메뉴 건너뛰기




Volumn 70, Issue , 2014, Pages 75-102

RXRs: Collegial partners

Author keywords

[No Author keywords available]

Indexed keywords

ALITRETINOIN; ISOPROTEIN; LIGAND; RETINOIC ACID; RETINOIC ACID RECEPTOR; RETINOID X RECEPTOR;

EID: 84910126184     PISSN: 03060225     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-94-017-9050-5_5     Document Type: Article
Times cited : (35)

References (150)
  • 4
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda A, Pascual A (2001) Nuclear hormone receptors and gene expression. Physiol Rev 81:1269-1304
    • (2001) Physiol Rev , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 5
    • 0027161015 scopus 로고
    • PPAR-RXR heterodimer activates a peroxisome proliferator response element upstream of the bifunctional enzyme gene
    • Bardot O, Aldridge TC, Latruffe N, Green S (1993) PPAR-RXR heterodimer activates a peroxisome proliferator response element upstream of the bifunctional enzyme gene. Biochem Biophys Res Commun 192:37-45
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 37-45
    • Bardot, O.1    Aldridge, T.C.2    Latruffe, N.3    Green, S.4
  • 6
    • 0026714849 scopus 로고
    • Heterodimerization among thyroid hormone receptor, retinoid X receptor, Chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein
    • Berrodin TJ, Marks MS, Ozato K, Linney E, Lazar MA (1992) Heterodimerization among thyroid hormone receptor, retinoid X receptor, Chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein. Mol Endocrinol 6:1468-1478
    • (1992) Mol Endocrinol , vol.6 , pp. 1468-1478
    • Berrodin, T.J.1    Marks, M.S.2    Ozato, K.3    Linney, E.4    Lazar, M.A.5
  • 10
    • 33747154772 scopus 로고    scopus 로고
    • Anatomical profiling of nuclear receptor expression reveals a hierarchical transcriptional network
    • Bookout AL, Jeong Y, Downes M, Yu R, Evans RM, Mangelsdorf DJ (2006) Anatomical profiling of nuclear receptor expression reveals a hierarchical transcriptional network. Cell 126:789-799
    • (2006) Cell , vol.126 , pp. 789-799
    • Bookout, A.L.1    Jeong, Y.2    Downes, M.3    Yu, R.4    Evans, R.M.5    Mangelsdorf, D.J.6
  • 11
    • 0034655252 scopus 로고    scopus 로고
    • Ubiquitin/Proteasome pathway regulates levels of retinoic acid receptor OE = and retinoid X receptor OE } in human keratinocytes
    • Boudjelal M, Wang Z, Voorhees JJ, Fisher GJ (2000) Ubiquitin/Proteasome pathway regulates levels of retinoic acid receptor OE = and retinoid X receptor OE } in human keratinocytes. Cancer Res 60:2247-2252
    • (2000) Cancer Res , vol.60 , pp. 2247-2252
    • Boudjelal, M.1    Wang, Z.2    Voorhees, J.J.3    Fisher, G.J.4
  • 12
    • 0029012163 scopus 로고
    • Crystal structure of the ligand binding domain of the human nuclear receptor RXR-alpha
    • Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D (1995) Crystal structure of the ligand binding domain of the human nuclear receptor RXR-alpha. 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
  • 13
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • Bourguet W, Vivat V, Wurtz J-M, Chambon P, Gronemeyer H, Moras D (2000) Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell 5:289-298
    • (2000) Mol Cell , vol.5 , pp. 289-298
    • Bourguet, W.1    Vivat, V.2    Wurtz, J.-M.3    Chambon, P.4    Gronemeyer, H.5    Moras, D.6
  • 15
    • 82655171926 scopus 로고    scopus 로고
    • Structural analysis of nuclear receptors: From isolated domains to integral proteins
    • Brelivet Y, Rochel N, Moras D (2012) Structural analysis of nuclear receptors: from isolated domains to integral proteins. Mol Cell Endocrinol 348:466-473
    • (2012) Mol Cell Endocrinol , vol.348 , pp. 466-473
    • Brelivet, Y.1    Rochel, N.2    Moras, D.3
  • 17
    • 0026551704 scopus 로고
    • RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors
    • Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG (1992) RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors. EMBO J 11:1409-1418
    • (1992) EMBO J , vol.11 , pp. 1409-1418
    • Bugge, T.H.1    Pohl, J.2    Lonnoy, O.3    Stunnenberg, H.G.4
  • 18
    • 0025317798 scopus 로고
    • A nuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements
    • Burnside J, Darling DS, Chin WW (1990) A nuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements. J Biol Chem 265:2500-2504
    • (1990) J Biol Chem , vol.265 , pp. 2500-2504
    • Burnside, J.1    Darling, D.S.2    Chin, W.W.3
  • 19
    • 84856397813 scopus 로고    scopus 로고
    • Targeting orphan nuclear receptors for treatment of metabolic diseases and autoimmunity
    • Burris TP, Busby SA, Griffin PR (2012) Targeting orphan nuclear receptors for treatment of metabolic diseases and autoimmunity. Chem Biol 19:51-59
    • (2012) Chem Biol , vol.19 , pp. 51-59
    • Burris, T.P.1    Busby, S.A.2    Griffin, P.R.3
  • 20
    • 84858796689 scopus 로고    scopus 로고
    • Transcriptional integration of metabolism by the nuclear sterol-activated receptors LXR and FXR
    • Calkin AC, Tontonoz P (2012) Transcriptional integration of metabolism by the nuclear sterol-activated receptors LXR and FXR. Nat Rev Mol Cell Biol 13:213-224
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 213-224
    • Calkin, A.C.1    Tontonoz, P.2
  • 23
    • 79951805682 scopus 로고    scopus 로고
    • Endocrine disruptors: From endocrine to metabolic disruption
    • Casals-Casas C, Desvergne B (2011) Endocrine disruptors: from endocrine to metabolic disruption. Annu Rev Physiol 73:135-162
    • (2011) Annu Rev Physiol , vol.73 , pp. 135-162
    • Casals-Casas, C.1    Desvergne, B.2
  • 24
    • 0347356359 scopus 로고    scopus 로고
    • A permissive retinoid X receptor/thyroid hormone receptor heterodimer allows stimulation of prolactin gene transcription by thyroid hormone and 9-cis-retinoic acid
    • Castillo AI, Sanchez-Martinez R, Moreno JL, Martinez-Iglesias OA, Palacios D, Aranda A (2004) A permissive retinoid X receptor/thyroid hormone receptor heterodimer allows stimulation of prolactin gene transcription by thyroid hormone and 9-cis-retinoic acid. Mol Cell Biol 24:502-513
    • (2004) Mol Cell Biol , vol.24 , pp. 502-513
    • Castillo, A.I.1    Sanchez-Martinez, R.2    Moreno, J.L.3    Martinez-Iglesias, O.A.4    Palacios, D.5    Aranda, A.6
  • 26
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM (1995) A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454-457
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 27
    • 22244476079 scopus 로고    scopus 로고
    • Unraveling protein-protein interactions in living cells with fluorescence fluctuation brightness analysis
    • Chen Y, Wei LN, Muller JD (2005) Unraveling protein-protein interactions in living cells with fluorescence fluctuation brightness analysis. Biophys J 88:4366-4377
    • (2005) Biophys J , vol.88 , pp. 4366-4377
    • Chen, Y.1    Wei, L.N.2    Muller, J.D.3
  • 29
    • 0033574663 scopus 로고    scopus 로고
    • A unified nomenclature system for the nuclear receptor superfamily
    • Committee NRN (1999) A unified nomenclature system for the nuclear receptor superfamily. Cell 97:161-163
    • (1999) Cell , vol.97 , pp. 161-163
    • Committee, N.R.N.1
  • 30
    • 33645863768 scopus 로고    scopus 로고
    • Transcriptional regulation of metabolism
    • Desvergne B, Michalik L, Wahli W (2006) Transcriptional regulation of metabolism. Physiol Rev 86:465-514
    • (2006) Physiol Rev , vol.86 , pp. 465-514
    • Desvergne, B.1    Michalik, L.2    Wahli, W.3
  • 31
    • 33947103526 scopus 로고    scopus 로고
    • RXR: From partnership to leadership in metabolic regulations
    • Gerald L (ed). Academic Press, New York
    • Desvergne B (2007) RXR: from partnership to leadership in metabolic regulations. In: Gerald L (ed) Vitamins &hormones. Academic Press, New York
    • (2007) Vitamins &hormones
    • Desvergne, B.1
  • 32
    • 0034999546 scopus 로고    scopus 로고
    • PHase 2 and 3 clinical trial of oral bexarotene (targretin capsules) for the treatment of refractory or persistent early-stage cutaneous t-cell lymphoma
    • Duvic M, Martin AG, Kim Y et al (2001) PHase 2 and 3 clinical trial of oral bexarotene (targretin capsules) for the treatment of refractory or persistent early-stage cutaneous t-cell lymphoma. Archives of Dermatology 137:581-593
    • (2001) Archives of Dermatology , vol.137 , pp. 581-593
    • Duvic, M.1    Martin, A.G.2    Kim, Y.3
  • 33
    • 0036251738 scopus 로고    scopus 로고
    • Molecular recognition of agonist ligands by RXRs
    • Egea PF, Mitschler A, Moras D (2002) Molecular recognition of agonist ligands by RXRs. Mol Endocrinol 16:987-997
    • (2002) Mol Endocrinol , vol.16 , pp. 987-997
    • Egea, P.F.1    Mitschler, A.2    Moras, D.3
  • 34
    • 0026718829 scopus 로고
    • Characterization of the myelin basic protein thyroid hormone response element and its function in the context of native and heterologous promoter
    • Farsetti A, Desvergne B, Hallenbeck PL, Robbins J, Nikodem VM (1992) Characterization of the myelin basic protein thyroid hormone response element and its function in the context of native and heterologous promoter. J Biol Chem 1992(267):15784-15788
    • (1992) J Biol Chem , vol.1992 , Issue.267 , pp. 15784-15788
    • Farsetti, A.1    Desvergne, B.2    Hallenbeck, P.L.3    Robbins, J.4    Nikodem, V.M.5
  • 35
    • 32644460092 scopus 로고    scopus 로고
    • From molecular action to physiological outputs: Peroxisome proliferator-activated receptors are nuclear receptors at the croassroads of key cellular functions
    • Feige JN, Gelman L, Michalik L, Desvergne B, Wahli W (2006) From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the croassroads of key cellular functions. Prog Lipid Res 45:120-159
    • (2006) Prog Lipid Res , vol.45 , pp. 120-159
    • Feige, J.N.1    Gelman, L.2    Michalik, L.3    Desvergne, B.4    Wahli, W.5
  • 36
    • 23644439144 scopus 로고    scopus 로고
    • Fluorescence imaging reveals the nuclear behavior of peroxisome proliferator-activated receptor/retinoid X receptor heterodimers in the absence and presence of ligand
    • Feige JRMN, Gelman L, Tudor C, Engelborghs Y, Wahli W, Desvergne B (2005) Fluorescence imaging reveals the nuclear behavior of peroxisome proliferator-activated receptor/retinoid X receptor heterodimers in the absence and presence of ligand. J Biol Chem 280:17880-17890
    • (2005) J Biol Chem , vol.280 , pp. 17880-17890
    • Feige, J.R.M.N.1    Gelman, L.2    Tudor, C.3    Engelborghs, Y.4    Wahli, W.5    Desvergne, B.6
  • 38
    • 0033855471 scopus 로고    scopus 로고
    • Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix
    • Gampe RT Jr, Montana VG, Lambert MH, Wisely GB, Milburn MV, Xu HE (2000) Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix. Genes Dev 14:2229-2241
    • (2000) Genes Dev , vol.14 , pp. 2229-2241
    • Gampe, R.T.1    Montana, V.G.2    Lambert, M.H.3    Wisely, G.B.4    Milburn, M.V.5    Xu, H.E.6
  • 41
    • 0037050017 scopus 로고    scopus 로고
    • Co-regulator recruitment and the mechanism of retinoic acid receptor synergy
    • Germain P, Jaya I, Zechel C, Gronemeyer H (2002) Co-regulator recruitment and the mechanism of retinoic acid receptor synergy. Nature 415:187-192
    • (2002) Nature , vol.415 , pp. 187-192
    • Germain, P.1    Jaya, I.2    Zechel, C.3    Gronemeyer, H.4
  • 42
    • 0037099584 scopus 로고    scopus 로고
    • Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RAR[gamma] degradation and transactivation
    • Gianni M, Bauer A, Garattini E, Chambon P, Rochette-Egly C (2002) Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RAR[gamma] degradation and transactivation. EMBO J 21:3760-3769
    • (2002) EMBO J , vol.21 , pp. 3760-3769
    • Gianni, M.1    Bauer, A.2    Garattini, E.3    Chambon, P.4    Rochette-Egly, C.5
  • 43
    • 0141706670 scopus 로고    scopus 로고
    • The AF-1 and AF-2 domains of RAR?2 and RXRa cooperate for triggering the transactivation and the degradation of RAR?2/RXRa heterodimers
    • Gianni M, Tarrade A, Nigro EA, Garattini E, Rochette-Egly C (2003) The AF-1 and AF-2 domains of RAR?2 and RXRa cooperate for triggering the transactivation and the degradation of RAR?2/RXRa heterodimers. J Biol Chem 278:34458-34466
    • (2003) J Biol Chem , vol.278 , pp. 34458-34466
    • Gianni, M.1    Tarrade, A.2    Nigro, E.A.3    Garattini, E.4    Rochette-Egly, C.5
  • 44
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers and heterodimers
    • Glass CK (1994) Differential recognition of target genes by nuclear receptor monomers, dimers and heterodimers. Endocr Rev 15:391-407
    • (1994) Endocr Rev , vol.15 , pp. 391-407
    • Glass, C.K.1
  • 45
    • 0025251135 scopus 로고
    • Multiple cell-type specific proteins differentially regulate target sequence recognition by the alpha retinoic acid receptor
    • Glass CK, Devary OV, Rosenfeld MG (1990) Multiple cell-type specific proteins differentially regulate target sequence recognition by the alpha retinoic acid receptor. Cell 63:729-738
    • (1990) Cell , vol.63 , pp. 729-738
    • Glass, C.K.1    Devary, O.V.2    Rosenfeld, M.G.3
  • 48
    • 0029044946 scopus 로고
    • Activation of mammalian retinoid X receptors by the insect growth regulator methoprene
    • Harmon MA, Boehm MF, Heyman RA, Mangelsdorf DJ (1995) Activation of mammalian retinoid X receptors by the insect growth regulator methoprene. Proc Natl Acad Sci 92:6157-6160
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 6157-6160
    • Harmon, M.A.1    Boehm, M.F.2    Heyman, R.A.3    Mangelsdorf, D.J.4
  • 49
    • 3843117675 scopus 로고    scopus 로고
    • Retinoid X receptor gamma-deficient mice have increased skeletal muscle lipoprotein lipase activity and less weight gain when fed a high-fat diet
    • Haugen BR, Jensen DR, Sharma V, Pulawa LK, Hays WR, Krezel W, Chambon P, Eckel RH (2004) Retinoid X receptor gamma-deficient mice have increased skeletal muscle lipoprotein lipase activity and less weight gain when fed a high-fat diet. Endocrinology 145:3679-3685
    • (2004) Endocrinology , vol.145 , pp. 3679-3685
    • Haugen, B.R.1    Jensen, D.R.2    Sharma, V.3    Pulawa, L.K.4    Hays, W.R.5    Krezel, W.6    Chambon, P.7    Eckel, R.H.8
  • 50
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional coactivators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker M (1997) A signature motif in transcriptional coactivators mediates binding to nuclear receptors. Nature 387:733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.4
  • 53
    • 0030818756 scopus 로고    scopus 로고
    • Polarity and specific sequence requirements of peroxisome proliferator-activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA
    • Ijpenberg A, Jeannin E, Wahli W, Desvergne B (1997) Polarity and specific sequence requirements of peroxisome proliferator-activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA. J Biol Chem 272:20108-20117
    • (1997) J Biol Chem , vol.272 , pp. 20108-20117
    • Ijpenberg, A.1    Jeannin, E.2    Wahli, W.3    Desvergne, B.4
  • 55
    • 0035793045 scopus 로고    scopus 로고
    • Impaired adipogenesis and lipolysis in the mouse upon selective ablation of the retinoid X receptor a mediated by a tamoxifen-inducible chimeric Cre recombinase (Cre-ERT2) in adipocytes
    • Imai T, Jiang M, Chambon P, Metzger D (2001) Impaired adipogenesis and lipolysis in the mouse upon selective ablation of the retinoid X receptor a mediated by a tamoxifen-inducible chimeric Cre recombinase (Cre-ERT2) in adipocytes. PNAS 98:224-228
    • (2001) PNAS , vol.98 , pp. 224-228
    • Imai, T.1    Jiang, M.2    Chambon, P.3    Metzger, D.4
  • 56
    • 0035836755 scopus 로고    scopus 로고
    • Selective ablation of retinoid X receptor alpha in hepatocytes impairs their lifespan and regenerative capacity
    • Imai T, Jiang M, Kastner P, Chambon P, Metzger D (2001) Selective ablation of retinoid X receptor alpha in hepatocytes impairs their lifespan and regenerative capacity. Proc Natl Acad Sci 98:4581-4586
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 4581-4586
    • Imai, T.1    Jiang, M.2    Kastner, P.3    Chambon, P.4    Metzger, D.5
  • 58
    • 27744577633 scopus 로고    scopus 로고
    • Lignans, bacteriocides and organochlorine compound activate the human pregnane X receptor (PXR)
    • Jacobs MN, Nolan GT, Hood SR (2005) Lignans, bacteriocides and organochlorine compound activate the human pregnane X receptor (PXR). Toxicol Appl Pharmacol 209:123-133
    • (2005) Toxicol Appl Pharmacol , vol.209 , pp. 123-133
    • Jacobs, M.N.1    Nolan, G.T.2    Hood, S.R.3
  • 60
    • 14944349712 scopus 로고    scopus 로고
    • Organotin compounds promote adipocyte differentiation as agonists of the peroxisome proliferator-activated receptor OE =/retinoid X receptor pathway
    • Kanayama T, Kobayashi N, Mamiya S, Nakanishi T, Nishikawa J-I (2005) Organotin compounds promote adipocyte differentiation as agonists of the peroxisome proliferator-activated receptor OE =/retinoid X receptor pathway. Mol Pharmacol 67:766-774
    • (2005) Mol Pharmacol , vol.67 , pp. 766-774
    • Kanayama, T.1    Kobayashi, N.2    Mamiya, S.3    Nakanishi, T.4    Nishikawa, J.-I.5
  • 61
    • 0038701656 scopus 로고    scopus 로고
    • Retinoid X receptor (RXR) agonistinduced antagonism of farnesoid X receptor (FXR) activity due to absence of coactivator recruitment and decreased DNA binding
    • Kassam A, Miao B, Young PR, Mukherjee R (2003) Retinoid X receptor (RXR) agonistinduced antagonism of farnesoid X receptor (FXR) activity due to absence of coactivator recruitment and decreased DNA binding. J Biol Chem 278:10028-10032
    • (2003) J Biol Chem , vol.278 , pp. 10028-10032
    • Kassam, A.1    Miao, B.2    Young, P.R.3    Mukherjee, R.4
  • 62
    • 0028168007 scopus 로고
    • Genetic analysis of RXR alpha developmental function: Convergence of RXR and RAR signaling pathways in heart and eye morphogenesis
    • Kastner P, Grondona JM, Mark M, Gansmuller A, Lemeur M, Decimo D, Vonesch J-L, Dolle P, Chambon P (1994) Genetic analysis of RXR alpha developmental function: convergence of RXR and RAR signaling pathways in heart and eye morphogenesis. Cell 78:987-1003
    • (1994) Cell , vol.78 , pp. 987-1003
    • Kastner, P.1    Grondona, J.M.2    Mark, M.3    Gansmuller, A.4    Lemeur, M.5    Decimo, D.6    Vonesch, J.-L.7    Dolle, P.8    Chambon, P.9
  • 64
    • 0027447461 scopus 로고
    • Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptor-retinoid X receptor heterodimers
    • Keller H, Dreyer C, Medin J, Mahfoudi A, Ozato K, Wahli W (1993) Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptor-retinoid X receptor heterodimers. Proc Natl Acad Sci USA 90:2160-2164
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2160-2164
    • Keller, H.1    Dreyer, C.2    Medin, J.3    Mahfoudi, A.4    Ozato, K.5    Wahli, W.6
  • 68
    • 0033617520 scopus 로고    scopus 로고
    • Orphan nuclear receptors: Shifting endocrinology into reverse
    • Kliewer SA, Lehmann JM, Willson TM (1999) Orphan nuclear receptors: shifting endocrinology into reverse. Science 284:757-760
    • (1999) Science , vol.284 , pp. 757-760
    • Kliewer, S.A.1    Lehmann, J.M.2    Willson, T.M.3
  • 70
    • 0026592518 scopus 로고
    • Retinoid X receptors interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling
    • Kliewer SA, Umesono K, Mangelsdorf DJ, Evans RM (1992) Retinoid X receptors interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling. Nature 355:446-449
    • (1992) Nature , vol.355 , pp. 446-449
    • Kliewer, S.A.1    Umesono, K.2    Mangelsdorf, D.J.3    Evans, R.M.4
  • 71
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
    • Kliewer SA, Umesono K, Nonan DJ, Heyman RA, Evans RM (1992) Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors. Nature 358:771-774
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Nonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 72
    • 0034721926 scopus 로고    scopus 로고
    • Dimerization with retinoid X receptors and phosphorylation modulate the retinoic acid-induced degradation of retinoic acid receptors alpha and gamma through the ubiquitin-proteasome pathway
    • Kopf E, Plassat J-L, Vivat V, De The H, Chambon P, Rochette-Egly C (2000) Dimerization with retinoid X receptors and phosphorylation modulate the retinoic acid-induced degradation of retinoic acid receptors alpha and gamma through the ubiquitin-proteasome pathway. J Biol Chem 275:33280-33288
    • (2000) J Biol Chem , vol.275 , pp. 33280-33288
    • Kopf, E.1    Plassat, J.-L.2    Vivat, V.3    De The, H.4    Chambon, P.5    Rochette-Egly, C.6
  • 75
    • 0034616147 scopus 로고    scopus 로고
    • Identification of the DNA binding specificity and potential target genes for the farnesoid X-activated receptor
    • Laffitte BA, Kast HR, Nguyen CM, Zavacki AM, Moore DD, Edwards PA (2000) Identification of the DNA binding specificity and potential target genes for the farnesoid X-activated receptor. J Biol Chem 275:10638-10647
    • (2000) J Biol Chem , vol.275 , pp. 10638-10647
    • Laffitte, B.A.1    Kast, H.R.2    Nguyen, C.M.3    Zavacki, A.M.4    Moore, D.D.5    Edwards, P.A.6
  • 77
    • 75449096571 scopus 로고    scopus 로고
    • Cross-talk between PPARs and the partners of RXR: A molecular perspective
    • Lap Shu AC, Richard AW (2009) Cross-talk between PPARs and the partners of RXR: a molecular perspective. PPAR Res
    • (2009) PPAR Res
    • Lap Shu, A.C.1    Richard, A.W.2
  • 80
    • 78049278719 scopus 로고    scopus 로고
    • Retinoid X receptors: Common heterodimerization partners with distinct functions
    • Lefebvre P, Benomar Y, Staels B (2010) Retinoid X receptors: common heterodimerization partners with distinct functions. Trends Endocrinol Metab: TEM 21:676-683
    • (2010) Trends Endocrinol Metab: TEM , vol.21 , pp. 676-683
    • Lefebvre, P.1    Benomar, Y.2    Staels, B.3
  • 83
    • 0029664544 scopus 로고    scopus 로고
    • Phytanic acid is a retinoid X receptor ligand
    • Lemotte PK, Keidel S, Apfel CM (1996) Phytanic acid is a retinoid X receptor ligand. Eur J Biochem 236:328-333
    • (1996) Eur J Biochem , vol.236 , pp. 328-333
    • Lemotte, P.K.1    Keidel, S.2    Apfel, C.M.3
  • 84
    • 0035933797 scopus 로고    scopus 로고
    • Role of retinoid receptor coactivator pockets in cofactor recruitment and transcriptional regulation
    • Leo C, Yang X, Liu J, Li H, Chen JD (2001) Role of retinoid receptor coactivator pockets in cofactor recruitment and transcriptional regulation. J Biol Chem 276:23127-23134
    • (2001) J Biol Chem , vol.276 , pp. 23127-23134
    • Leo, C.1    Yang, X.2    Liu, J.3    Li, H.4    Chen, J.D.5
  • 86
    • 0025650361 scopus 로고
    • Vitamin D receptor interaction with specific DNA requires a nuclear protein and 1,25-dihydroxyvitamin D3
    • Liao J, Ozono K, Sone T, Mcdonnell DP, Pike JW (1990) Vitamin D receptor interaction with specific DNA requires a nuclear protein and 1,25-dihydroxyvitamin D3. Proc Natl Acad Sci USA 87:9751-9788
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9751-9788
    • Liao, J.1    Ozono, K.2    Sone, T.3    Mcdonnell, D.P.4    Pike, J.W.5
  • 88
    • 34247526984 scopus 로고    scopus 로고
    • Triterpenoids and rexinoids as multifunctional agents for the prevention and treatment of cancer
    • Liby KT, Yore MM, Sporn MB (2007) Triterpenoids and rexinoids as multifunctional agents for the prevention and treatment of cancer. Nat Rev Cancer 7:357-369
    • (2007) Nat Rev Cancer , vol.7 , pp. 357-369
    • Liby, K.T.1    Yore, M.M.2    Sporn, M.B.3
  • 89
    • 0027223007 scopus 로고
    • The mouse retinoid-X receptor-gamma gene: Genomic organization and evidence for functional isoforms
    • Liu Q, Linney E (1993) The mouse retinoid-X receptor-gamma gene: genomic organization and evidence for functional isoforms. Mol Endocrinol 7:651-658
    • (1993) Mol Endocrinol , vol.7 , pp. 651-658
    • Liu, Q.1    Linney, E.2
  • 90
    • 0027389116 scopus 로고
    • Multiple parameters control the selectivity of nuclear receptors for their response elements
    • Mader S, Leroy P, Chen J-Y, Chambon P (1993) Multiple parameters control the selectivity of nuclear receptors for their response elements. J Biol Chem 268:591-600
    • (1993) J Biol Chem , vol.268 , pp. 591-600
    • Mader, S.1    Leroy, P.2    Chen, J.-Y.3    Chambon, P.4
  • 92
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf DJ, Evans RM (1995) The RXR heterodimers and orphan receptors. Cell 83:841-850
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 93
    • 0025270737 scopus 로고
    • Nuclear receptor that identifies a novel retinoic acid response pathway
    • Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (1990) Nuclear receptor that identifies a novel retinoic acid response pathway. Nature 345:224-229
    • (1990) Nature , vol.345 , pp. 224-229
    • Mangelsdorf, D.J.1    Ong, E.S.2    Dyck, J.A.3    Evans, R.M.4
  • 94
    • 0025938132 scopus 로고
    • A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR
    • Mangelsdorf DJ, Umesono K, Kilewer SA, Borgmeyer U, Ong ES, Evans RM (1991) A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR. Cell 66:555-561
    • (1991) Cell , vol.66 , pp. 555-561
    • Mangelsdorf, D.J.1    Umesono, K.2    Kilewer, S.A.3    Borgmeyer, U.4    Ong, E.S.5    Evans, R.M.6
  • 95
    • 0026608464 scopus 로고
    • H-2RIIBP (RXR beta) heterodimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive genes
    • Marks MS, Hallenbeck PL, Nagata T, Segars JH, Appella E, Nikodem VM, Ozato K (1992) H-2RIIBP (RXR beta) heterodimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive genes. EMBO J 11:1419-1435
    • (1992) EMBO J , vol.11 , pp. 1419-1435
    • Marks, M.S.1    Hallenbeck, P.L.2    Nagata, T.3    Segars, J.H.4    Appella, E.5    Nikodem, V.M.6    Ozato, K.7
  • 97
    • 0035886844 scopus 로고    scopus 로고
    • Phosphorylation of retinoid X receptor alpha at Serine 260 impairs its metabolism and function in human hepatocellular carcinoma
    • Matsushima-Nishiwaki R, Okuno M, Adachi S, Sano T, Akita K, Moriwaki H, Friedman SL, Kojima S (2001) Phosphorylation of retinoid X receptor alpha at Serine 260 impairs its metabolism and function in human hepatocellular carcinoma. Cancer Res 61:7675-7682
    • (2001) Cancer Res , vol.61 , pp. 7675-7682
    • Matsushima-Nishiwaki, R.1    Okuno, M.2    Adachi, S.3    Sano, T.4    Akita, K.5    Moriwaki, H.6    Friedman, S.L.7    Kojima, S.8
  • 98
    • 0030071518 scopus 로고    scopus 로고
    • Activation of retinoid receptors RAR alpha and RXR alpha induces differentiation and apoptosis, respectively, in HL-60 cells
    • Mehta K, Mcqueen T, Neamati N, Collins S, Andreeff M (1996) Activation of retinoid receptors RAR alpha and RXR alpha induces differentiation and apoptosis, respectively, in HL-60 cells. Cell Growth Differ 7:179-186
    • (1996) Cell Growth Differ , vol.7 , pp. 179-186
    • Mehta, K.1    Mcqueen, T.2    Neamati, N.3    Collins, S.4    Andreeff, M.5
  • 99
    • 77954761161 scopus 로고    scopus 로고
    • Genome-wide analysis of the VDR/RXR cistrome in osteoblast cells provides new mechanistic insight into the actions of the vitamin D hormone
    • Meyer MB, Goetsch PD, Pike JW (2010) Genome-wide analysis of the VDR/RXR cistrome in osteoblast cells provides new mechanistic insight into the actions of the vitamin D hormone. J Steroid Biochem Mol Biol 121:136-141
    • (2010) J Steroid Biochem Mol Biol , vol.121 , pp. 136-141
    • Meyer, M.B.1    Goetsch, P.D.2    Pike, J.W.3
  • 101
  • 103
    • 0024458145 scopus 로고
    • Identification of nuclear factors that enhance binding of the htyroid hormone receptor to a thyroid hormone response element
    • Murray MB, Towle HC (1989) Identification of nuclear factors that enhance binding of the htyroid hormone receptor to a thyroid hormone response element. Mol Endocrinol 3:1434-1442
    • (1989) Mol Endocrinol , vol.3 , pp. 1434-1442
    • Murray, M.B.1    Towle, H.C.2
  • 104
    • 0025860708 scopus 로고
    • The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors
    • Naar AM, Boutin J, Lipkin SM, Yu VC, Holloway JM, Glass CK, Rosenfeld MG (1991) The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors. Cell 65:1267-1279
    • (1991) Cell , vol.65 , pp. 1267-1279
    • Naar, A.M.1    Boutin, J.2    Lipkin, S.M.3    Yu, V.C.4    Holloway, J.M.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 106
    • 55749101777 scopus 로고    scopus 로고
    • Genome-wide profiling of PPARgamma: RXR and RNA polymerase II occupancy reveals temporal activation of distinct metabolic pathways and changes in RXR dimer composition during adipogenesis
    • Nielsen R, Pedersen T, Hagenbeek D, Moulos P, Siersbaek R, Megens E, Denissov S, Borgesen M, Francoijs K-J, Mandrup S, Stunnenberg HG (2008) Genome-wide profiling of PPARgamma: RXR and RNA polymerase II occupancy reveals temporal activation of distinct metabolic pathways and changes in RXR dimer composition during adipogenesis. Genes Dev 22:2953-2967
    • (2008) Genes Dev , vol.22 , pp. 2953-2967
    • Nielsen, R.1    Pedersen, T.2    Hagenbeek, D.3    Moulos, P.4    Siersbaek, R.5    Megens, E.6    Denissov, S.7    Borgesen, M.8    Francoijs, K.-J.9    Mandrup, S.10    Stunnenberg, H.G.11
  • 109
    • 84857183093 scopus 로고    scopus 로고
    • Structure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNA
    • Orlov I, Rochel N, Moras D, Klaholz BP (2012) Structure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNA. EMBO J 31:291-300
    • (2012) EMBO J , vol.31 , pp. 291-300
    • Orlov, I.1    Rochel, N.2    Moras, D.3    Klaholz, B.P.4
  • 111
    • 0028946634 scopus 로고
    • A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1
    • Perlmann T, Jansson L (1995) A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1. Genes Dev 9:769-782
    • (1995) Genes Dev , vol.9 , pp. 769-782
    • Perlmann, T.1    Jansson, L.2
  • 112
    • 0029736983 scopus 로고    scopus 로고
    • Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors
    • Perlmann T, Umesono K, Rangarajan PN, Forman BM, Evans RM (1996) Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors. Mol Endocrinol 10:958-966
    • (1996) Mol Endocrinol , vol.10 , pp. 958-966
    • Perlmann, T.1    Umesono, K.2    Rangarajan, P.N.3    Forman, B.M.4    Evans, R.M.5
  • 113
    • 19944430311 scopus 로고    scopus 로고
    • Characterization of the Interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies
    • Pogenberg V, Guichou J-FO, Vivat-Hannah V, Kammerer S, Perez E, Germain P, De Lera AR, Gronemeyer H, Royer CA, Bourguet W (2005) Characterization of the Interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. J Biol Chem 280:1625-1633
    • (2005) J Biol Chem , vol.280 , pp. 1625-1633
    • Pogenberg, V.1    Guichou, J.-F.O.2    Vivat-Hannah, V.3    Kammerer, S.4    Perez, E.5    Germain, P.6    De Lera, A.R.7    Gronemeyer, H.8    Royer, C.A.9    Bourguet, W.10
  • 114
    • 69249090970 scopus 로고    scopus 로고
    • Direct interdomain interactions can mediate allosterism in the thyroid receptor
    • Putcha B-DK, Fernandez EJ (2009) Direct interdomain interactions can mediate allosterism in the thyroid receptor. J Biol Chem 284:22517-22524
    • (2009) J Biol Chem , vol.284 , pp. 22517-22524
    • Putcha, B.-D.K.1    Fernandez, E.J.2
  • 118
    • 0033026860 scopus 로고    scopus 로고
    • Impaired extrapyramidal function caused by the targeted disruption of retinoid X receptor RXR?1 isoform
    • Saga Y, Kobayashi M, Ohta H, Murai N, Nakai N, Oshima M, Taketo MM (1999) Impaired extrapyramidal function caused by the targeted disruption of retinoid X receptor RXR?1 isoform. Genes Cells 4:219-228
    • (1999) Genes Cells , vol.4 , pp. 219-228
    • Saga, Y.1    Kobayashi, M.2    Ohta, H.3    Murai, N.4    Nakai, N.5    Oshima, M.6    Taketo, M.M.7
  • 119
    • 0030994388 scopus 로고    scopus 로고
    • The promoter context is a decisive factor in establishing selective responsiveness to class II nuclear receptors
    • Sanguedolce MV, Leblanc BP, Betz JL, Stunnenberg HG (1997) The promoter context is a decisive factor in establishing selective responsiveness to class II nuclear receptors. EMBO J 15:2861-2873
    • (1997) EMBO J , vol.15 , pp. 2861-2873
    • Sanguedolce, M.V.1    Leblanc, B.P.2    Betz, J.L.3    Stunnenberg, H.G.4
  • 120
    • 79952103416 scopus 로고    scopus 로고
    • Negative regulation by nuclear receptors: A plethora of mechanisms
    • Santos GM, Fairall L, Schwabe JWR (2011) Negative regulation by nuclear receptors: a plethora of mechanisms. Trends Endocrinol Metab 22:87-93
    • (2011) Trends Endocrinol Metab , vol.22 , pp. 87-93
    • Santos, G.M.1    Fairall, L.2    Schwabe, J.W.R.3
  • 121
    • 79954617449 scopus 로고    scopus 로고
    • Liver X receptor-retinoid X receptor (LXR-RXR) heterodimer cistrome reveals coordination of LXR and AP1 signaling in keratinocytes
    • Shen Q, Bai Y, Chang KCN, Wang Y, Burris TP, Freedman LP, Thompson CC, Nagpal S (2011) Liver X receptor-retinoid X receptor (LXR-RXR) heterodimer cistrome reveals coordination of LXR and AP1 signaling in keratinocytes. J Biol Chem 286:14554-14563
    • (2011) J Biol Chem , vol.286 , pp. 14554-14563
    • Shen, Q.1    Bai, Y.2    Chang, K.C.N.3    Wang, Y.4    Burris, T.P.5    Freedman, L.P.6    Thompson, C.C.7    Nagpal, S.8
  • 122
    • 2442454641 scopus 로고    scopus 로고
    • Effects of rexinoids on glucose transport and insulin-mediated signaling in skeletal muscles of diabetic (db/db) mice
    • Shen Q, Cline GW, Shulman GI, Leibowitz MD, Davies PJA (2004) Effects of rexinoids on glucose transport and insulin-mediated signaling in skeletal muscles of diabetic (db/db) mice. J Biol Chem 279:19721-19731
    • (2004) J Biol Chem , vol.279 , pp. 19721-19731
    • Shen, Q.1    Cline, G.W.2    Shulman, G.I.3    Leibowitz, M.D.4    Davies, P.J.A.5
  • 123
    • 1642304065 scopus 로고    scopus 로고
    • Structural determinants of allosteric ligand activation in RXR heterodimers
    • Shulman AI, Larson C, Mangelsdorf DJ, Ranganathan R (2004) Structural determinants of allosteric ligand activation in RXR heterodimers. Cell 116:417-429
    • (2004) Cell , vol.116 , pp. 417-429
    • Shulman, A.I.1    Larson, C.2    Mangelsdorf, D.J.3    Ranganathan, R.4
  • 124
    • 65649131624 scopus 로고    scopus 로고
    • Molecular determinants of the interactions between LXR/RXR heterodimers and TRAP2 20
    • Son YL, Lee YC (2009) Molecular determinants of the interactions between LXR/RXR heterodimers and TRAP2 20. Biochem Biophys Res Commun 384:389-393
    • (2009) Biochem Biophys Res Commun , vol.384 , pp. 389-393
    • Son, Y.L.1    Lee, Y.C.2
  • 125
    • 0028175195 scopus 로고
    • RXR alpha mutant mice establish a genetic basis for vitamin A signaling in heart morphogenesis
    • Sucov HM, Dyson E, Gumeringer CL, Price J, Chien KR, Evans RM (1994) RXR alpha mutant mice establish a genetic basis for vitamin A signaling in heart morphogenesis. Genes Dev 8:1007-1018
    • (1994) Genes Dev , vol.8 , pp. 1007-1018
    • Sucov, H.M.1    Dyson, E.2    Gumeringer, C.L.3    Price, J.4    Chien, K.R.5    Evans, R.M.6
  • 126
    • 10944250224 scopus 로고    scopus 로고
    • The nuclear xenobiotic receptor CAR: Structural determinants of constitutive activation and heterodimerization
    • Suino K, Peng L, Reynolds R, Li Y, Cha J-Y, Repa JJ, Kliewer SA, Xu HE (2004) The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization. Mol Cell 16:893-905
    • (2004) Mol Cell , vol.16 , pp. 893-905
    • Suino, K.1    Peng, L.2    Reynolds, R.3    Li, Y.4    Cha, J.-Y.5    Repa, J.J.6    Kliewer, S.A.7    Xu, H.E.8
  • 128
    • 78049342781 scopus 로고    scopus 로고
    • Research resource: Transcriptome profiling of genes regulated by RXR and its permissive and nonpermissive partners in differentiating monocytederived dendritic cells
    • Szeles L, Poliska S, Nagy G, Szatmari I, Szanto A, Pap A, Lindstedt M, Santegoets SJAM, Ruhl R, Dezso B, Nagy L (2010) Research resource: transcriptome profiling of genes regulated by RXR and its permissive and nonpermissive partners in differentiating monocytederived dendritic cells. Mol Endocrinol 24:2218-2231
    • (2010) Mol Endocrinol , vol.24 , pp. 2218-2231
    • Szeles, L.1    Poliska, S.2    Nagy, G.3    Szatmari, I.4    Szanto, A.5    Pap, A.6    Lindstedt, M.7    Santegoets, S.J.A.M.8    Ruhl, R.9    Dezso, B.10    Nagy, L.11
  • 130
    • 18844480014 scopus 로고    scopus 로고
    • Involvement of all-transretinoic acid in the breakdown of retinoic acid receptors alpha and gamma through proteasomes in mcf-7 human breast cancer cells
    • Tanaka T, Rodriguez De La Conception ML, De Luca LM (2001) Involvement of all-transretinoic acid in the breakdown of retinoic acid receptors alpha and gamma through proteasomes in mcf-7 human breast cancer cells. Biochem Pharmacol 61:1347-1355
    • (2001) Biochem Pharmacol , vol.61 , pp. 1347-1355
    • Tanaka, T.1    Rodriguez De La Conception, M.L.2    De Luca, L.M.3
  • 131
    • 33947541887 scopus 로고    scopus 로고
    • Association with coregulators is the major determinant governing peroxisome proliferator-activated receptor mobility in living cells
    • Tudor C, Feige JRMN, Pingali H, Lohray VB, Wahli W, Desvergne BA, Engelborghs Y, Gelman L (2007) Association with coregulators is the major determinant governing peroxisome proliferator-activated receptor mobility in living cells. J Biol Chem 282:4417-4426
    • (2007) J Biol Chem , vol.282 , pp. 4417-4426
    • Tudor, C.1    Feige, J.R.M.N.2    Pingali, H.3    Lohray, V.B.4    Wahli, W.5    Desvergne, B.A.6    Engelborghs, Y.7    Gelman, L.8
  • 133
    • 0026766654 scopus 로고
    • Binding characteristics of the thyroid hormone receptor homo- and heterodimers to consensus AGGTCA repeat motifs
    • Wahlstrom GM, Sjoberg M, Andersson M, Nordstrom K, Vennstrom B (1992) Binding characteristics of the thyroid hormone receptor homo- and heterodimers to consensus AGGTCA repeat motifs. Mol Endocrinol 6
    • (1992) Mol Endocrinol , pp. 6
    • Wahlstrom, G.M.1    Sjoberg, M.2    Andersson, M.3    Nordstrom, K.4    Vennstrom, B.5
  • 138
    • 0029035278 scopus 로고
    • LXR, a nuclear receptor that defines a distinct retinoid response pathway
    • Willy P, Umesono K, Ong E, Evans R, Heyman R, Mangelsdorf D (1995) LXR, a nuclear receptor that defines a distinct retinoid response pathway. Genes Dev 9:1033-1045
    • (1995) Genes Dev , vol.9 , pp. 1033-1045
    • Willy, P.1    Umesono, K.2    Ong, E.3    Evans, R.4    Heyman, R.5    Mangelsdorf, D.6
  • 140
  • 147
    • 0026536522 scopus 로고
    • Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors
    • Zhang XK, Hoffman BE, Tran PBV, Graupner G, Pfahl M (1992) Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors. Nature 355:441-446
    • (1992) Nature , vol.355 , pp. 441-446
    • Zhang, X.K.1    Hoffman, B.E.2    Tran, P.B.V.3    Graupner, G.4    Pfahl, M.5
  • 150
    • 33845996557 scopus 로고    scopus 로고
    • Asymmetric cleavage of beta carotene yields a transcriptional repressor of retinoid X receptor and peroxisome proliferator-activated receptor responses
    • Ziouzenkova O, Orasanu G, Sukhova G, Lau E, Berger JP, Tang G, Krinsky NI, Dolnikowski GG, Plutzky J (2007) Asymmetric cleavage of beta carotene yields a transcriptional repressor of retinoid X receptor and peroxisome proliferator-activated receptor responses. Mol Endocrinol 21:77-88
    • (2007) Mol Endocrinol , vol.21 , pp. 77-88
    • Ziouzenkova, O.1    Orasanu, G.2    Sukhova, G.3    Lau, E.4    Berger, J.P.5    Tang, G.6    Krinsky, N.I.7    Dolnikowski, G.G.8    Plutzky, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.