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Volumn 407, Issue 1, 2011, Pages 13-20

Structure basis of bigelovin as a selective RXR agonist with a distinct binding mode

Author keywords

agonist; bigelovin; cancer; crystal structure; RXR

Indexed keywords

BIGELOVIN; FARNESOID X RECEPTOR; LIVER X RECEPTOR ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; RECEPTOR BLOCKING AGENT; RETINOID X RECEPTOR ALPHA; STEROID RECEPTOR COACTIVATOR 1; STEROL REGULATORY ELEMENT BINDING PROTEIN 1C; TRIACYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 79952006933     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.01.032     Document Type: Article
Times cited : (42)

References (43)
  • 2
    • 34848862778 scopus 로고    scopus 로고
    • Design of selective nuclear receptor modulators: RAR and RXR as a case study
    • DOI 10.1038/nrd2398, PII NRD2398
    • De Lera A.R., Bourguet W., Altucci L., and Gronemeyer H. Design of selective nuclear receptor modulators: RAR and RXR as a case study Nat. Rev. Drug Discov. 6 2007 811 820 (Pubitemid 47504872)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.10 , pp. 811-820
    • De Lera, A.R.1    Bourguet, W.2    Altucci, L.3    Gronemeyer, H.4
  • 7
    • 0025612655 scopus 로고
    • Retinoid-sensitive cells and cell lines
    • Amos B., and Lotan R. Retinoid-sensitive cells and cell lines Methods Enzymol. 190 1990 217 225
    • (1990) Methods Enzymol. , vol.190 , pp. 217-225
    • Amos, B.1    Lotan, R.2
  • 8
    • 54149115973 scopus 로고    scopus 로고
    • Combination chemoprevention of HER2/neu-induced breast cancer using a cyclooxygenase-2 inhibitor and a retinoid X receptor-selective retinoid
    • Brown P.H., Subbaramaiah K., Salmon A.P., Baker R., Newman R.A., and Yang P. Combination chemoprevention of HER2/neu-induced breast cancer using a cyclooxygenase-2 inhibitor and a retinoid X receptor-selective retinoid Cancer Prev. Res. (Phila. Pa) 1 2008 208 214
    • (2008) Cancer Prev. Res. (Phila. Pa) , vol.1 , pp. 208-214
    • Brown, P.H.1    Subbaramaiah, K.2    Salmon, A.P.3    Baker, R.4    Newman, R.A.5    Yang, P.6
  • 14
    • 0033711971 scopus 로고    scopus 로고
    • Structural studies on nuclear receptors
    • Renaud J.P., and Moras D. Structural studies on nuclear receptors Cell. Mol. Life Sci. 57 2000 1748 1769
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1748-1769
    • Renaud, J.P.1    Moras, D.2
  • 15
    • 23444431623 scopus 로고    scopus 로고
    • Retinoid X receptor heterodimers in the metabolic syndrome
    • DOI 10.1056/NEJMra043590
    • Shulman A.I., and Mangelsdorf D.J. Retinoid x receptor heterodimers in the metabolic syndrome N. Engl. J. Med. 353 2005 604 615 (Pubitemid 41138942)
    • (2005) New England Journal of Medicine , vol.353 , Issue.6 , pp. 604-615
    • Shulman, A.I.1    Mangelsdorf, D.J.2
  • 17
    • 8844262660 scopus 로고    scopus 로고
    • Principles for modulation of the nuclear receptor superfamily
    • DOI 10.1038/nrd1551
    • Gronemeyer H., Gustafsson J.A., and Laudet V. Principles for modulation of the nuclear receptor superfamily Nat. Rev. Drug Discov. 3 2004 950 964 (Pubitemid 39534319)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.11 , pp. 950-964
    • Gronemeyer, H.1    Gustafsson, J.-A.2    Laudet, V.3
  • 18
    • 0038701656 scopus 로고    scopus 로고
    • Retinoid X receptor (RXR) agonist-induced antagonism of farnesoid X receptor (FXR) activity due to absence of coactivator recruitment and decreased DNA binding
    • DOI 10.1074/jbc.M208312200
    • Kassam A., Miao B., Young P.R., and Mukherjee R. Retinoid X receptor (RXR) agonist-induced antagonism of farnesoid X receptor (FXR) activity due to absence of coactivator recruitment and decreased DNA binding J. Biol. Chem. 278 2003 10028 10032 (Pubitemid 36800256)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10028-10032
    • Kassam, A.1    Miao, B.2    Young, P.R.3    Mukherjee, R.4
  • 19
  • 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, Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K., and Milburn M.V. Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors Mol. Cell 5 2000 545 555
    • (2000) Mol. Cell , vol.5 , pp. 545-555
    • Gampe Jr., R.T.1    Montana, V.G.2    Lambert, M.H.3    Miller, A.B.4    Bledsoe, R.K.5    Milburn, M.V.6
  • 21
    • 0032947848 scopus 로고    scopus 로고
    • Retinoid X receptor (RXR) agonist-induced activation of dominant- negative RXR-retinoic acid receptor α403 heterodimers is developmentally regulated during myeloid differentiation
    • Johnson B.S., Chandraratna R.A., Heyman R.A., Allegretto E.A., Mueller L., and Collins S.J. Retinoid X receptor (RXR) agonist-induced activation of dominant-negative RXR-retinoic acid receptor α403 heterodimers is developmentally regulated during myeloid differentiation Mol. Cell. Biol. 19 1999 3372 3382 (Pubitemid 29193797)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.5 , pp. 3372-3382
    • Johnson, B.S.1    Chandraratna, R.A.S.2    Heyman, R.A.3    Allegretto, E.A.4    Mueller, L.5    Collins, S.J.6
  • 22
    • 0036251738 scopus 로고    scopus 로고
    • Molecular recognition of agonist ligands by RXRs
    • DOI 10.1210/me.16.5.987
    • Egea P.F., Mitschler A., and Moras D. Molecular recognition of agonist ligands by RXRs Mol. Endocrinol. 16 2002 987 997 (Pubitemid 34478536)
    • (2002) Molecular Endocrinology , vol.16 , Issue.5 , pp. 987-997
    • Egea, P.F.1    Mitschler, A.2    Moras, D.3
  • 24
    • 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., Mitschler A., Rochel N., Ruff M., Chambon P., and Moras D. Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis retinoic acid EMBO J. 19 2000 2592 2601 (Pubitemid 30323548)
    • (2000) EMBO Journal , vol.19 , Issue.11 , pp. 2592-2601
    • Egea, P.F.1    Mitschler, A.2    Rochel, N.3    Ruff, M.4    Chambon, P.5    Moras, D.6
  • 27
    • 33645237713 scopus 로고    scopus 로고
    • Anti-diabetic and hypolipidemic effects of aqueous-extract from the flower of Inula japonica in alloxan-induced diabetic mice
    • Shan J.J., Yang M., and Ren J.W. Anti-diabetic and hypolipidemic effects of aqueous-extract from the flower of Inula japonica in alloxan-induced diabetic mice Biol. Pharm. Bull. 29 2006 455 459
    • (2006) Biol. Pharm. Bull. , vol.29 , pp. 455-459
    • Shan, J.J.1    Yang, M.2    Ren, J.W.3
  • 28
    • 0030004037 scopus 로고    scopus 로고
    • Cytotoxicity and NMR spectral assignments of ergolide and bigelovin
    • DOI 10.1055/s-2006-957843
    • Wang Q., Zhou B.N., Zhang R.W., Lin Y.Y., Lin L.Z., Gil R.R., and Cordell G.A. Cytotoxicity and NMR spectral assignments of ergolide and bigelovin Planta Med. 62 1996 166 168 (Pubitemid 26163224)
    • (1996) Planta Medica , vol.62 , Issue.2 , pp. 166-168
    • Wang, Q.1    Zhou, B.-N.2    Zhang, R.-W.3    Lin, Y.-Y.4    Lin, L.-Z.5    Gil, R.R.6    Cordell, G.A.7
  • 29
    • 41949086428 scopus 로고    scopus 로고
    • Structural basis for catalytic and inhibitory mechanisms of β-hydroxyacyl-acyl carrier protein dehydratase (FabZ)
    • Zhang L., Liu W., Hu T., Du L., Luo C., and Chen K. Structural basis for catalytic and inhibitory mechanisms of β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) J. Biol. Chem. 283 2008 5370 5379
    • (2008) J. Biol. Chem. , vol.283 , pp. 5370-5379
    • Zhang, L.1    Liu, W.2    Hu, T.3    Du, L.4    Luo, C.5    Chen, K.6
  • 30
    • 67149144841 scopus 로고    scopus 로고
    • Apoptosis inducement of bigelovin from Inula helianthus-aquatica on human Leukemia U937 cells
    • Zeng G.Z., Tan N.H., Ji C.J., Fan J.T., Huang H.Q., Han H.J., and Zhou G.B. Apoptosis inducement of bigelovin from Inula helianthus-aquatica on human Leukemia U937 cells Phytother. Res. 23 2009 885 891
    • (2009) Phytother. Res. , vol.23 , pp. 885-891
    • Zeng, G.Z.1    Tan, N.H.2    Ji, C.J.3    Fan, J.T.4    Huang, H.Q.5    Han, H.J.6    Zhou, G.B.7
  • 31
    • 33644696706 scopus 로고    scopus 로고
    • Distinct mechanisms of glucose lowering by specific agonists for peroxisomal proliferator activated receptor γ and retinoic acid X receptors
    • DOI 10.1074/jbc.M505853200
    • Li X., Hansen P.A., Xi L., Chandraratna R.A., and Burant C.F. Distinct mechanisms of glucose lowering by specific agonists for peroxisomal proliferator activated receptor γ and retinoic acid X receptors J. Biol. Chem. 280 2005 38317 38327 (Pubitemid 43860306)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38317-38327
    • Li, X.1    Hansen, P.A.2    Xi, L.3    Chandraratna, R.A.S.4    Burant, C.F.5
  • 32
    • 69249090970 scopus 로고    scopus 로고
    • Direct interdomain interactions can mediate allosterism in the thyroid receptor
    • Putcha B.D., and Fernandez E.J. Direct interdomain interactions can mediate allosterism in the thyroid receptor J. Biol. Chem. 284 2009 22517 22524
    • (2009) J. Biol. Chem. , vol.284 , pp. 22517-22524
    • Putcha, B.D.1    Fernandez, E.J.2
  • 33
    • 77955654529 scopus 로고    scopus 로고
    • Modification at the acidic domain of RXR agonists has little effect on permissive RXR-heterodimer activation
    • Fujii S., Ohsawa F., Yamada S., Shinozaki R., Fukai R., and Makishima M. Modification at the acidic domain of RXR agonists has little effect on permissive RXR-heterodimer activation Bioorg. Med. Chem. Lett. 20 2010 5139 5142
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 5139-5142
    • Fujii, S.1    Ohsawa, F.2    Yamada, S.3    Shinozaki, R.4    Fukai, R.5    Makishima, M.6
  • 34
    • 1542573353 scopus 로고    scopus 로고
    • Structure-activity relationship of nuclear receptor-ligand interactions
    • Greschik H., and Moras D. Structure-activity relationship of nuclear receptor-ligand interactions Curr. Top. Med. Chem. 3 2003 1573 1599
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 1573-1599
    • Greschik, H.1    Moras, D.2
  • 35
    • 70349139683 scopus 로고    scopus 로고
    • Rosiglitazone sensitizes hepatocellular carcinoma cell lines to 5-fluorouracil antitumor activity through activation of the PPARγ signaling pathway
    • Cao L.Q., Wang X.L., Wang Q., Xue P., Jiao X.Y., and Peng H.P. Rosiglitazone sensitizes hepatocellular carcinoma cell lines to 5-fluorouracil antitumor activity through activation of the PPARγ signaling pathway Acta Pharmacol. Sin. 30 2009 1316 1322
    • (2009) Acta Pharmacol. Sin. , vol.30 , pp. 1316-1322
    • Cao, L.Q.1    Wang, X.L.2    Wang, Q.3    Xue, P.4    Jiao, X.Y.5    Peng, H.P.6
  • 36
    • 13844306722 scopus 로고    scopus 로고
    • Activation of PPARγ by curcumin inhibits Moser cell growth and mediates suppression of gene expression of cyclin D1 and EGFR
    • Chen A., and Xu J. Activation of PPARγ by curcumin inhibits Moser cell growth and mediates suppression of gene expression of cyclin D1 and EGFR Am. J. Physiol.: Gasterointest. Liver Physiol. 288 2005 G447 G456
    • (2005) Am. J. Physiol.: Gasterointest. Liver Physiol. , vol.288
    • Chen, A.1    Xu, J.2
  • 37
    • 50649097541 scopus 로고    scopus 로고
    • Fat and beyond: The diverse biology of PPARγ
    • Tontonoz P., and Spiegelman B.M. Fat and beyond: the diverse biology of PPARγ Annu. Rev. Biochem. 77 2008 289 312
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 289-312
    • Tontonoz, P.1    Spiegelman, B.M.2
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Minor Z.O. a. W Processing of X-ray diffraction data collected in oscillation mode C.W. Carter Jr R.M. Sweet, Methods in Enzymology: Macromolecular Crystallography: Part A 276 1997 Academic Press New York, NY 307 326
    • (1997) Methods in Enzymology: Macromolecular Crystallography: Part A , vol.276 , pp. 307-326
    • Minor, Z.O.A.W.1
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763


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