scopus 로고
    • Synthesis, structure-affinity relationships. and biological activities of ligands binding to retinoic acid receptor subtypes
    • Charpentier, B. et al. Synthesis, structure-affinity relationships. and biological activities of ligands binding to retinoic acid receptor subtypes. J. Med. Chem. 38, 4993-5006 (1995).
    • (1995) J. Med. Chem , vol.38 , pp. 4993-5006
    • Charpentier, B.1
  • 57
    • 0030960146 scopus 로고    scopus 로고
    • Induction of apoptosis by retinoids and retinoic acid receptor γ-selective compounds in mouse thymocytes through a novel apoptosis pathway
    • Szondy, Z. et al. Induction of apoptosis by retinoids and retinoic acid receptor γ-selective compounds in mouse thymocytes through a novel apoptosis pathway. Mol. Pharmacol. 51, 972-982 (1997).
    • (1997) Mol. Pharmacol , vol.51 , pp. 972-982
    • Szondy, Z.1
  • 58
    • 0029895639 scopus 로고    scopus 로고
    • Discovery of novel retinoic acid receptor agonists having potent antiproliferative activity in cervical cancer cells
    • Zhang, L. et al. Discovery of novel retinoic acid receptor agonists having potent antiproliferative activity in cervical cancer cells. J. Med. Chem. 39, 2659-2663 (1996).
    • (1996) J. Med. Chem , vol.39 , pp. 2659-2663
    • Zhang, L.1
  • 59
    • 0034686419 scopus 로고    scopus 로고
    • Dawson, M. I. et al. 4-[3-(5,6,7,8-Tetrahydro-5,5,8,8-tetramethyl- 2-naphthalenylphenyl]benzoic acid and heterocyclic-bridged analogues are novel retinoic acid receptor subtype and retinoid X receptor α agonists. Bioorg. Med. Chem. Lett. 10, 1311-1313 (2000).
    • Dawson, M. I. et al. 4-[3-(5,6,7,8-Tetrahydro-5,5,8,8-tetramethyl- 2-naphthalenylphenyl]benzoic acid and heterocyclic-bridged analogues are novel retinoic acid receptor subtype and retinoid X receptor α agonists. Bioorg. Med. Chem. Lett. 10, 1311-1313 (2000).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.