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Volumn 45, Issue 2, 2006, Pages 120-159

From molecular action to physiological outputs: Peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions

Author keywords

Apoptosis; Coactivators; Corepressors; Differentiation; Lipid metabolism; Proliferation; Transcriptional regulation

Indexed keywords

CELL NUCLEUS RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; FATTY ACID; LIGAND; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR DELTA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; REGULATOR PROTEIN; SIGNAL PEPTIDE; SUMO PROTEIN; TRANSCRIPTION FACTOR;

EID: 32644460092     PISSN: 01637827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plipres.2005.12.002     Document Type: Review
Times cited : (665)

References (338)
  • 1
    • 0033574663 scopus 로고    scopus 로고
    • A unified nomenclature system for the nuclear receptor superfamily
    • Nuclear Receptor Nomenclature Committee A unified nomenclature system for the nuclear receptor superfamily Cell 97 1999 161 163
    • (1999) Cell , vol.97 , pp. 161-163
    • Receptor Nomenclature Committee, N.1
  • 2
    • 0025132245 scopus 로고
    • Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
    • I. Issemann, and S. Green Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators Nature 347 1990 645 650
    • (1990) Nature , vol.347 , pp. 645-650
    • Issemann, I.1    Green, S.2
  • 3
    • 0026517010 scopus 로고
    • Control of the peroxisomal beta-oxidation pathway by a novel family of nuclear hormone receptors
    • C. Dreyer, G. Krey, H. Keller, F. Givel, G. Helftenbein, and W. Wahli Control of the peroxisomal beta-oxidation pathway by a novel family of nuclear hormone receptors Cell 68 1992 879 887
    • (1992) Cell , vol.68 , pp. 879-887
    • Dreyer, C.1    Krey, G.2    Keller, H.3    Givel, F.4    Helftenbein, G.5    Wahli, W.6
  • 4
    • 0034678088 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors: Insight into multiple cellular functions
    • P. Escher, and W. Wahli Peroxisome proliferator-activated receptors: insight into multiple cellular functions Mutat Res 448 2000 121 138
    • (2000) Mutat Res , vol.448 , pp. 121-138
    • Escher, P.1    Wahli, W.2
  • 5
    • 0030985318 scopus 로고    scopus 로고
    • Fatty acids, eicosanoids, and hypolipidemic agents identified as ligands of peroxisome proliferator-activated receptors by coactivator-dependent receptor ligand assay
    • G. Krey, O. Braissant, F. L'Horset, E. Kalkhoven, M. Perroud, and M.G. Parker Fatty acids, eicosanoids, and hypolipidemic agents identified as ligands of peroxisome proliferator-activated receptors by coactivator-dependent receptor ligand assay Mol Endocrinol 11 1997 779 791
    • (1997) Mol Endocrinol , vol.11 , pp. 779-791
    • Krey, G.1    Braissant, O.2    L'Horset, F.3    Kalkhoven, E.4    Perroud, M.5    Parker, M.G.6
  • 6
    • 0036183630 scopus 로고    scopus 로고
    • The mechanisms of action of PPARs
    • J. Berger, and D.E. Moller The mechanisms of action of PPARs Annu Rev Med 53 2002 409 435
    • (2002) Annu Rev Med , vol.53 , pp. 409-435
    • Berger, J.1    Moller, D.E.2
  • 7
    • 21444456038 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha interacts with high affinity and is conformationally responsive to endogenous ligands
    • H.A. Hostetler, A.D. Petrescu, A.B. Kier, and F. Schroeder Peroxisome proliferator-activated receptor alpha interacts with high affinity and is conformationally responsive to endogenous ligands J Biol Chem 280 2005 18667 18682
    • (2005) J Biol Chem , vol.280 , pp. 18667-18682
    • Hostetler, H.A.1    Petrescu, A.D.2    Kier, A.B.3    Schroeder, F.4
  • 8
  • 9
    • 17144381253 scopus 로고    scopus 로고
    • Alpha,beta-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor gamma
    • T. Shiraki, N. Kamiya, S. Shiki, T.S. Kodama, A. Kakizuka, and H. Jingami Alpha,beta-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor gamma J Biol Chem 280 2005 14145 14153
    • (2005) J Biol Chem , vol.280 , pp. 14145-14153
    • Shiraki, T.1    Kamiya, N.2    Shiki, S.3    Kodama, T.S.4    Kakizuka, A.5    Jingami, H.6
  • 10
    • 0035956863 scopus 로고    scopus 로고
    • Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors alpha - And gamma-mediated gene expression via liver fatty acid binding protein: A signaling path to the nucleus
    • C. Wolfrum, C.M. Borrmann, T. Borchers, and F. Spener Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors alpha - and gamma-mediated gene expression via liver fatty acid binding protein: a signaling path to the nucleus Proc Natl Acad Sci USA 98 2001 2323 2328
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2323-2328
    • Wolfrum, C.1    Borrmann, C.M.2    Borchers, T.3    Spener, F.4
  • 11
    • 0036291635 scopus 로고    scopus 로고
    • Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription
    • N.S. Tan, N.S. Shaw, N. Vinckenbosch, P. Liu, R. Yasmin, and B. Desvergne Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription Mol Cell Biol 22 2002 5114 5127
    • (2002) Mol Cell Biol , vol.22 , pp. 5114-5127
    • Tan, N.S.1    Shaw, N.S.2    Vinckenbosch, N.3    Liu, P.4    Yasmin, R.5    Desvergne, B.6
  • 12
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma
    • R.T. Nolte, G.B. Wisely, S. Westin, J.E. Cobb, M.H. Lambert, and R. Kurokawa Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma Nature 395 1998 137 143
    • (1998) Nature , vol.395 , pp. 137-143
    • Nolte, R.T.1    Wisely, G.B.2    Westin, S.3    Cobb, J.E.4    Lambert, M.H.5    Kurokawa, R.6
  • 13
    • 0031833450 scopus 로고    scopus 로고
    • The nuclear receptor ligand-binding domain: Structure and function
    • D. Moras, and H. Gronemeyer The nuclear receptor ligand-binding domain: structure and function Curr Opin Cell Biol 10 1998 384 391
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 384-391
    • Moras, D.1    Gronemeyer, H.2
  • 14
    • 18044365802 scopus 로고    scopus 로고
    • Conformational adaptation of nuclear receptor ligand binding domains to agonists: Potential for novel approaches to ligand design
    • M. Togashi, S. Borngraeber, B. Sandler, R.J. Fletterick, P. Webb, and J.D. Baxter Conformational adaptation of nuclear receptor ligand binding domains to agonists: potential for novel approaches to ligand design J Steroid Biochem Mol Biol 93 2005 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
  • 15
    • 0033105510 scopus 로고    scopus 로고
    • Molecular recognition of fatty acids by peroxisome proliferator-activated receptors
    • H.E. Xu, M.H. Lambert, V.G. Montana, D.J. Parks, S.G. Blanchard, and P.J. Brown Molecular recognition of fatty acids by peroxisome proliferator-activated receptors Mol Cell 3 1999 397 403
    • (1999) Mol Cell , vol.3 , pp. 397-403
    • Xu, H.E.1    Lambert, M.H.2    Montana, V.G.3    Parks, D.J.4    Blanchard, S.G.5    Brown, P.J.6
  • 16
    • 22544456280 scopus 로고    scopus 로고
    • Structural determinants of the agonist-independent association of human peroxisome proliferator-activated receptors with coactivators
    • F. Molnar, M. Matilainen, and C. Carlberg Structural determinants of the agonist-independent association of human peroxisome proliferator-activated receptors with coactivators J Biol Chem 280 2005 26543 26556
    • (2005) J Biol Chem , vol.280 , pp. 26543-26556
    • Molnar, F.1    Matilainen, M.2    Carlberg, C.3
  • 17
    • 0037317303 scopus 로고    scopus 로고
    • A dynamic mechanism of nuclear receptor activation and its perturbation in a human disease
    • B.C. Kallenberger, J.D. Love, V.K. Chatterjee, and J.W. Schwabe A dynamic mechanism of nuclear receptor activation and its perturbation in a human disease Nat Struct Biol 10 2003 136 140
    • (2003) Nat Struct Biol , vol.10 , pp. 136-140
    • Kallenberger, B.C.1    Love, J.D.2    Chatterjee, V.K.3    Schwabe, J.W.4
  • 18
    • 0027447461 scopus 로고
    • Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptor-retinoid X receptor heterodimers
    • H. Keller, C. Dreyer, J. Medin, A. Mahfoudi, K. Ozato, and W. Wahli Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptor-retinoid X receptor heterodimers Proc Natl Acad Sci USA 90 1993 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
  • 20
    • 0030771852 scopus 로고    scopus 로고
    • DNA binding properties of peroxisome proliferator-activated receptor subtypes on various natural peroxisome proliferator response elements. Importance of the 5′-flanking region
    • C. Juge-Aubry, A. Pernin, T. Favez, A.G. Burger, W. Wahli, and C.A. Meier DNA binding properties of peroxisome proliferator-activated receptor subtypes on various natural peroxisome proliferator response elements. Importance of the 5′-flanking region J Biol Chem 272 1997 25252 25259
    • (1997) J Biol Chem , vol.272 , pp. 25252-25259
    • Juge-Aubry, C.1    Pernin, A.2    Favez, T.3    Burger, A.G.4    Wahli, W.5    Meier, C.A.6
  • 21
    • 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
    • J.N. Feige, L. Gelman, C. Tudor, Y. Engelborghs, W. Wahli, and B. Desvergne 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 2005 17880 17890
    • (2005) J Biol Chem , vol.280 , pp. 17880-17890
    • Feige, J.N.1    Gelman, L.2    Tudor, C.3    Engelborghs, Y.4    Wahli, W.5    Desvergne, B.6
  • 22
    • 0029066447 scopus 로고
    • Novel sequence determinants in peroxisome proliferator signaling
    • C.N. Palmer, M.H. Hsu, H.J. Griffin, and E.F. Johnson Novel sequence determinants in peroxisome proliferator signaling J Biol Chem 270 1995 16114 16121
    • (1995) J Biol Chem , vol.270 , pp. 16114-16121
    • Palmer, C.N.1    Hsu, M.H.2    Griffin, H.J.3    Johnson, E.F.4
  • 23
    • 0030818756 scopus 로고    scopus 로고
    • Polarity and specific sequence requirements of peroxisome proliferator-activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA. a functional analysis of the malic enzyme gene PPAR response element
    • A. IJpenberg, E. Jeannin, W. Wahli, and B. Desvergne Polarity and specific sequence requirements of peroxisome proliferator-activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA. A functional analysis of the malic enzyme gene PPAR response element J Biol Chem 272 1997 20108 20117
    • (1997) J Biol Chem , vol.272 , pp. 20108-20117
    • Ijpenberg, A.1    Jeannin, E.2    Wahli, W.3    Desvergne, B.4
  • 24
    • 0030952937 scopus 로고    scopus 로고
    • Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors alpha and delta
    • B.M. Forman, J. Chen, and R.M. Evans Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors alpha and delta Proc Natl Acad Sci USA 94 1997 4312 4317
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4312-4317
    • Forman, B.M.1    Chen, J.2    Evans, R.M.3
  • 25
    • 0033615352 scopus 로고    scopus 로고
    • PPARdelta is an APC-regulated target of nonsteroidal anti-inflammatory drugs
    • T.C. He, T.A. Chan, B. Vogelstein, and K.W. Kinzler PPARdelta is an APC-regulated target of nonsteroidal anti-inflammatory drugs Cell 99 1999 335 345
    • (1999) Cell , vol.99 , pp. 335-345
    • He, T.C.1    Chan, T.A.2    Vogelstein, B.3    Kinzler, K.W.4
  • 26
    • 13844262924 scopus 로고    scopus 로고
    • Corepressors selectively control the transcriptional activity of PPARgamma in adipocytes
    • H.P. Guan, T. Ishizuka, P.C. Chui, M. Lehrke, and M.A. Lazar Corepressors selectively control the transcriptional activity of PPARgamma in adipocytes Genes Dev 19 2005 453 461
    • (2005) Genes Dev , vol.19 , pp. 453-461
    • Guan, H.P.1    Ishizuka, T.2    Chui, P.C.3    Lehrke, M.4    Lazar, M.A.5
  • 27
    • 23644455127 scopus 로고    scopus 로고
    • PPARgamma regulates adipocyte cholesterol metabolism via oxidized LDL receptor 1
    • P.C. Chui, H.P. Guan, M. Lehrke, and M.A. Lazar PPARgamma regulates adipocyte cholesterol metabolism via oxidized LDL receptor 1 J Clin Invest 2005
    • (2005) J Clin Invest
    • Chui, P.C.1    Guan, H.P.2    Lehrke, M.3    Lazar, M.A.4
  • 28
    • 20444439929 scopus 로고    scopus 로고
    • Cyclin D1 inhibits peroxisome proliferator-activated receptor gamma-mediated adipogenesis through histone deacetylase recruitment
    • M. Fu, M. Rao, T. Bouras, C. Wang, K. Wu, and X. Zhang Cyclin D1 inhibits peroxisome proliferator-activated receptor gamma-mediated adipogenesis through histone deacetylase recruitment J Biol Chem 280 2005 16934 16941
    • (2005) J Biol Chem , vol.280 , pp. 16934-16941
    • Fu, M.1    Rao, M.2    Bouras, T.3    Wang, C.4    Wu, K.5    Zhang, X.6
  • 29
    • 7644234115 scopus 로고    scopus 로고
    • Evidence for a new human CYP1A1 regulation pathway involving PPAR-alpha and 2 PPRE sites
    • E. Seree, P.H. Villard, J.M. Pascussi, T. Pineau, P. Maurel, and Q.B. Nguyen Evidence for a new human CYP1A1 regulation pathway involving PPAR-alpha and 2 PPRE sites Gastroenterology 127 2004 1436 1445
    • (2004) Gastroenterology , vol.127 , pp. 1436-1445
    • Seree, E.1    Villard, P.H.2    Pascussi, J.M.3    Pineau, T.4    Maurel, P.5    Nguyen, Q.B.6
  • 30
    • 1642458359 scopus 로고    scopus 로고
    • Tissue-selective, bidirectional regulation of PEX11 alpha and perilipin genes through a common peroxisome proliferator response element
    • M. Shimizu, A. Takeshita, T. Tsukamoto, F.J. Gonzalez, and T. Osumi Tissue-selective, bidirectional regulation of PEX11 alpha and perilipin genes through a common peroxisome proliferator response element Mol Cell Biol 24 2004 1313 1323
    • (2004) Mol Cell Biol , vol.24 , pp. 1313-1323
    • Shimizu, M.1    Takeshita, A.2    Tsukamoto, T.3    Gonzalez, F.J.4    Osumi, T.5
  • 32
    • 4544274752 scopus 로고    scopus 로고
    • The direct peroxisome proliferator-activated receptor target fasting-induced adipose factor (FIAF/PGAR/ANGPTL4) is present in blood plasma as a truncated protein that is increased by fenofibrate treatment
    • S. Mandard, F. Zandbergen, N.S. Tan, P. Escher, D. Patsouris, and W. Koenig The direct peroxisome proliferator-activated receptor target fasting-induced adipose factor (FIAF/PGAR/ANGPTL4) is present in blood plasma as a truncated protein that is increased by fenofibrate treatment J Biol Chem 279 2004 34411 34420
    • (2004) J Biol Chem , vol.279 , pp. 34411-34420
    • Mandard, S.1    Zandbergen, F.2    Tan, N.S.3    Escher, P.4    Patsouris, D.5    Koenig, W.6
  • 33
    • 2442696086 scopus 로고    scopus 로고
    • Transcription coactivator PBP, the peroxisome proliferator-activated receptor (PPAR)-binding protein, is required for PPARalpha-regulated gene expression in liver
    • Y. Jia, C. Qi, P. Kashireddi, S. Surapureddi, Y.J. Zhu, and M.S. Rao Transcription coactivator PBP, the peroxisome proliferator-activated receptor (PPAR)-binding protein, is required for PPARalpha-regulated gene expression in liver J Biol Chem 279 2004 24427 24434
    • (2004) J Biol Chem , vol.279 , pp. 24427-24434
    • Jia, Y.1    Qi, C.2    Kashireddi, P.3    Surapureddi, S.4    Zhu, Y.J.5    Rao, M.S.6
  • 34
    • 21744438445 scopus 로고    scopus 로고
    • Dysregulation of the peroxisome proliferator-activated receptor target genes by XPD mutations
    • E. Compe, P. Drane, C. Laurent, K. Diderich, C. Braun, and J.H. Hoeijmakers Dysregulation of the peroxisome proliferator-activated receptor target genes by XPD mutations Mol Cell Biol 25 2005 6065 6076
    • (2005) Mol Cell Biol , vol.25 , pp. 6065-6076
    • Compe, E.1    Drane, P.2    Laurent, C.3    Diderich, K.4    Braun, C.5    Hoeijmakers, J.H.6
  • 35
    • 26444471700 scopus 로고    scopus 로고
    • A sumoylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-gamma
    • G. Pascual, A.L. Fong, S. Ogawa, A. Gamliel, A.C. Li, and V. Perissi A sumoylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-gamma Nature 1 2005
    • (2005) Nature , vol.1
    • Pascual, G.1    Fong, A.L.2    Ogawa, S.3    Gamliel, A.4    Li, A.C.5    Perissi, V.6
  • 36
    • 27644590901 scopus 로고    scopus 로고
    • PPARalpha inhibits vascular smooth muscle cell proliferation underlying intimal hyperplasia by inducing the tumor suppressor p16
    • F. Gizard, C. Amant, O. Barbier, S. Bellosta, R. Robillard, and F. Percevault PPARalpha inhibits vascular smooth muscle cell proliferation underlying intimal hyperplasia by inducing the tumor suppressor p16 J Clin Invest 2005
    • (2005) J Clin Invest
    • Gizard, F.1    Amant, C.2    Barbier, O.3    Bellosta, S.4    Robillard, R.5    Percevault, F.6
  • 37
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
    • S.A. Kliewer, K. Umesono, D.J. Noonan, R.A. Heyman, and R.M. Evans Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors Nature 358 1992 771 774
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 38
    • 0027525576 scopus 로고
    • The peroxisome proliferator-activated receptor:retinoid X receptor heterodimer is activated by fatty acids and fibrate hypolipidaemic drugs
    • I. Issemann, R.A. Prince, J.D. Tugwood, and S. Green The peroxisome proliferator-activated receptor:retinoid X receptor heterodimer is activated by fatty acids and fibrate hypolipidaemic drugs J Mol Endocrinol 11 1993 37 47
    • (1993) J Mol Endocrinol , vol.11 , pp. 37-47
    • Issemann, I.1    Prince, R.A.2    Tugwood, J.D.3    Green, S.4
  • 39
    • 17444442152 scopus 로고    scopus 로고
    • Sensitization of diabetic and obese mice to insulin by retinoid X receptor agonists
    • R. Mukherjee, P.J. Davies, D.L. Crombie, E.D. Bischoff, R.M. Cesario, and L. Jow Sensitization of diabetic and obese mice to insulin by retinoid X receptor agonists Nature 386 1997 407 410
    • (1997) Nature , vol.386 , pp. 407-410
    • Mukherjee, R.1    Davies, P.J.2    Crombie, D.L.3    Bischoff, E.D.4    Cesario, R.M.5    Jow, L.6
  • 40
    • 0031813879 scopus 로고    scopus 로고
    • Transactivation by retinoid X receptor-peroxisome proliferator-activated receptor gamma (PPARgamma) heterodimers: Intermolecular synergy requires only the PPARgamma hormone-dependent activation function
    • I.G. Schulman, G. Shao, and R.A. Heyman Transactivation by retinoid X receptor-peroxisome proliferator-activated receptor gamma (PPARgamma) heterodimers: intermolecular synergy requires only the PPARgamma hormone-dependent activation function Mol Cell Biol 18 1998 3483 3494
    • (1998) Mol Cell Biol , vol.18 , pp. 3483-3494
    • Schulman, I.G.1    Shao, G.2    Heyman, R.A.3
  • 41
    • 0034007387 scopus 로고    scopus 로고
    • A dominant-negative peroxisome proliferator-activated receptor gamma (PPARgamma) mutant is a constitutive repressor and inhibits PPARgamma-mediated adipogenesis
    • M. Gurnell, J.M. Wentworth, M. Agostini, M. Adams, T.N. Collingwood, and C. Provenzano A dominant-negative peroxisome proliferator-activated receptor gamma (PPARgamma) mutant is a constitutive repressor and inhibits PPARgamma-mediated adipogenesis J Biol Chem 275 2000 5754 5759
    • (2000) J Biol Chem , vol.275 , pp. 5754-5759
    • Gurnell, M.1    Wentworth, J.M.2    Agostini, M.3    Adams, M.4    Collingwood, T.N.5    Provenzano, C.6
  • 42
    • 0033537827 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of the peroxisome proliferator-activated receptor alpha by phosphorylation of a ligand-independent trans-activating domain
    • C.E. Juge-Aubry, E. Hammar, C. Siegrist-Kaiser, A. Pernin, A. Takeshita, and W.W. Chin Regulation of the transcriptional activity of the peroxisome proliferator-activated receptor alpha by phosphorylation of a ligand-independent trans-activating domain J Biol Chem 274 1999 10505 10510
    • (1999) J Biol Chem , vol.274 , pp. 10505-10510
    • Juge-Aubry, C.E.1    Hammar, E.2    Siegrist-Kaiser, C.3    Pernin, A.4    Takeshita, A.5    Chin, W.W.6
  • 43
    • 0031057517 scopus 로고    scopus 로고
    • Transcriptional activation by peroxisome proliferator-activated receptor gamma is inhibited by phosphorylation at a consensus mitogen-activated protein kinase site
    • M. Adams, M.J. Reginato, D. Shao, M.A. Lazar, and V.K. Chatterjee Transcriptional activation by peroxisome proliferator-activated receptor gamma is inhibited by phosphorylation at a consensus mitogen-activated protein kinase site J Biol Chem 272 1997 5128 5132
    • (1997) J Biol Chem , vol.272 , pp. 5128-5132
    • Adams, M.1    Reginato, M.J.2    Shao, D.3    Lazar, M.A.4    Chatterjee, V.K.5
  • 44
    • 0030877565 scopus 로고    scopus 로고
    • Ligand-independent activation domain in the N terminus of peroxisome proliferator-activated receptor gamma (PPARgamma). Differential activity of PPARgamma1 and -2 isoforms and influence of insulin
    • A. Werman, A. Hollenberg, G. Solanes, C. Bjorbaek, A.J. Vidal-Puig, and J.S. Flier Ligand-independent activation domain in the N terminus of peroxisome proliferator-activated receptor gamma (PPARgamma). Differential activity of PPARgamma1 and -2 isoforms and influence of insulin J Biol Chem 272 1997 20230 20235
    • (1997) J Biol Chem , vol.272 , pp. 20230-20235
    • Werman, A.1    Hollenberg, A.2    Solanes, G.3    Bjorbaek, C.4    Vidal-Puig, A.J.5    Flier, J.S.6
  • 45
    • 0033521025 scopus 로고    scopus 로고
    • Characterization of the amino-terminal activation domain of peroxisome proliferator-activated receptor alpha. Importance of alpha-helical structure in the transactivating function
    • R. Hi, S. Osada, N. Yumoto, and T. Osumi Characterization of the amino-terminal activation domain of peroxisome proliferator-activated receptor alpha. Importance of alpha-helical structure in the transactivating function J Biol Chem 274 1999 35152 35158
    • (1999) J Biol Chem , vol.274 , pp. 35152-35158
    • Hi, R.1    Osada, S.2    Yumoto, N.3    Osumi, T.4
  • 46
    • 0033583023 scopus 로고    scopus 로고
    • P300 interacts with the N- and C-terminal part of PPARgamma2 in a ligand-independent and -dependent manner, respectively
    • L. Gelman, G. Zhou, L. Fajas, E. Raspe, J.C. Fruchart, and J. Auwerx p300 interacts with the N- and C-terminal part of PPARgamma2 in a ligand-independent and -dependent manner, respectively J Biol Chem 274 1999 7681 7688
    • (1999) J Biol Chem , vol.274 , pp. 7681-7688
    • Gelman, L.1    Zhou, G.2    Fajas, L.3    Raspe, E.4    Fruchart, J.C.5    Auwerx, J.6
  • 48
    • 0034530972 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptors (PPARs) by their ligands and protein kinase a activators
    • G. Lazennec, L. Canaple, D. Saugy, and W. Wahli Activation of peroxisome proliferator-activated receptors (PPARs) by their ligands and protein kinase A activators Mol Endocrinol 14 2000 1962 1975
    • (2000) Mol Endocrinol , vol.14 , pp. 1962-1975
    • Lazennec, G.1    Canaple, L.2    Saugy, D.3    Wahli, W.4
  • 49
    • 0028641559 scopus 로고
    • Stimulation of adipogenesis in fibroblasts by PPAR gamma 2, a lipid-activated transcription factor
    • P. Tontonoz, E. Hu, and B.M. Spiegelman Stimulation of adipogenesis in fibroblasts by PPAR gamma 2, a lipid-activated transcription factor Cell 79 1994 1147 1156
    • (1994) Cell , vol.79 , pp. 1147-1156
    • Tontonoz, P.1    Hu, E.2    Spiegelman, B.M.3
  • 50
    • 0034949053 scopus 로고    scopus 로고
    • Differential contributions of AF-1 and AF-2 activities to the developmental functions of RXR alpha
    • B. Mascrez, M. Mark, W. Krezel, V. Dupe, M. LeMeur, and N.B. Ghyselinck Differential contributions of AF-1 and AF-2 activities to the developmental functions of RXR alpha Development 128 2001 2049 2062
    • (2001) Development , vol.128 , pp. 2049-2062
    • Mascrez, B.1    Mark, M.2    Krezel, W.3    Dupe, V.4    Lemeur, M.5    Ghyselinck, N.B.6
  • 51
    • 19944372389 scopus 로고    scopus 로고
    • A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer
    • R.X. Xu, M.H. Lambert, B.B. Wisely, E.N. Warren, E.E. Weinert, and G.M. Waitt A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer Mol Cell 16 2004 919 928
    • (2004) Mol Cell , vol.16 , pp. 919-928
    • Xu, R.X.1    Lambert, M.H.2    Wisely, B.B.3    Warren, E.N.4    Weinert, E.E.5    Waitt, G.M.6
  • 52
    • 4043173466 scopus 로고    scopus 로고
    • Agonist-dependent and agonist-independent transactivations of the human constitutive androstane receptor are modulated by specific amino acid pairs
    • C. Frank, F. Molnar, M. Matilainen, H. Lempiainen, and C. Carlberg Agonist-dependent and agonist-independent transactivations of the human constitutive androstane receptor are modulated by specific amino acid pairs J Biol Chem 279 2004 33558 33566
    • (2004) J Biol Chem , vol.279 , pp. 33558-33566
    • Frank, C.1    Molnar, F.2    Matilainen, M.3    Lempiainen, H.4    Carlberg, C.5
  • 53
    • 0001297403 scopus 로고    scopus 로고
    • Activation of human T lymphocytes is inhibited by peroxisome proliferator-activated receptor gamma (PPARgamma) agonists. PPARgamma co-association with transcription factor NFAT
    • X.Y. Yang, L.H. Wang, T. Chen, D.R. Hodge, J.H. Resau, and L. DaSilva Activation of human T lymphocytes is inhibited by peroxisome proliferator-activated receptor gamma (PPARgamma) agonists. PPARgamma co-association with transcription factor NFAT J Biol Chem 275 2000 4541 4544
    • (2000) J Biol Chem , vol.275 , pp. 4541-4544
    • Yang, X.Y.1    Wang, L.H.2    Chen, T.3    Hodge, D.R.4    Resau, J.H.5    Dasilva, L.6
  • 54
    • 10744226417 scopus 로고    scopus 로고
    • Transcriptional inactivation of STAT3 by PPARgamma suppresses IL-6-responsive multiple myeloma cells
    • L.H. Wang, X.Y. Yang, X. Zhang, J. Huang, J. Hou, and J. Li Transcriptional inactivation of STAT3 by PPARgamma suppresses IL-6-responsive multiple myeloma cells Immunity 20 2004 205 218
    • (2004) Immunity , vol.20 , pp. 205-218
    • Wang, L.H.1    Yang, X.Y.2    Zhang, X.3    Huang, J.4    Hou, J.5    Li, J.6
  • 55
    • 17844378444 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha physically interacts with CCAAT/enhancer binding protein (C/EBPbeta) to inhibit C/EBPbeta-responsive alpha1-acid glycoprotein gene expression
    • A. Mouthiers, A. Baillet, C. Delomenie, D. Porquet, and N. Mejdoubi-Charef Peroxisome proliferator-activated receptor alpha physically interacts with CCAAT/enhancer binding protein (C/EBPbeta) to inhibit C/EBPbeta-responsive alpha1-acid glycoprotein gene expression Mol Endocrinol 19 2005 1135 1146
    • (2005) Mol Endocrinol , vol.19 , pp. 1135-1146
    • Mouthiers, A.1    Baillet, A.2    Delomenie, C.3    Porquet, D.4    Mejdoubi-Charef, N.5
  • 56
    • 0033527569 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-kappaB and AP-1
    • P. Delerive, K. De Bosscher, S. Besnard, W. Vanden Berghe, J.M. Peters, and F.J. Gonzalez Peroxisome proliferator-activated receptor alpha negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-kappaB and AP-1 J Biol Chem 274 1999 32048 32054
    • (1999) J Biol Chem , vol.274 , pp. 32048-32054
    • Delerive, P.1    De Bosscher, K.2    Besnard, S.3    Vanden Berghe, W.4    Peters, J.M.5    Gonzalez, F.J.6
  • 57
    • 0032565868 scopus 로고    scopus 로고
    • Activation of human aortic smooth-muscle cells is inhibited by PPARalpha but not by PPARgamma activators
    • B. Staels, W. Koenig, A. Habib, R. Merval, M. Lebret, and I.P. Torra Activation of human aortic smooth-muscle cells is inhibited by PPARalpha but not by PPARgamma activators Nature 393 1998 790 793
    • (1998) Nature , vol.393 , pp. 790-793
    • Staels, B.1    Koenig, W.2    Habib, A.3    Merval, R.4    Lebret, M.5    Torra, I.P.6
  • 58
    • 0034693323 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein inhibits interleukin-12 production in lipopolysaccharide-activated mouse macrophages via direct interactions between peroxisome proliferator-activated receptor-gamma and nuclear factor-kappa B
    • S.W. Chung, B.Y. Kang, S.H. Kim, Y.K. Pak, D. Cho, and G. Trinchieri Oxidized low density lipoprotein inhibits interleukin-12 production in lipopolysaccharide-activated mouse macrophages via direct interactions between peroxisome proliferator-activated receptor-gamma and nuclear factor-kappa B J Biol Chem 275 2000 32681 32687
    • (2000) J Biol Chem , vol.275 , pp. 32681-32687
    • Chung, S.W.1    Kang, B.Y.2    Kim, S.H.3    Pak, Y.K.4    Cho, D.5    Trinchieri, G.6
  • 59
    • 0347756655 scopus 로고    scopus 로고
    • Commensal anaerobic gut bacteria attenuate inflammation by regulating nuclear-cytoplasmic shuttling of PPAR-gamma and RelA
    • D. Kelly, J.I. Campbell, T.P. King, G. Grant, E.A. Jansson, and A.G. Coutts Commensal anaerobic gut bacteria attenuate inflammation by regulating nuclear-cytoplasmic shuttling of PPAR-gamma and RelA Nat Immunol 5 2004 104 112
    • (2004) Nat Immunol , vol.5 , pp. 104-112
    • Kelly, D.1    Campbell, J.I.2    King, T.P.3    Grant, G.4    Jansson, E.A.5    Coutts, A.G.6
  • 60
    • 0031886864 scopus 로고    scopus 로고
    • The peroxisome proliferator-activated receptor-gamma is a negative regulator of macrophage activation
    • M. Ricote, A.C. Li, T.M. Willson, C.J. Kelly, and C.K. Glass The peroxisome proliferator-activated receptor-gamma is a negative regulator of macrophage activation Nature 391 1998 79 82
    • (1998) Nature , vol.391 , pp. 79-82
    • Ricote, M.1    Li, A.C.2    Willson, T.M.3    Kelly, C.J.4    Glass, C.K.5
  • 61
    • 0034121698 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma-dependent repression of the inducible nitric oxide synthase gene
    • M. Li, G. Pascual, and C.K. Glass Peroxisome proliferator-activated receptor gamma-dependent repression of the inducible nitric oxide synthase gene Mol Cell Biol 20 2000 4699 4707
    • (2000) Mol Cell Biol , vol.20 , pp. 4699-4707
    • Li, M.1    Pascual, G.2    Glass, C.K.3
  • 62
    • 0035052916 scopus 로고    scopus 로고
    • Inhibition of cellular proliferation through IkappaB kinase-independent and peroxisome proliferator-activated receptor gamma-dependent repression of cyclin D1
    • C. Wang, M. Fu, M. D'Amico, C. Albanese, J.N. Zhou, and M. Brownlee Inhibition of cellular proliferation through IkappaB kinase-independent and peroxisome proliferator-activated receptor gamma-dependent repression of cyclin D1 Mol Cell Biol 21 2001 3057 3070
    • (2001) Mol Cell Biol , vol.21 , pp. 3057-3070
    • Wang, C.1    Fu, M.2    D'Amico, M.3    Albanese, C.4    Zhou, J.N.5    Brownlee, M.6
  • 63
    • 0035823551 scopus 로고    scopus 로고
    • Negative regulation of human fibrinogen gene expression by peroxisome proliferator-activated receptor alpha agonists via inhibition of CCAAT box/enhancer-binding protein beta
    • P. Gervois, N. Vu-Dac, R. Kleemann, M. Kockx, G. Dubois, and B. Laine Negative regulation of human fibrinogen gene expression by peroxisome proliferator-activated receptor alpha agonists via inhibition of CCAAT box/enhancer-binding protein beta J Biol Chem 276 2001 33471 33477
    • (2001) J Biol Chem , vol.276 , pp. 33471-33477
    • Gervois, P.1    Vu-Dac, N.2    Kleemann, R.3    Kockx, M.4    Dubois, G.5    Laine, B.6
  • 64
    • 0142116239 scopus 로고    scopus 로고
    • Transcriptional repression of atherogenic inflammation: Modulation by PPARdelta
    • C.H. Lee, A. Chawla, N. Urbiztondo, D. Liao, W.A. Boisvert, and R.M. Evans Transcriptional repression of atherogenic inflammation: modulation by PPARdelta Science 302 2003 453 457
    • (2003) Science , vol.302 , pp. 453-457
    • Lee, C.H.1    Chawla, A.2    Urbiztondo, N.3    Liao, D.4    Boisvert, W.A.5    Evans, R.M.6
  • 65
    • 14544272384 scopus 로고    scopus 로고
    • Phosphorylation of PPARs: From molecular characterization to physiological relevance
    • C. Diradourian, J. Girard, and J.P. Pegorier Phosphorylation of PPARs: from molecular characterization to physiological relevance Biochimie 87 2005 33 38
    • (2005) Biochimie , vol.87 , pp. 33-38
    • Diradourian, C.1    Girard, J.2    Pegorier, J.P.3
  • 67
    • 0038776380 scopus 로고    scopus 로고
    • Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARgamma
    • E. Hu, J.B. Kim, P. Sarraf, and B.M. Spiegelman Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARgamma Science 274 1996 2100 2103
    • (1996) Science , vol.274 , pp. 2100-2103
    • Hu, E.1    Kim, J.B.2    Sarraf, P.3    Spiegelman, B.M.4
  • 68
    • 23044488641 scopus 로고    scopus 로고
    • Regulation of peroxisome proliferator-activated receptor alpha by protein kinase C
    • J.P. Gray, K.A. Burns, T.L. Leas, G.H. Perdew, and J.P. Vanden Heuvel Regulation of peroxisome proliferator-activated receptor alpha by protein kinase C Biochemistry 44 2005 10313 10321
    • (2005) Biochemistry , vol.44 , pp. 10313-10321
    • Gray, J.P.1    Burns, K.A.2    Leas, T.L.3    Perdew, G.H.4    Vanden Heuvel, J.P.5
  • 69
    • 0033018148 scopus 로고    scopus 로고
    • Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein
    • P. Dowell, J.E. Ishmael, D. Avram, V.J. Peterson, D.J. Nevrivy, and M. Leid Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein J Biol Chem 274 1999 15901 15907
    • (1999) J Biol Chem , vol.274 , pp. 15901-15907
    • Dowell, P.1    Ishmael, J.E.2    Avram, D.3    Peterson, V.J.4    Nevrivy, D.J.5    Leid, M.6
  • 70
    • 0035977050 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase activates peroxisome proliferator-activated receptor alpha: A potential role in the cardiac metabolic stress response
    • P.M. Barger, A.C. Browning, A.N. Garner, and D.P. Kelly p38 mitogen-activated protein kinase activates peroxisome proliferator-activated receptor alpha: a potential role in the cardiac metabolic stress response J Biol Chem 276 2001 44495 44501
    • (2001) J Biol Chem , vol.276 , pp. 44495-44501
    • Barger, P.M.1    Browning, A.C.2    Garner, A.N.3    Kelly, D.P.4
  • 71
    • 0033977890 scopus 로고    scopus 로고
    • The coactivator PGC-1 cooperates with peroxisome proliferator-activated receptor alpha in transcriptional control of nuclear genes encoding mitochondrial fatty acid oxidation enzymes
    • R.B. Vega, J.M. Huss, and D.P. Kelly The coactivator PGC-1 cooperates with peroxisome proliferator-activated receptor alpha in transcriptional control of nuclear genes encoding mitochondrial fatty acid oxidation enzymes Mol Cell Biol 20 2000 1868 1876
    • (2000) Mol Cell Biol , vol.20 , pp. 1868-1876
    • Vega, R.B.1    Huss, J.M.2    Kelly, D.P.3
  • 72
    • 0035976331 scopus 로고    scopus 로고
    • The transcription of the peroxisome proliferator-activated receptor alpha gene is regulated by protein kinase C
    • N.S. Yaacob, M.N. Norazmi, G.G. Gibson, and G.E. Kass The transcription of the peroxisome proliferator-activated receptor alpha gene is regulated by protein kinase C Toxicol Lett 125 2001 133 141
    • (2001) Toxicol Lett , vol.125 , pp. 133-141
    • Yaacob, N.S.1    Norazmi, M.N.2    Gibson, G.G.3    Kass, G.E.4
  • 73
    • 0035893364 scopus 로고    scopus 로고
    • Critical roles of PPAR beta/delta in keratinocyte response to inflammation
    • N.S. Tan, L. Michalik, N. Noy, R. Yasmin, C. Pacot, and M. Heim Critical roles of PPAR beta/delta in keratinocyte response to inflammation Genes Dev 15 2001 3263 3277
    • (2001) Genes Dev , vol.15 , pp. 3263-3277
    • Tan, N.S.1    Michalik, L.2    Noy, N.3    Yasmin, R.4    Pacot, C.5    Heim, M.6
  • 74
    • 0032695358 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase inhibits 1,25-dihydroxyvitamin D3-dependent signal transduction by phosphorylating human retinoid X receptor alpha
    • C. Solomon, J.H. White, and R. Kremer Mitogen-activated protein kinase inhibits 1,25-dihydroxyvitamin D3-dependent signal transduction by phosphorylating human retinoid X receptor alpha J Clin Invest 103 1999 1729 1735
    • (1999) J Clin Invest , vol.103 , pp. 1729-1735
    • Solomon, C.1    White, J.H.2    Kremer, R.3
  • 75
    • 18244399631 scopus 로고    scopus 로고
    • Cytokine stimulation of energy expenditure through p38 MAP kinase activation of PPARgamma coactivator-1
    • P. Puigserver, J. Rhee, J. Lin, Z. Wu, J.C. Yoon, and C.Y. Zhang Cytokine stimulation of energy expenditure through p38 MAP kinase activation of PPARgamma coactivator-1 Mol Cell 8 2001 971 982
    • (2001) Mol Cell , vol.8 , pp. 971-982
    • Puigserver, P.1    Rhee, J.2    Lin, J.3    Wu, Z.4    Yoon, J.C.5    Zhang, C.Y.6
  • 76
    • 0035859836 scopus 로고    scopus 로고
    • Regulation of the transcriptional coactivator PGC-1 via MAPK-sensitive interaction with a repressor
    • D. Knutti, D. Kressler, and A. Kralli Regulation of the transcriptional coactivator PGC-1 via MAPK-sensitive interaction with a repressor Proc Natl Acad Sci USA 98 2001 9713 9718
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9713-9718
    • Knutti, D.1    Kressler, D.2    Kralli, A.3
  • 77
    • 2242451441 scopus 로고    scopus 로고
    • Phosphorylation of transcriptional coactivator peroxisome proliferator-activated receptor (PPAR)-binding protein (PBP). Stimulation of transcriptional regulation by mitogen-activated protein kinase
    • P. Misra, E.D. Owuor, W. Li, S. Yu, C. Qi, and K. Meyer Phosphorylation of transcriptional coactivator peroxisome proliferator-activated receptor (PPAR)-binding protein (PBP). Stimulation of transcriptional regulation by mitogen-activated protein kinase J Biol Chem 277 2002 48745 48754
    • (2002) J Biol Chem , vol.277 , pp. 48745-48754
    • Misra, P.1    Owuor, E.D.2    Li, W.3    Yu, S.4    Qi, C.5    Meyer, K.6
  • 78
    • 0034635553 scopus 로고    scopus 로고
    • Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway
    • B.G. Rowan, N.L. Weigel, and B.W. O'Malley Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway J Biol Chem 275 2000 4475 4483
    • (2000) J Biol Chem , vol.275 , pp. 4475-4483
    • Rowan, B.G.1    Weigel, N.L.2    O'Malley, B.W.3
  • 79
    • 0035933737 scopus 로고    scopus 로고
    • Growth factors signal to steroid receptors through mitogen-activated protein kinase regulation of p160 coactivator activity
    • G.N. Lopez, C.W. Turck, F. Schaufele, M.R. Stallcup, and P.J. Kushner Growth factors signal to steroid receptors through mitogen-activated protein kinase regulation of p160 coactivator activity J Biol Chem 276 2001 22177 22182
    • (2001) J Biol Chem , vol.276 , pp. 22177-22182
    • Lopez, G.N.1    Turck, C.W.2    Schaufele, F.3    Stallcup, M.R.4    Kushner, P.J.5
  • 80
    • 0037206890 scopus 로고    scopus 로고
    • N-CoR controls differentiation of neural stem cells into astrocytes
    • O. Hermanson, K. Jepsen, and M.G. Rosenfeld N-CoR controls differentiation of neural stem cells into astrocytes Nature 419 2002 934 939
    • (2002) Nature , vol.419 , pp. 934-939
    • Hermanson, O.1    Jepsen, K.2    Rosenfeld, M.G.3
  • 81
    • 11144230050 scopus 로고    scopus 로고
    • SMRT and N-CoR corepressors are regulated by distinct kinase signaling pathways
    • B.A. Jonas, and M.L. Privalsky SMRT and N-CoR corepressors are regulated by distinct kinase signaling pathways J Biol Chem 2004
    • (2004) J Biol Chem
    • Jonas, B.A.1    Privalsky, M.L.2
  • 82
    • 0029775642 scopus 로고    scopus 로고
    • Insulin- and mitogen-activated protein kinase-mediated phosphorylation and activation of peroxisome proliferator-activated receptor gamma
    • B. Zhang, J. Berger, G. Zhou, A. Elbrecht, S. Biswas, and S. White-Carrington Insulin- and mitogen-activated protein kinase-mediated phosphorylation and activation of peroxisome proliferator-activated receptor gamma J Biol Chem 271 1996 31771 31774
    • (1996) J Biol Chem , vol.271 , pp. 31771-31774
    • Zhang, B.1    Berger, J.2    Zhou, G.3    Elbrecht, A.4    Biswas, S.5    White-Carrington, S.6
  • 84
    • 0033212964 scopus 로고    scopus 로고
    • PPAR gamma mediates high-fat diet-induced adipocyte hypertrophy and insulin resistance
    • N. Kubota, Y. Terauchi, H. Miki, H. Tamemoto, T. Yamauchi, and K. Komeda PPAR gamma mediates high-fat diet-induced adipocyte hypertrophy and insulin resistance Mol Cell 4 1999 597 609
    • (1999) Mol Cell , vol.4 , pp. 597-609
    • Kubota, N.1    Terauchi, Y.2    Miki, H.3    Tamemoto, H.4    Yamauchi, T.5    Komeda, K.6
  • 85
    • 0036843143 scopus 로고    scopus 로고
    • A new selective peroxisome proliferator-activated receptor gamma antagonist with antiobesity and antidiabetic activity
    • J. Rieusset, F. Touri, L. Michalik, P. Escher, B. Desvergne, and E. Niesor A new selective peroxisome proliferator-activated receptor gamma antagonist with antiobesity and antidiabetic activity Mol Endocrinol 16 2002 2628 2644
    • (2002) Mol Endocrinol , vol.16 , pp. 2628-2644
    • Rieusset, J.1    Touri, F.2    Michalik, L.3    Escher, P.4    Desvergne, B.5    Niesor, E.6
  • 87
    • 18044366572 scopus 로고    scopus 로고
    • Rush hour at the promoter: How the ubiquitin-proteasome pathway polices the traffic flow of nuclear receptor-dependent transcription
    • A.P. Dennis, and B.W. O'Malley Rush hour at the promoter: how the ubiquitin-proteasome pathway polices the traffic flow of nuclear receptor-dependent transcription J Steroid Biochem Mol Biol 93 2005 139 151
    • (2005) J Steroid Biochem Mol Biol , vol.93 , pp. 139-151
    • Dennis, A.P.1    O'Malley, B.W.2
  • 88
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling
    • G. Reid, M.R. Hubner, R. Metivier, H. Brand, S. Denger, and D. Manu Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling Mol Cell 11 2003 695 707
    • (2003) Mol Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hubner, M.R.2    Metivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6
  • 89
    • 0034674567 scopus 로고    scopus 로고
    • Degradation of the peroxisome proliferator-activated receptor gamma is linked to ligand-dependent activation
    • S. Hauser, G. Adelmant, P. Sarraf, H.M. Wright, E. Mueller, and B.M. Spiegelman Degradation of the peroxisome proliferator-activated receptor gamma is linked to ligand-dependent activation J Biol Chem 275 2000 18527 18533
    • (2000) J Biol Chem , vol.275 , pp. 18527-18533
    • Hauser, S.1    Adelmant, G.2    Sarraf, P.3    Wright, H.M.4    Mueller, E.5    Spiegelman, B.M.6
  • 90
    • 0037020156 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha (PPARalpha) turnover by the ubiquitin-proteasome system controls the ligand-induced expression level of its target genes
    • C. Blanquart, O. Barbier, J.C. Fruchart, B. Staels, and C. Glineur Peroxisome proliferator-activated receptor alpha (PPARalpha) turnover by the ubiquitin-proteasome system controls the ligand-induced expression level of its target genes J Biol Chem 277 2002 37254 37259
    • (2002) J Biol Chem , vol.277 , pp. 37254-37259
    • Blanquart, C.1    Barbier, O.2    Fruchart, J.C.3    Staels, B.4    Glineur, C.5
  • 93
    • 0037040272 scopus 로고    scopus 로고
    • Interferon-gamma-mediated activation and ubiquitin-proteasome-dependent degradation of PPARgamma in adipocytes
    • Z.E. Floyd, and J.M. Stephens Interferon-gamma-mediated activation and ubiquitin-proteasome-dependent degradation of PPARgamma in adipocytes J Biol Chem 277 2002 4062 4068
    • (2002) J Biol Chem , vol.277 , pp. 4062-4068
    • Floyd, Z.E.1    Stephens, J.M.2
  • 94
    • 13544261566 scopus 로고    scopus 로고
    • Proteasome inhibitors induce peroxisome proliferator-activated receptor transactivation through RXR accumulation and a protein kinase C-dependent pathway
    • W.C. Tsao, H.M. Wu, K.H. Chi, Y.H. Chang, and W.W. Lin Proteasome inhibitors induce peroxisome proliferator-activated receptor transactivation through RXR accumulation and a protein kinase C-dependent pathway Exp Cell Res 304 2005 234 243
    • (2005) Exp Cell Res , vol.304 , pp. 234-243
    • Tsao, W.C.1    Wu, H.M.2    Chi, K.H.3    Chang, Y.H.4    Lin, W.W.5
  • 95
    • 2542421984 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor beta (delta)-dependent regulation of ubiquitin C expression contributes to attenuation of skin carcinogenesis
    • D.J. Kim, T.E. Akiyama, F.S. Harman, A.M. Burns, W. Shan, and J.M. Ward Peroxisome proliferator-activated receptor beta (delta)-dependent regulation of ubiquitin C expression contributes to attenuation of skin carcinogenesis J Biol Chem 279 2004 23719 23727
    • (2004) J Biol Chem , vol.279 , pp. 23719-23727
    • Kim, D.J.1    Akiyama, T.E.2    Harman, F.S.3    Burns, A.M.4    Shan, W.5    Ward, J.M.6
  • 96
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • R.T. Hay SUMO: a history of modification Mol Cell 18 2005 1 12
    • (2005) Mol Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 97
    • 3142716146 scopus 로고    scopus 로고
    • Transcriptional activity of peroxisome proliferator-activated receptor gamma is modulated by SUMO-1 modification
    • T. Ohshima, H. Koga, and K. Shimotohno Transcriptional activity of peroxisome proliferator-activated receptor gamma is modulated by SUMO-1 modification J Biol Chem 279 2004 29551 29557
    • (2004) J Biol Chem , vol.279 , pp. 29551-29557
    • Ohshima, T.1    Koga, H.2    Shimotohno, K.3
  • 98
    • 7944236265 scopus 로고    scopus 로고
    • The transactivating function of peroxisome proliferator-activated receptor gamma is negatively regulated by SUMO conjugation in the amino-terminal domain
    • D. Yamashita, T. Yamaguchi, M. Shimizu, N. Nakata, F. Hirose, and T. Osumi The transactivating function of peroxisome proliferator-activated receptor gamma is negatively regulated by SUMO conjugation in the amino-terminal domain Genes Cells 9 2004 1017 1029
    • (2004) Genes Cells , vol.9 , pp. 1017-1029
    • Yamashita, D.1    Yamaguchi, T.2    Shimizu, M.3    Nakata, N.4    Hirose, F.5    Osumi, T.6
  • 99
    • 0034530046 scopus 로고    scopus 로고
    • ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation
    • N. Kotaja, S. Aittomaki, O. Silvennoinen, J.J. Palvimo, and O.A. Janne ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation Mol Endocrinol 14 2000 1986 2000
    • (2000) Mol Endocrinol , vol.14 , pp. 1986-2000
    • Kotaja, N.1    Aittomaki, S.2    Silvennoinen, O.3    Palvimo, J.J.4    Janne, O.A.5
  • 100
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • G. Gill SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev 18 2004 2046 2059
    • (2004) Genes Dev , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 101
    • 0038380293 scopus 로고    scopus 로고
    • Chromatin remodeling by nuclear receptors
    • P.B. Hebbar, and T.K. Archer Chromatin remodeling by nuclear receptors Chromosoma 111 2003 495 504
    • (2003) Chromosoma , vol.111 , pp. 495-504
    • Hebbar, P.B.1    Archer, T.K.2
  • 102
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: Diversity for shared tasks
    • D. Robyr, A.P. Wolffe, and W. Wahli Nuclear hormone receptor coregulators in action: diversity for shared tasks Mol Endocrinol 14 2000 329 347
    • (2000) Mol Endocrinol , vol.14 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 103
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • N.J. McKenna, and B.W. O'Malley Combinatorial control of gene expression by nuclear receptors and coregulators Cell 108 2002 465 474
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 104
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • A.J. Horlein, A.M. Naar, T. Heinzel, J. Torchia, B. Gloss, and R. Kurokawa Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor Nature 377 1995 397 404
    • (1995) Nature , vol.377 , pp. 397-404
    • Horlein, A.J.1    Naar, A.M.2    Heinzel, T.3    Torchia, J.4    Gloss, B.5    Kurokawa, R.6
  • 105
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • J.D. Chen, and R.M. Evans A transcriptional co-repressor that interacts with nuclear hormone receptors Nature 377 1995 454 457
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 106
    • 0032526615 scopus 로고    scopus 로고
    • The corepressor N-CoR and its variants RIP13a and RIP13Delta1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70
    • G.E. Muscat, L.J. Burke, and M. Downes The corepressor N-CoR and its variants RIP13a and RIP13Delta1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70 Nucleic Acids Res 26 1998 2899 2907
    • (1998) Nucleic Acids Res , vol.26 , pp. 2899-2907
    • Muscat, G.E.1    Burke, L.J.2    Downes, M.3
  • 107
    • 0035138513 scopus 로고    scopus 로고
    • Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors
    • X. Hu, Y. Li, and M.A. Lazar Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors Mol Cell Biol 21 2001 1747 1758
    • (2001) Mol Cell Biol , vol.21 , pp. 1747-1758
    • Hu, X.1    Li, Y.2    Lazar, M.A.3
  • 108
    • 0036535037 scopus 로고    scopus 로고
    • Nuclear receptor corepressor-dependent repression of peroxisome- proliferator-activated receptor delta-mediated transactivation
    • A.M. Krogsdam, C.A. Nielsen, S. Neve, D. Holst, T. Helledie, and B. Thomsen Nuclear receptor corepressor-dependent repression of peroxisome-proliferator-activated receptor delta-mediated transactivation Biochem J 363 2002 157 165
    • (2002) Biochem J , vol.363 , pp. 157-165
    • Krogsdam, A.M.1    Nielsen, C.A.2    Neve, S.3    Holst, D.4    Helledie, T.5    Thomsen, B.6
  • 109
    • 0042072797 scopus 로고    scopus 로고
    • Subtype specific effects of peroxisome proliferator-activated receptor ligands on corepressor affinity
    • T.B. Stanley, L.M. Leesnitzer, V.G. Montana, C.M. Galardi, M.H. Lambert, and J.A. Holt Subtype specific effects of peroxisome proliferator-activated receptor ligands on corepressor affinity Biochemistry 42 2003 9278 9287
    • (2003) Biochemistry , vol.42 , pp. 9278-9287
    • Stanley, T.B.1    Leesnitzer, L.M.2    Montana, V.G.3    Galardi, C.M.4    Lambert, M.H.5    Holt, J.A.6
  • 110
    • 17144395146 scopus 로고    scopus 로고
    • The nuclear receptor corepressors NCoR and SMRT decrease peroxisome proliferator-activated receptor gamma transcriptional activity and repress 3T3-L1 adipogenesis
    • C. Yu, K. Markan, K.A. Temple, D. Deplewski, M.J. Brady, and R.N. Cohen The nuclear receptor corepressors NCoR and SMRT decrease peroxisome proliferator-activated receptor gamma transcriptional activity and repress 3T3-L1 adipogenesis J Biol Chem 280 2005 13600 13605
    • (2005) J Biol Chem , vol.280 , pp. 13600-13605
    • Yu, C.1    Markan, K.2    Temple, K.A.3    Deplewski, D.4    Brady, M.J.5    Cohen, R.N.6
  • 111
    • 0030991152 scopus 로고    scopus 로고
    • Stoichiometric and steric principles governing repression by nuclear hormone receptors
    • I. Zamir, J. Zhang, and M.A. Lazar Stoichiometric and steric principles governing repression by nuclear hormone receptors Genes Dev 11 1997 835 846
    • (1997) Genes Dev , vol.11 , pp. 835-846
    • Zamir, I.1    Zhang, J.2    Lazar, M.A.3
  • 113
    • 23644431709 scopus 로고    scopus 로고
    • TAZ, a transcriptional modulator of mesenchymal stem cell differentiation
    • J.H. Hong, E.S. Hwang, M.T. McManus, A. Amsterdam, Y. Tian, and R. Kalmukova TAZ, a transcriptional modulator of mesenchymal stem cell differentiation Science 309 2005 1074 1078
    • (2005) Science , vol.309 , pp. 1074-1078
    • Hong, J.H.1    Hwang, E.S.2    McManus, M.T.3    Amsterdam, A.4    Tian, Y.5    Kalmukova, R.6
  • 114
    • 0037022592 scopus 로고    scopus 로고
    • The peroxisome proliferator-activated receptor delta, an integrator of transcriptional repression and nuclear receptor signaling
    • Y. Shi, M. Hon, and R.M. Evans The peroxisome proliferator-activated receptor delta, an integrator of transcriptional repression and nuclear receptor signaling Proc Natl Acad Sci USA 99 2002 2613 2618
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2613-2618
    • Shi, Y.1    Hon, M.2    Evans, R.M.3
  • 115
    • 18244393501 scopus 로고    scopus 로고
    • Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha
    • H.E. Xu, T.B. Stanley, V.G. Montana, M.H. Lambert, B.G. Shearer, and J.E. Cobb Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha Nature 415 2002 813 817
    • (2002) Nature , vol.415 , pp. 813-817
    • Xu, H.E.1    Stanley, T.B.2    Montana, V.G.3    Lambert, M.H.4    Shearer, B.G.5    Cobb, J.E.6
  • 116
    • 3242881571 scopus 로고    scopus 로고
    • Corepressor recruitment by agonist-bound nuclear receptors
    • J.H. White, I. Fernandes, S. Mader, and X.J. Yang Corepressor recruitment by agonist-bound nuclear receptors Vitam Horm 68 2004 123 143
    • (2004) Vitam Horm , vol.68 , pp. 123-143
    • White, J.H.1    Fernandes, I.2    Mader, S.3    Yang, X.J.4
  • 118
    • 0032567204 scopus 로고    scopus 로고
    • Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor alpha and liver-X-receptor alpha
    • K.S. Miyata, S.E. McCaw, L.M. Meertens, H.V. Patel, R.A. Rachubinski, and J.P. Capone Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor alpha and liver-X-receptor alpha Mol Cell Endocrinol 146 1998 69 76
    • (1998) Mol Cell Endocrinol , vol.146 , pp. 69-76
    • Miyata, K.S.1    McCaw, S.E.2    Meertens, L.M.3    Patel, H.V.4    Rachubinski, R.A.5    Capone, J.P.6
  • 120
    • 0036900873 scopus 로고    scopus 로고
    • The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation
    • L. Fajas, V. Egler, R. Reiter, J. Hansen, K. Kristiansen, and M.B. Debril The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation Dev Cell 3 2002 903 910
    • (2002) Dev Cell , vol.3 , pp. 903-910
    • Fajas, L.1    Egler, V.2    Reiter, R.3    Hansen, J.4    Kristiansen, K.5    Debril, M.B.6
  • 121
    • 9744273192 scopus 로고    scopus 로고
    • Isolation and functional analysis of a keratinocyte-derived, ligand-regulated nuclear receptor comodulator
    • A.M. Flores, L. Li, and B.J. Aneskievich Isolation and functional analysis of a keratinocyte-derived, ligand-regulated nuclear receptor comodulator J Invest Dermatol 123 2004 1092 1101
    • (2004) J Invest Dermatol , vol.123 , pp. 1092-1101
    • Flores, A.M.1    Li, L.2    Aneskievich, B.J.3
  • 122
    • 0037248643 scopus 로고    scopus 로고
    • Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms
    • I. Fernandes, Y. Bastien, T. Wai, K. Nygard, R. Lin, and O. Cormier Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms Mol Cell 11 2003 139 150
    • (2003) Mol Cell , vol.11 , pp. 139-150
    • Fernandes, I.1    Bastien, Y.2    Wai, T.3    Nygard, K.4    Lin, R.5    Cormier, O.6
  • 123
    • 21744435965 scopus 로고    scopus 로고
    • Controlling nuclear receptors: The circular logic of cofactor cycles
    • V. Perissi, and M.G. Rosenfeld Controlling nuclear receptors: the circular logic of cofactor cycles Nat Rev Mol Cell Biol 6 2005 542 554
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 542-554
    • Perissi, V.1    Rosenfeld, M.G.2
  • 124
    • 1342264315 scopus 로고    scopus 로고
    • A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors
    • V. Perissi, A. Aggarwal, C.K. Glass, D.W. Rose, and M.G. Rosenfeld A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors Cell 116 2004 511 526
    • (2004) Cell , vol.116 , pp. 511-526
    • Perissi, V.1    Aggarwal, A.2    Glass, C.K.3    Rose, D.W.4    Rosenfeld, M.G.5
  • 125
    • 0037380161 scopus 로고    scopus 로고
    • Recent advances in understanding chromatin remodeling by Swi/Snf complexes
    • J.A. Martens, and F. Winston Recent advances in understanding chromatin remodeling by Swi/Snf complexes Curr Opin Genet Dev 13 2003 136 142
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 136-142
    • Martens, J.A.1    Winston, F.2
  • 126
    • 0035924326 scopus 로고    scopus 로고
    • Selectivity of chromatin-remodelling cofactors for ligand-activated transcription
    • B. Lemon, C. Inouye, D.S. King, and R. Tjian Selectivity of chromatin-remodelling cofactors for ligand-activated transcription Nature 414 2001 924 928
    • (2001) Nature , vol.414 , pp. 924-928
    • Lemon, B.1    Inouye, C.2    King, D.S.3    Tjian, R.4
  • 127
    • 1942533411 scopus 로고    scopus 로고
    • Transcription factors and nuclear receptors interact with the SWI/SNF complex through the BAF60c subunit
    • M.B. Debril, L. Gelman, E. Fayard, J.S. Annicotte, S. Rocchi, and J. Auwerx Transcription factors and nuclear receptors interact with the SWI/SNF complex through the BAF60c subunit J Biol Chem 279 2004 16677 16686
    • (2004) J Biol Chem , vol.279 , pp. 16677-16686
    • Debril, M.B.1    Gelman, L.2    Fayard, E.3    Annicotte, J.S.4    Rocchi, S.5    Auwerx, J.6
  • 128
    • 2442691703 scopus 로고    scopus 로고
    • Temporal recruitment of transcription factors and SWI/SNF chromatin-remodeling enzymes during adipogenic induction of the peroxisome proliferator-activated receptor gamma nuclear hormone receptor
    • N. Salma, H. Xiao, E. Mueller, and A.N. Imbalzano Temporal recruitment of transcription factors and SWI/SNF chromatin-remodeling enzymes during adipogenic induction of the peroxisome proliferator-activated receptor gamma nuclear hormone receptor Mol Cell Biol 24 2004 4651 4663
    • (2004) Mol Cell Biol , vol.24 , pp. 4651-4663
    • Salma, N.1    Xiao, H.2    Mueller, E.3    Imbalzano, A.N.4
  • 129
    • 0037015030 scopus 로고    scopus 로고
    • Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator
    • S. Surapureddi, S. Yu, H. Bu, T. Hashimoto, A.V. Yeldandi, and P. Kashireddy Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator Proc Natl Acad Sci USA 99 2002 11836 11841
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11836-11841
    • Surapureddi, S.1    Yu, S.2    Bu, H.3    Hashimoto, T.4    Yeldandi, A.V.5    Kashireddy, P.6
  • 130
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T. Jenuwein, and C.D. Allis Translating the histone code Science 293 2001 1074 1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 131
    • 0037425598 scopus 로고    scopus 로고
    • Histone modifications: An assembly line for active chromatin?
    • A. Imhof Histone modifications: an assembly line for active chromatin? Curr Biol 13 2003 R22 R24
    • (2003) Curr Biol , vol.13
    • Imhof, A.1
  • 132
    • 4143098311 scopus 로고    scopus 로고
    • CBP and p300: HATs for different occasions
    • E. Kalkhoven CBP and p300: HATs for different occasions Biochem Pharmacol 68 2004 1145 1155
    • (2004) Biochem Pharmacol , vol.68 , pp. 1145-1155
    • Kalkhoven, E.1
  • 133
    • 0031439111 scopus 로고    scopus 로고
    • P300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha
    • P. Dowell, J.E. Ishmael, D. Avram, V.J. Peterson, D.J. Nevrivy, and M. Leid p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha J Biol Chem 272 1997 33435 33443
    • (1997) J Biol Chem , vol.272 , pp. 33435-33443
    • Dowell, P.1    Ishmael, J.E.2    Avram, D.3    Peterson, V.J.4    Nevrivy, D.J.5    Leid, M.6
  • 134
    • 14044265869 scopus 로고    scopus 로고
    • Biochemical and NMR mapping of the interface between CREB-binding protein and ligand binding domains of nuclear receptor: Beyond the LXXLL motif
    • F.A. Klein, R.A. Atkinson, N. Potier, D. Moras, and J. Cavarelli Biochemical and NMR mapping of the interface between CREB-binding protein and ligand binding domains of nuclear receptor: beyond the LXXLL motif J Biol Chem 280 2005 5682 5692
    • (2005) J Biol Chem , vol.280 , pp. 5682-5692
    • Klein, F.A.1    Atkinson, R.A.2    Potier, N.3    Moras, D.4    Cavarelli, J.5
  • 135
    • 0036478904 scopus 로고    scopus 로고
    • Increased insulin sensitivity despite lipodystrophy in Crebbp heterozygous mice
    • T. Yamauchi, Y. Oike, J. Kamon, H. Waki, K. Komeda, and A. Tsuchida Increased insulin sensitivity despite lipodystrophy in Crebbp heterozygous mice Nat Genet 30 2002 221 226
    • (2002) Nat Genet , vol.30 , pp. 221-226
    • Yamauchi, T.1    Oike, Y.2    Kamon, J.3    Waki, H.4    Komeda, K.5    Tsuchida, A.6
  • 136
    • 0032230368 scopus 로고    scopus 로고
    • Nuclear receptors have distinct affinities for coactivators: Characterization by fluorescence resonance energy transfer
    • G. Zhou, R. Cummings, Y. Li, S. Mitra, H.A. Wilkinson, and A. Elbrecht Nuclear receptors have distinct affinities for coactivators: characterization by fluorescence resonance energy transfer Mol Endocrinol 12 1998 1594 1604
    • (1998) Mol Endocrinol , vol.12 , pp. 1594-1604
    • Zhou, G.1    Cummings, R.2    Li, Y.3    Mitra, S.4    Wilkinson, H.A.5    Elbrecht, A.6
  • 137
    • 18544390636 scopus 로고    scopus 로고
    • Ligand and coactivator recruitment preferences of peroxisome proliferator activated receptor alpha
    • R. Mukherjee, S. Sun, L. Santomenna, B. Miao, H. Walton, and B. Liao Ligand and coactivator recruitment preferences of peroxisome proliferator activated receptor alpha J Steroid Biochem Mol Biol 81 2002 217 225
    • (2002) J Steroid Biochem Mol Biol , vol.81 , pp. 217-225
    • Mukherjee, R.1    Sun, S.2    Santomenna, L.3    Miao, B.4    Walton, H.5    Liao, B.6
  • 139
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • H. Chen, R.J. Lin, R.L. Schiltz, D. Chakravarti, A. Nash, and L. Nagy Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300 Cell 90 1997 569 580
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6
  • 140
    • 1842295133 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors and retinoic acid receptors differentially control the interactions of retinoid X receptor heterodimers with ligands, coactivators, and corepressors
    • J. DiRenzo, M. Soderstrom, R. Kurokawa, M.H. Ogliastro, M. Ricote, and S. Ingrey Peroxisome proliferator-activated receptors and retinoic acid receptors differentially control the interactions of retinoid X receptor heterodimers with ligands, coactivators, and corepressors Mol Cell Biol 17 1997 2166 2176
    • (1997) Mol Cell Biol , vol.17 , pp. 2166-2176
    • Direnzo, J.1    Soderstrom, M.2    Kurokawa, R.3    Ogliastro, M.H.4    Ricote, M.5    Ingrey, S.6
  • 141
    • 0037184960 scopus 로고    scopus 로고
    • SRC-1 and TIF2 control energy balance between white and brown adipose tissues
    • F. Picard, M. Gehin, J. Annicotte, S. Rocchi, M.F. Champy, and B.W. O'Malley SRC-1 and TIF2 control energy balance between white and brown adipose tissues Cell 111 2002 931 941
    • (2002) Cell , vol.111 , pp. 931-941
    • Picard, F.1    Gehin, M.2    Annicotte, J.3    Rocchi, S.4    Champy, M.F.5    O'Malley, B.W.6
  • 142
    • 13044266369 scopus 로고    scopus 로고
    • Mouse steroid receptor coactivator-1 is not essential for peroxisome proliferator-activated receptor alpha-regulated gene expression
    • C. Qi, Y. Zhu, J. Pan, A.V. Yeldandi, M.S. Rao, and N. Maeda Mouse steroid receptor coactivator-1 is not essential for peroxisome proliferator-activated receptor alpha-regulated gene expression Proc Natl Acad Sci USA 96 1999 1585 1590
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1585-1590
    • Qi, C.1    Zhu, Y.2    Pan, J.3    Yeldandi, A.V.4    Rao, M.S.5    Maeda, N.6
  • 143
    • 0042334873 scopus 로고    scopus 로고
    • Review of the in vivo functions of the p160 steroid receptor coactivator family
    • J. Xu, and Q. Li Review of the in vivo functions of the p160 steroid receptor coactivator family Mol Endocrinol 17 2003 1681 1692
    • (2003) Mol Endocrinol , vol.17 , pp. 1681-1692
    • Xu, J.1    Li, Q.2
  • 144
    • 0033777133 scopus 로고    scopus 로고
    • Discrete roles for peroxisome proliferator-activated receptor gamma and retinoid X receptor in recruiting nuclear receptor coactivators
    • W. Yang, C. Rachez, and L.P. Freedman Discrete roles for peroxisome proliferator-activated receptor gamma and retinoid X receptor in recruiting nuclear receptor coactivators Mol Cell Biol 20 2000 8008 8017
    • (2000) Mol Cell Biol , vol.20 , pp. 8008-8017
    • Yang, W.1    Rachez, C.2    Freedman, L.P.3
  • 145
    • 0033603396 scopus 로고    scopus 로고
    • Regulation of transcription by a protein methyltransferase
    • D. Chen, H. Ma, H. Hong, S.S. Koh, S.M. Huang, and B.T. Schurter Regulation of transcription by a protein methyltransferase Science 284 1999 2174 2177
    • (1999) Science , vol.284 , pp. 2174-2177
    • Chen, D.1    Ma, H.2    Hong, H.3    Koh, S.S.4    Huang, S.M.5    Schurter, B.T.6
  • 146
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • S.S. Koh, D. Chen, Y.H. Lee, and M.R. Stallcup Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities J Biol Chem 276 2001 1089 1098
    • (2001) J Biol Chem , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 147
    • 0035800524 scopus 로고    scopus 로고
    • Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor
    • H. Wang, Z.Q. Huang, L. Xia, Q. Feng, H. Erdjument-Bromage, and B.D. Strahl Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor Science 293 2001 853 857
    • (2001) Science , vol.293 , pp. 853-857
    • Wang, H.1    Huang, Z.Q.2    Xia, L.3    Feng, Q.4    Erdjument-Bromage, H.5    Strahl, B.D.6
  • 148
    • 0037047399 scopus 로고    scopus 로고
    • Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha
    • C. Qi, J. Chang, Y. Zhu, A.V. Yeldandi, S.M. Rao, and Y.J. Zhu Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha J Biol Chem 277 2002 28624 28630
    • (2002) J Biol Chem , vol.277 , pp. 28624-28630
    • Qi, C.1    Chang, J.2    Zhu, Y.3    Yeldandi, A.V.4    Rao, S.M.5    Zhu, Y.J.6
  • 149
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Y. Shi, F. Lan, C. Matson, P. Mulligan, J.R. Whetstine, and P.A. Cole Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 Cell 119 2004 941 953
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6
  • 150
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • E. Metzger, M. Wissmann, N. Yin, J.M. Muller, R. Schneider, and A.H. Peters LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription Nature 2005
    • (2005) Nature
    • Metzger, E.1    Wissmann, M.2    Yin, N.3    Muller, J.M.4    Schneider, R.5    Peters, A.H.6
  • 151
    • 0032589689 scopus 로고    scopus 로고
    • Activation of PPARgamma coactivator-1 through transcription factor docking
    • P. Puigserver, G. Adelmant, Z. Wu, M. Fan, J. Xu, and B. O'Malley Activation of PPARgamma coactivator-1 through transcription factor docking Science 286 1999 1368 1371
    • (1999) Science , vol.286 , pp. 1368-1371
    • Puigserver, P.1    Adelmant, G.2    Wu, Z.3    Fan, M.4    Xu, J.5    O'Malley, B.6
  • 152
    • 0033638283 scopus 로고    scopus 로고
    • Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1
    • M. Monsalve, Z. Wu, G. Adelmant, P. Puigserver, M. Fan, and B.M. Spiegelman Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1 Mol Cell 6 2000 307 316
    • (2000) Mol Cell , vol.6 , pp. 307-316
    • Monsalve, M.1    Wu, Z.2    Adelmant, G.3    Puigserver, P.4    Fan, M.5    Spiegelman, B.M.6
  • 153
    • 0037453718 scopus 로고    scopus 로고
    • Peroxisome-proliferator-activated receptor delta activates fat metabolism to prevent obesity
    • Y.X. Wang, C.H. Lee, S. Tiep, R.T. Yu, J. Ham, and H. Kang Peroxisome-proliferator-activated receptor delta activates fat metabolism to prevent obesity Cell 113 2003 159 170
    • (2003) Cell , vol.113 , pp. 159-170
    • Wang, Y.X.1    Lee, C.H.2    Tiep, S.3    Yu, R.T.4    Ham, J.5    Kang, H.6
  • 154
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • P. Puigserver, Z. Wu, C.W. Park, R. Graves, M. Wright, and B.M. Spiegelman A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis Cell 92 1998 829 839
    • (1998) Cell , vol.92 , pp. 829-839
    • Puigserver, P.1    Wu, Z.2    Park, C.W.3    Graves, R.4    Wright, M.5    Spiegelman, B.M.6
  • 155
    • 0037424268 scopus 로고    scopus 로고
    • Ligand and coactivator identity determines the requirement of the charge clamp for coactivation of the peroxisome proliferator-activated receptor gamma
    • Y. Wu, W.W. Chin, Y. Wang, and T.P. Burris Ligand and coactivator identity determines the requirement of the charge clamp for coactivation of the peroxisome proliferator-activated receptor gamma J Biol Chem 278 2003 8637 8644
    • (2003) J Biol Chem , vol.278 , pp. 8637-8644
    • Wu, Y.1    Chin, W.W.2    Wang, Y.3    Burris, T.P.4
  • 156
    • 0037053326 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor (PPAR) gamma coactivator-1 recruitment regulates PPAR subtype specificity
    • H. Oberkofler, H. Esterbauer, V. Linnemayr, A.D. Strosberg, F. Krempler, and W. Patsch Peroxisome proliferator-activated receptor (PPAR) gamma coactivator-1 recruitment regulates PPAR subtype specificity J Biol Chem 277 2002 16750 16757
    • (2002) J Biol Chem , vol.277 , pp. 16750-16757
    • Oberkofler, H.1    Esterbauer, H.2    Linnemayr, V.3    Strosberg, A.D.4    Krempler, F.5    Patsch, W.6
  • 157
    • 0037326196 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): Transcriptional coactivator and metabolic regulator
    • P. Puigserver, and B.M. Spiegelman Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator Endocr Rev 24 2003 78 90
    • (2003) Endocr Rev , vol.24 , pp. 78-90
    • Puigserver, P.1    Spiegelman, B.M.2
  • 158
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family of transcription coactivators
    • J. Lin, C. Handschin, and B.M. Spiegelman Metabolic control through the PGC-1 family of transcription coactivators Cell Metab 1 2005 361 370
    • (2005) Cell Metab , vol.1 , pp. 361-370
    • Lin, J.1    Handschin, C.2    Spiegelman, B.M.3
  • 159
    • 0034607983 scopus 로고    scopus 로고
    • Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR
    • Y. Zhu, L. Kan, C. Qi, Y.S. Kanwar, A.V. Yeldandi, and M.S. Rao Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR J Biol Chem 275 2000 13510 13516
    • (2000) J Biol Chem , vol.275 , pp. 13510-13516
    • Zhu, Y.1    Kan, L.2    Qi, C.3    Kanwar, Y.S.4    Yeldandi, A.V.5    Rao, M.S.6
  • 160
    • 0035964208 scopus 로고    scopus 로고
    • Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function
    • Y. Zhu, C. Qi, W.Q. Cao, A.V. Yeldandi, M.S. Rao, and J.K. Reddy Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function Proc Natl Acad Sci USA 98 2001 10380 10385
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10380-10385
    • Zhu, Y.1    Qi, C.2    Cao, W.Q.3    Yeldandi, A.V.4    Rao, M.S.5    Reddy, J.K.6
  • 161
    • 0037449714 scopus 로고    scopus 로고
    • Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development
    • Y.J. Zhu, S.E. Crawford, V. Stellmach, R.S. Dwivedi, M.S. Rao, and F.J. Gonzalez Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development J Biol Chem 278 2003 1986 1990
    • (2003) J Biol Chem , vol.278 , pp. 1986-1990
    • Zhu, Y.J.1    Crawford, S.E.2    Stellmach, V.3    Dwivedi, R.S.4    Rao, M.S.5    Gonzalez, F.J.6
  • 162
    • 0037314821 scopus 로고    scopus 로고
    • Inactivation of the nuclear receptor coactivator RAP250 in mice results in placental vascular dysfunction
    • P. Antonson, G.U. Schuster, L. Wang, B. Rozell, E. Holter, and P. Flodby Inactivation of the nuclear receptor coactivator RAP250 in mice results in placental vascular dysfunction Mol Cell Biol 23 2003 1260 1268
    • (2003) Mol Cell Biol , vol.23 , pp. 1260-1268
    • Antonson, P.1    Schuster, G.U.2    Wang, L.3    Rozell, B.4    Holter, E.5    Flodby, P.6
  • 163
    • 0038153901 scopus 로고    scopus 로고
    • Transcriptional coactivator PRIP, the peroxisome proliferator-activated receptor gamma (PPARgamma)-interacting protein, is required for PPARgamma-mediated adipogenesis
    • C. Qi, S. Surapureddi, Y.J. Zhu, S. Yu, P. Kashireddy, and M.S. Rao Transcriptional coactivator PRIP, the peroxisome proliferator-activated receptor gamma (PPARgamma)-interacting protein, is required for PPARgamma-mediated adipogenesis J Biol Chem 278 2003 25281 25284
    • (2003) J Biol Chem , vol.278 , pp. 25281-25284
    • Qi, C.1    Surapureddi, S.2    Zhu, Y.J.3    Yu, S.4    Kashireddy, P.5    Rao, M.S.6
  • 164
    • 0141725524 scopus 로고    scopus 로고
    • The mediator coactivator complex: Functional and physical roles in transcriptional regulation
    • B.A. Lewis, and D. Reinberg The mediator coactivator complex: functional and physical roles in transcriptional regulation J Cell Sci 116 2003 3667 3675
    • (2003) J Cell Sci , vol.116 , pp. 3667-3675
    • Lewis, B.A.1    Reinberg, D.2
  • 165
    • 14544280757 scopus 로고    scopus 로고
    • Transcriptional regulation and the role of diverse coactivators in animal cells
    • R.G. Roeder Transcriptional regulation and the role of diverse coactivators in animal cells FEBS Lett 579 2005 909 915
    • (2005) FEBS Lett , vol.579 , pp. 909-915
    • Roeder, R.G.1
  • 166
    • 0030771856 scopus 로고    scopus 로고
    • Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor
    • Y. Zhu, C. Qi, S. Jain, M.S. Rao, and J.K. Reddy Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor J Biol Chem 272 1997 25500 25506
    • (1997) J Biol Chem , vol.272 , pp. 25500-25506
    • Zhu, Y.1    Qi, C.2    Jain, S.3    Rao, M.S.4    Reddy, J.K.5
  • 167
    • 0032493455 scopus 로고    scopus 로고
    • The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion
    • C.X. Yuan, M. Ito, J.D. Fondell, Z.Y. Fu, and R.G. Roeder The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion Proc Natl Acad Sci USA 95 1998 7939 7944
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7939-7944
    • Yuan, C.X.1    Ito, M.2    Fondell, J.D.3    Fu, Z.Y.4    Roeder, R.G.5
  • 168
    • 0033614417 scopus 로고    scopus 로고
    • Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex
    • C. Rachez, B.D. Lemon, Z. Suldan, V. Bromleigh, M. Gamble, and A.M. Naar Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex Nature 398 1999 824 828
    • (1999) Nature , vol.398 , pp. 824-828
    • Rachez, C.1    Lemon, B.D.2    Suldan, Z.3    Bromleigh, V.4    Gamble, M.5    Naar, A.M.6
  • 169
    • 4444333428 scopus 로고    scopus 로고
    • Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors
    • S. Malik, M. Guermah, C.X. Yuan, W. Wu, S. Yamamura, and R.G. Roeder Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors Mol Cell Biol 24 2004 8244 8254
    • (2004) Mol Cell Biol , vol.24 , pp. 8244-8254
    • Malik, S.1    Guermah, M.2    Yuan, C.X.3    Wu, W.4    Yamamura, S.5    Roeder, R.G.6
  • 170
    • 21244466640 scopus 로고    scopus 로고
    • MED1/TRAP220 exists predominantly in a TRAP/mediator subpopulation enriched in rna polymerase II and is required for ER-mediated transcription
    • X. Zhang, A. Krutchinsky, A. Fukuda, W. Chen, S. Yamamura, and B.T. Chait MED1/TRAP220 exists predominantly in a TRAP/mediator subpopulation enriched in rna polymerase II and is required for ER-mediated transcription Mol Cell 19 2005 89 100
    • (2005) Mol Cell , vol.19 , pp. 89-100
    • Zhang, X.1    Krutchinsky, A.2    Fukuda, A.3    Chen, W.4    Yamamura, S.5    Chait, B.T.6
  • 171
    • 0033635048 scopus 로고    scopus 로고
    • Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex in embryonic development and thyroid hormone action
    • M. Ito, C.X. Yuan, H.J. Okano, R.B. Darnell, and R.G. Roeder Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex in embryonic development and thyroid hormone action Mol Cell 5 2000 683 693
    • (2000) Mol Cell , vol.5 , pp. 683-693
    • Ito, M.1    Yuan, C.X.2    Okano, H.J.3    Darnell, R.B.4    Roeder, R.G.5
  • 172
    • 0034685547 scopus 로고    scopus 로고
    • Deletion of PBP/PPARBP, the gene for nuclear receptor coactivator peroxisome proliferator-activated receptor-binding protein, results in embryonic lethality
    • Y. Zhu, C. Qi, Y. Jia, J.S. Nye, M.S. Rao, and J.K. Reddy Deletion of PBP/PPARBP, the gene for nuclear receptor coactivator peroxisome proliferator-activated receptor-binding protein, results in embryonic lethality J Biol Chem 275 2000 14779 14782
    • (2000) J Biol Chem , vol.275 , pp. 14779-14782
    • Zhu, Y.1    Qi, C.2    Jia, Y.3    Nye, J.S.4    Rao, M.S.5    Reddy, J.K.6
  • 173
    • 0036479110 scopus 로고    scopus 로고
    • Defects of the heart, eye, and megakaryocytes in peroxisome proliferator activator receptor-binding protein (PBP) null embryos implicate GATA family of transcription factors
    • S.E. Crawford, C. Qi, P. Misra, V. Stellmach, M.S. Rao, and J.D. Engel Defects of the heart, eye, and megakaryocytes in peroxisome proliferator activator receptor-binding protein (PBP) null embryos implicate GATA family of transcription factors J Biol Chem 277 2002 3585 3592
    • (2002) J Biol Chem , vol.277 , pp. 3585-3592
    • Crawford, S.E.1    Qi, C.2    Misra, P.3    Stellmach, V.4    Rao, M.S.5    Engel, J.D.6
  • 174
    • 0037198679 scopus 로고    scopus 로고
    • Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis
    • K. Ge, M. Guermah, C.X. Yuan, M. Ito, A.E. Wallberg, and B.M. Spiegelman Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis Nature 417 2002 563 567
    • (2002) Nature , vol.417 , pp. 563-567
    • Ge, K.1    Guermah, M.2    Yuan, C.X.3    Ito, M.4    Wallberg, A.E.5    Spiegelman, B.M.6
  • 175
    • 2642518857 scopus 로고    scopus 로고
    • Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor alpha coregulator
    • E.S. Tien, J.W. Davis, and J.P. Vanden Heuvel Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor alpha coregulator J Biol Chem 279 2004 24053 24063
    • (2004) J Biol Chem , vol.279 , pp. 24053-24063
    • Tien, E.S.1    Davis, J.W.2    Vanden Heuvel, J.P.3
  • 176
    • 0036234545 scopus 로고    scopus 로고
    • ERAP140, a conserved tissue-specific nuclear receptor coactivator
    • W. Shao, S. Halachmi, and M. Brown ERAP140, a conserved tissue-specific nuclear receptor coactivator Mol Cell Biol 22 2002 3358 3372
    • (2002) Mol Cell Biol , vol.22 , pp. 3358-3372
    • Shao, W.1    Halachmi, S.2    Brown, M.3
  • 177
    • 0033523021 scopus 로고    scopus 로고
    • Identification of ARA70 as a ligand-enhanced coactivator for the peroxisome proliferator-activated receptor gamma
    • C.A. Heinlein, H.J. Ting, S. Yeh, and C. Chang Identification of ARA70 as a ligand-enhanced coactivator for the peroxisome proliferator-activated receptor gamma J Biol Chem 274 1999 16147 16152
    • (1999) J Biol Chem , vol.274 , pp. 16147-16152
    • Heinlein, C.A.1    Ting, H.J.2    Yeh, S.3    Chang, C.4
  • 178
    • 0344413490 scopus 로고    scopus 로고
    • Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha
    • A.E. Wallberg, S. Yamamura, S. Malik, B.M. Spiegelman, and R.G. Roeder Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha Mol Cell 12 2003 1137 1149
    • (2003) Mol Cell , vol.12 , pp. 1137-1149
    • Wallberg, A.E.1    Yamamura, S.2    Malik, S.3    Spiegelman, B.M.4    Roeder, R.G.5
  • 179
    • 0034705203 scopus 로고    scopus 로고
    • Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator
    • L. Ko, G.R. Cardona, and W.W. Chin Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator Proc Natl Acad Sci USA 97 2000 6212 6217
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6212-6217
    • Ko, L.1    Cardona, G.R.2    Chin, W.W.3
  • 180
    • 0037205403 scopus 로고    scopus 로고
    • Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation
    • P. Misra, C. Qi, S. Yu, S.H. Shah, W.Q. Cao, and M.S. Rao Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation J Biol Chem 277 2002 20011 20019
    • (2002) J Biol Chem , vol.277 , pp. 20011-20019
    • Misra, P.1    Qi, C.2    Yu, S.3    Shah, S.H.4    Cao, W.Q.5    Rao, M.S.6
  • 181
    • 5444264003 scopus 로고    scopus 로고
    • Biological control through regulated transcriptional coactivators
    • B.M. Spiegelman, and R. Heinrich Biological control through regulated transcriptional coactivators Cell 119 2004 157 167
    • (2004) Cell , vol.119 , pp. 157-167
    • Spiegelman, B.M.1    Heinrich, R.2
  • 183
    • 20744451863 scopus 로고    scopus 로고
    • A subset of nuclear receptor coregulators act as coupling proteins during synthesis and maturation of RNA transcripts
    • D. Auboeuf, D.H. Dowhan, M. Dutertre, N. Martin, S.M. Berget, and B.W. O'Malley A subset of nuclear receptor coregulators act as coupling proteins during synthesis and maturation of RNA transcripts Mol Cell Biol 25 2005 5307 5316
    • (2005) Mol Cell Biol , vol.25 , pp. 5307-5316
    • Auboeuf, D.1    Dowhan, D.H.2    Dutertre, M.3    Martin, N.4    Berget, S.M.5    O'Malley, B.W.6
  • 184
    • 23844435269 scopus 로고    scopus 로고
    • Coactivator-associated arginine methyltransferase 1, CARM1, affects pre-mRNA splicing in an isoform-specific manner
    • N. Ohkura, M. Takahashi, H. Yaguchi, Y. Nagamura, and T. Tsukada Coactivator-associated arginine methyltransferase 1, CARM1, affects pre-mRNA splicing in an isoform-specific manner J Biol Chem 280 2005 28927 28935
    • (2005) J Biol Chem , vol.280 , pp. 28927-28935
    • Ohkura, N.1    Takahashi, M.2    Yaguchi, H.3    Nagamura, Y.4    Tsukada, T.5
  • 186
    • 27844511538 scopus 로고    scopus 로고
    • Selective estrogen receptor modulators (SERMs): Mechanisms of anticarcinogenesis and drug resistance
    • J.S. Lewis, and V.C. Jordan Selective estrogen receptor modulators (SERMs): Mechanisms of anticarcinogenesis and drug resistance Mutat Res 591 2005 247 263
    • (2005) Mutat Res , vol.591 , pp. 247-263
    • Lewis, J.S.1    Jordan, V.C.2
  • 187
    • 2642557181 scopus 로고    scopus 로고
    • A unique PPARgamma ligand with potent insulin-sensitizing yet weak adipogenic activity
    • S. Rocchi, F. Picard, J. Vamecq, L. Gelman, N. Potier, and D. Zeyer A unique PPARgamma ligand with potent insulin-sensitizing yet weak adipogenic activity Mol Cell 8 2001 737 747
    • (2001) Mol Cell , vol.8 , pp. 737-747
    • Rocchi, S.1    Picard, F.2    Vamecq, J.3    Gelman, L.4    Potier, N.5    Zeyer, D.6
  • 188
    • 12444273748 scopus 로고    scopus 로고
    • Distinct properties and advantages of a novel peroxisome proliferator-activated protein [gamma] selective modulator
    • J.P. Berger, A.E. Petro, K.L. Macnaul, L.J. Kelly, B.B. Zhang, and K. Richards Distinct properties and advantages of a novel peroxisome proliferator-activated protein [gamma] selective modulator Mol Endocrinol 17 2003 662 676
    • (2003) Mol Endocrinol , vol.17 , pp. 662-676
    • Berger, J.P.1    Petro, A.E.2    MacNaul, K.L.3    Kelly, L.J.4    Zhang, B.B.5    Richards, K.6
  • 191
    • 0034021443 scopus 로고    scopus 로고
    • The novel hypoglycemic agent YM440 normalizes hyperglycemia without changing body fat weight in diabetic db/db mice
    • A. Shimaya, E. Kurosaki, R. Nakano, R. Hirayama, M. Shibasaki, and H. Shikama The novel hypoglycemic agent YM440 normalizes hyperglycemia without changing body fat weight in diabetic db/db mice Metabolism 49 2000 411 417
    • (2000) Metabolism , vol.49 , pp. 411-417
    • Shimaya, A.1    Kurosaki, E.2    Nakano, R.3    Hirayama, R.4    Shibasaki, M.5    Shikama, H.6
  • 192
    • 0037333355 scopus 로고    scopus 로고
    • Differential effects of YM440 a hypoglycemic agent on binding to a peroxisome proliferator-activated receptor gamma and its transactivation
    • E. Kurosaki, R. Nakano, A. Shimaya, S. Yoshida, M. Ida, and T. Suzuki Differential effects of YM440 a hypoglycemic agent on binding to a peroxisome proliferator-activated receptor gamma and its transactivation Biochem Pharmacol 65 2003 795 805
    • (2003) Biochem Pharmacol , vol.65 , pp. 795-805
    • Kurosaki, E.1    Nakano, R.2    Shimaya, A.3    Yoshida, S.4    Ida, M.5    Suzuki, T.6
  • 193
    • 22444447736 scopus 로고    scopus 로고
    • Imaging molecular interactions in living cells
    • R.N. Day, and F. Schaufele Imaging molecular interactions in living cells Mol Endocrinol 19 2005 1675 1686
    • (2005) Mol Endocrinol , vol.19 , pp. 1675-1686
    • Day, R.N.1    Schaufele, F.2
  • 194
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • R.D. Phair, and T. Misteli High mobility of proteins in the mammalian cell nucleus Nature 404 2000 604 609
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 195
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: Three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • R.D. Phair, P. Scaffidi, C. Elbi, J. Vecerova, A. Dey, and K. Ozato Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins Mol Cell Biol 24 2004 6393 6402
    • (2004) Mol Cell Biol , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerova, J.4    Dey, A.5    Ozato, K.6
  • 196
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • J.G. McNally, W.G. Muller, D. Walker, R. Wolford, and G.L. Hager The glucocorticoid receptor: rapid exchange with regulatory sites in living cells Science 287 2000 1262 1265
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 197
    • 15944375439 scopus 로고    scopus 로고
    • GR and HMGB1 interact only within chromatin and influence each other's residence time
    • A. Agresti, P. Scaffidi, A. Riva, V.R. Caiolfa, and M.E. Bianchi GR and HMGB1 interact only within chromatin and influence each other's residence time Mol Cell 18 2005 109 121
    • (2005) Mol Cell , vol.18 , pp. 109-121
    • Agresti, A.1    Scaffidi, P.2    Riva, A.3    Caiolfa, V.R.4    Bianchi, M.E.5
  • 198
    • 0034977031 scopus 로고    scopus 로고
    • Ligand-mediated assembly and real-time cellular dynamics of estrogen receptor alpha-coactivator complexes in living cells
    • D.L. Stenoien, A.C. Nye, M.G. Mancini, K. Patel, M. Dutertre, and B.W. O'Malley Ligand-mediated assembly and real-time cellular dynamics of estrogen receptor alpha-coactivator complexes in living cells Mol Cell Biol 21 2001 4404 4412
    • (2001) Mol Cell Biol , vol.21 , pp. 4404-4412
    • Stenoien, D.L.1    Nye, A.C.2    Mancini, M.G.3    Patel, K.4    Dutertre, M.5    O'Malley, B.W.6
  • 199
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Y. Shang, X. Hu, J. DiRenzo, M.A. Lazar, and M. Brown Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription Cell 103 2000 843 852
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    Direnzo, J.3    Lazar, M.A.4    Brown, M.5
  • 200
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • R. Metivier, G. Penot, M.R. Hubner, G. Reid, H. Brand, and M. Kos Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter Cell 115 2003 751 763
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6
  • 201
    • 1942502820 scopus 로고    scopus 로고
    • Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling
    • A.K. Nagaich, D.A. Walker, R. Wolford, and G.L. Hager Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling Mol Cell 14 2004 163 174
    • (2004) Mol Cell , vol.14 , pp. 163-174
    • Nagaich, A.K.1    Walker, D.A.2    Wolford, R.3    Hager, G.L.4
  • 202
    • 0029791412 scopus 로고    scopus 로고
    • PPARalpha and PPARgamma activators direct a distinct tissue-specific transcriptional response via a PPRE in the lipoprotein lipase gene
    • K. Schoonjans, J. Peinado-Onsurbe, A.M. Lefebvre, R.A. Heyman, M. Briggs, and S. Deeb PPARalpha and PPARgamma activators direct a distinct tissue-specific transcriptional response via a PPRE in the lipoprotein lipase gene EMBO J 15 1996 5336 5348
    • (1996) EMBO J , vol.15 , pp. 5336-5348
    • Schoonjans, K.1    Peinado-Onsurbe, J.2    Lefebvre, A.M.3    Heyman, R.A.4    Briggs, M.5    Deeb, S.6
  • 203
    • 0030658022 scopus 로고    scopus 로고
    • Coordinate regulation of the expression of the fatty acid transport protein and acyl-CoA synthetase genes by PPARalpha and PPARgamma activators
    • G. Martin, K. Schoonjans, A.M. Lefebvre, B. Staels, and J. Auwerx Coordinate regulation of the expression of the fatty acid transport protein and acyl-CoA synthetase genes by PPARalpha and PPARgamma activators J Biol Chem 272 1997 28210 28217
    • (1997) J Biol Chem , vol.272 , pp. 28210-28217
    • Martin, G.1    Schoonjans, K.2    Lefebvre, A.M.3    Staels, B.4    Auwerx, J.5
  • 204
    • 0033579432 scopus 로고    scopus 로고
    • The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase
    • N.R. Coe, A.J. Smith, B.I. Frohnert, P.A. Watkins, and D.A. Bernlohr The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase J Biol Chem 274 1999 36300 36304
    • (1999) J Biol Chem , vol.274 , pp. 36300-36304
    • Coe, N.R.1    Smith, A.J.2    Frohnert, B.I.3    Watkins, P.A.4    Bernlohr, D.A.5
  • 205
    • 3242669109 scopus 로고    scopus 로고
    • Fatty acid-binding proteins - Insights from genetic manipulations
    • N.H. Haunerland, and F. Spener Fatty acid-binding proteins - insights from genetic manipulations Prog Lipid Res 43 2004 328 349
    • (2004) Prog Lipid Res , vol.43 , pp. 328-349
    • Haunerland, N.H.1    Spener, F.2
  • 206
    • 1542283630 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha target genes
    • S. Mandard, M. Muller, and S. Kersten Peroxisome proliferator-activated receptor alpha target genes Cell Mol Life Sci 61 2004 393 416
    • (2004) Cell Mol Life Sci , vol.61 , pp. 393-416
    • Mandard, S.1    Muller, M.2    Kersten, S.3
  • 207
    • 23644445667 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor beta/delta as a therapeutic target for metabolic diseases
    • E. Bedu, W. Wahli, and B. Desvergne Peroxisome proliferator-activated receptor beta/delta as a therapeutic target for metabolic diseases Expert Opin Ther Targets 9 2005 861 873
    • (2005) Expert Opin Ther Targets , vol.9 , pp. 861-873
    • Bedu, E.1    Wahli, W.2    Desvergne, B.3
  • 208
    • 0034698051 scopus 로고    scopus 로고
    • Constitutive regulation of cardiac fatty acid metabolism through peroxisome proliferator-activated receptor alpha associated with age-dependent cardiac toxicity
    • K. Watanabe, H. Fujii, T. Takahashi, M. Kodama, Y. Aizawa, and Y. Ohta Constitutive regulation of cardiac fatty acid metabolism through peroxisome proliferator-activated receptor alpha associated with age-dependent cardiac toxicity J Biol Chem 275 2000 22293 22299
    • (2000) J Biol Chem , vol.275 , pp. 22293-22299
    • Watanabe, K.1    Fujii, H.2    Takahashi, T.3    Kodama, M.4    Aizawa, Y.5    Ohta, Y.6
  • 209
    • 0036143320 scopus 로고    scopus 로고
    • The cardiac phenotype induced by PPARalpha overexpression mimics that caused by diabetes mellitus
    • B.N. Finck, J.J. Lehman, T.C. Leone, M.J. Welch, M.J. Bennett, and A. Kovacs The cardiac phenotype induced by PPARalpha overexpression mimics that caused by diabetes mellitus J Clin Invest 109 2002 121 130
    • (2002) J Clin Invest , vol.109 , pp. 121-130
    • Finck, B.N.1    Lehman, J.J.2    Leone, T.C.3    Welch, M.J.4    Bennett, M.J.5    Kovacs, A.6
  • 210
    • 22544462381 scopus 로고    scopus 로고
    • A potential link between muscle peroxisome proliferator-activated receptor-alpha signaling and obesity-related diabetes
    • B.N. Finck, C. Bernal-Mizrachi, D.H. Han, T. Coleman, N. Sambandam, and L.L. LaRiviere A potential link between muscle peroxisome proliferator-activated receptor-alpha signaling and obesity-related diabetes Cell Metab 1 2005 133 144
    • (2005) Cell Metab , vol.1 , pp. 133-144
    • Finck, B.N.1    Bernal-Mizrachi, C.2    Han, D.H.3    Coleman, T.4    Sambandam, N.5    Lariviere, L.L.6
  • 211
    • 0032699670 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha mediates the adaptive response to fasting
    • S. Kersten, J. Seydoux, J.M. Peters, F.J. Gonzalez, B. Desvergne, and W. Wahli Peroxisome proliferator-activated receptor alpha mediates the adaptive response to fasting J Clin Invest 103 1999 1489 1498
    • (1999) J Clin Invest , vol.103 , pp. 1489-1498
    • Kersten, S.1    Seydoux, J.2    Peters, J.M.3    Gonzalez, F.J.4    Desvergne, B.5    Wahli, W.6
  • 212
    • 0033594980 scopus 로고    scopus 로고
    • A critical role for the peroxisome proliferator-activated receptor alpha (PPARalpha) in the cellular fasting response: The PPARalpha-null mouse as a model of fatty acid oxidation disorders
    • T.C. Leone, C.J. Weinheimer, and D.P. Kelly A critical role for the peroxisome proliferator-activated receptor alpha (PPARalpha) in the cellular fasting response: the PPARalpha-null mouse as a model of fatty acid oxidation disorders Proc Natl Acad Sci USA 96 1999 7473 7478
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7473-7478
    • Leone, T.C.1    Weinheimer, C.J.2    Kelly, D.P.3
  • 214
    • 0642303113 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor delta controls muscle development and oxidative capability
    • S. Luquet, J. Lopez-Soriano, D. Holst, A. Fredenrich, J. Melki, and M. Rassoulzadegan Peroxisome proliferator-activated receptor delta controls muscle development and oxidative capability FASEB J 17 2003 2299 2301
    • (2003) FASEB J , vol.17 , pp. 2299-2301
    • Luquet, S.1    Lopez-Soriano, J.2    Holst, D.3    Fredenrich, A.4    Melki, J.5    Rassoulzadegan, M.6
  • 216
    • 9144262378 scopus 로고    scopus 로고
    • Cardiomyocyte-restricted peroxisome proliferator-activated receptor-delta deletion perturbs myocardial fatty acid oxidation and leads to cardiomyopathy
    • L. Cheng, G. Ding, Q. Qin, Y. Huang, W. Lewis, and N. He Cardiomyocyte-restricted peroxisome proliferator-activated receptor-delta deletion perturbs myocardial fatty acid oxidation and leads to cardiomyopathy Nat Med 10 2004 1245 1250
    • (2004) Nat Med , vol.10 , pp. 1245-1250
    • Cheng, L.1    Ding, G.2    Qin, Q.3    Huang, Y.4    Lewis, W.5    He, N.6
  • 217
    • 0037039374 scopus 로고    scopus 로고
    • Effects of peroxisome proliferator-activated receptor delta on placentation, adiposity, and colorectal cancer
    • Y. Barak, D. Liao, W. He, E.S. Ong, M.C. Nelson, and J.M. Olefsky Effects of peroxisome proliferator-activated receptor delta on placentation, adiposity, and colorectal cancer Proc Natl Acad Sci USA 99 2002 303 308
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 303-308
    • Barak, Y.1    Liao, D.2    He, W.3    Ong, E.S.4    Nelson, M.C.5    Olefsky, J.M.6
  • 218
    • 0035091701 scopus 로고    scopus 로고
    • Comprehensive messenger ribonucleic acid profiling reveals that peroxisome proliferator-activated receptor gamma activation has coordinate effects on gene expression in multiple insulin-sensitive tissues
    • J.M. Way, W.W. Harrington, K.K. Brown, W.K. Gottschalk, S.S. Sundseth, and T.A. Mansfield Comprehensive messenger ribonucleic acid profiling reveals that peroxisome proliferator-activated receptor gamma activation has coordinate effects on gene expression in multiple insulin-sensitive tissues Endocrinology 142 2001 1269 1277
    • (2001) Endocrinology , vol.142 , pp. 1269-1277
    • Way, J.M.1    Harrington, W.W.2    Brown, K.K.3    Gottschalk, W.K.4    Sundseth, S.S.5    Mansfield, T.A.6
  • 219
    • 20944444283 scopus 로고    scopus 로고
    • Rosiglitazone increases indexes of stearoyl-CoA desaturase activity in humans: Link to insulin sensitization and the role of dominant-negative mutation in peroxisome proliferator-activated receptor-gamma
    • U. Riserus, G.D. Tan, B.A. Fielding, M.J. Neville, J. Currie, and D.B. Savage Rosiglitazone increases indexes of stearoyl-CoA desaturase activity in humans: link to insulin sensitization and the role of dominant-negative mutation in peroxisome proliferator-activated receptor-gamma Diabetes 54 2005 1379 1384
    • (2005) Diabetes , vol.54 , pp. 1379-1384
    • Riserus, U.1    Tan, G.D.2    Fielding, B.A.3    Neville, M.J.4    Currie, J.5    Savage, D.B.6
  • 220
    • 0036797450 scopus 로고    scopus 로고
    • A futile metabolic cycle activated in adipocytes by antidiabetic agents
    • H.P. Guan, Y. Li, M.V. Jensen, C.B. Newgard, C.M. Steppan, and M.A. Lazar A futile metabolic cycle activated in adipocytes by antidiabetic agents Nat Med 8 2002 1122 1128
    • (2002) Nat Med , vol.8 , pp. 1122-1128
    • Guan, H.P.1    Li, Y.2    Jensen, M.V.3    Newgard, C.B.4    Steppan, C.M.5    Lazar, M.A.6
  • 221
    • 2342466747 scopus 로고    scopus 로고
    • Adipose tissue expression of the lipid droplet-associating proteins S3-12 and perilipin is controlled by peroxisome proliferator-activated receptor-gamma
    • K.T. Dalen, K. Schoonjans, S.M. Ulven, M.S. Weedon-Fekjaer, T.G. Bentzen, and H. Koutnikova Adipose tissue expression of the lipid droplet-associating proteins S3-12 and perilipin is controlled by peroxisome proliferator-activated receptor-gamma Diabetes 53 2004 1243 1252
    • (2004) Diabetes , vol.53 , pp. 1243-1252
    • Dalen, K.T.1    Schoonjans, K.2    Ulven, S.M.3    Weedon-Fekjaer, M.S.4    Bentzen, T.G.5    Koutnikova, H.6
  • 223
    • 0347753697 scopus 로고    scopus 로고
    • Peroxisome-proliferator-activated receptors and cancers: Complex stories
    • L. Michalik, B. Desvergne, and W. Wahli Peroxisome-proliferator-activated receptors and cancers: complex stories Nat Rev Cancer 4 2004 61 70
    • (2004) Nat Rev Cancer , vol.4 , pp. 61-70
    • Michalik, L.1    Desvergne, B.2    Wahli, W.3
  • 224
    • 0031418657 scopus 로고    scopus 로고
    • Role of PPAR alpha in the mechanism of action of the nongenotoxic carcinogen and peroxisome proliferator Wy-14,643
    • J.M. Peters, R.C. Cattley, and F.J. Gonzalez Role of PPAR alpha in the mechanism of action of the nongenotoxic carcinogen and peroxisome proliferator Wy-14,643 Carcinogenesis 18 1997 2029 2033
    • (1997) Carcinogenesis , vol.18 , pp. 2029-2033
    • Peters, J.M.1    Cattley, R.C.2    Gonzalez, F.J.3
  • 225
    • 0031781381 scopus 로고    scopus 로고
    • Role of peroxisome proliferator-activated receptor alpha in altered cell cycle regulation in mouse liver
    • J.M. Peters, T. Aoyama, R.C. Cattley, U. Nobumitsu, T. Hashimoto, and F.J. Gonzalez Role of peroxisome proliferator-activated receptor alpha in altered cell cycle regulation in mouse liver Carcinogenesis 19 1998 1989 1994
    • (1998) Carcinogenesis , vol.19 , pp. 1989-1994
    • Peters, J.M.1    Aoyama, T.2    Cattley, R.C.3    Nobumitsu, U.4    Hashimoto, T.5    Gonzalez, F.J.6
  • 226
    • 26044475136 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-alpha and liver cancer: Where do we stand?
    • J.M. Peters, C. Cheung, and F.J. Gonzalez Peroxisome proliferator- activated receptor-alpha and liver cancer: where do we stand? J Mol Med 83 2005 774 785
    • (2005) J Mol Med , vol.83 , pp. 774-785
    • Peters, J.M.1    Cheung, C.2    Gonzalez, F.J.3
  • 228
    • 2542635631 scopus 로고    scopus 로고
    • Diminished hepatocellular proliferation in mice humanized for the nuclear receptor peroxisome proliferator-activated receptor alpha
    • C. Cheung, T.E. Akiyama, J.M. Ward, C.J. Nicol, L. Feigenbaum, and C. Vinson Diminished hepatocellular proliferation in mice humanized for the nuclear receptor peroxisome proliferator-activated receptor alpha Cancer Res 64 2004 3849 3854
    • (2004) Cancer Res , vol.64 , pp. 3849-3854
    • Cheung, C.1    Akiyama, T.E.2    Ward, J.M.3    Nicol, C.J.4    Feigenbaum, L.5    Vinson, C.6
  • 229
    • 0035921419 scopus 로고    scopus 로고
    • Impaired skin wound healing in peroxisome proliferator-activated receptor (PPAR)alpha and PPARbeta mutant mice
    • L. Michalik, B. Desvergne, N.S. Tan, S. Basu-Modak, P. Escher, and J. Rieusset Impaired skin wound healing in peroxisome proliferator-activated receptor (PPAR)alpha and PPARbeta mutant mice J Cell Biol 154 2001 799 814
    • (2001) J Cell Biol , vol.154 , pp. 799-814
    • Michalik, L.1    Desvergne, B.2    Tan, N.S.3    Basu-Modak, S.4    Escher, P.5    Rieusset, J.6
  • 230
    • 0033625677 scopus 로고    scopus 로고
    • Growth, adipose, brain, and skin alterations resulting from targeted disruption of the mouse peroxisome proliferator-activated receptor beta(delta)
    • J.M. Peters, S.S. Lee, W. Li, J.M. Ward, O. Gavrilova, and C. Everett Growth, adipose, brain, and skin alterations resulting from targeted disruption of the mouse peroxisome proliferator-activated receptor beta(delta) Mol Cell Biol 20 2000 5119 5128
    • (2000) Mol Cell Biol , vol.20 , pp. 5119-5128
    • Peters, J.M.1    Lee, S.S.2    Li, W.3    Ward, J.M.4    Gavrilova, O.5    Everett, C.6
  • 232
    • 0037221210 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-beta signaling contributes to enhanced proliferation of hepatic stellate cells
    • K. Hellemans, L. Michalik, A. Dittie, A. Knorr, K. Rombouts, and J. De Jong Peroxisome proliferator-activated receptor-beta signaling contributes to enhanced proliferation of hepatic stellate cells Gastroenterology 124 2003 184 201
    • (2003) Gastroenterology , vol.124 , pp. 184-201
    • Hellemans, K.1    Michalik, L.2    Dittie, A.3    Knorr, A.4    Rombouts, K.5    De Jong, J.6
  • 233
    • 0037192764 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor delta is up-regulated during vascular lesion formation and promotes post-confluent cell proliferation in vascular smooth muscle cells
    • J. Zhang, M. Fu, X. Zhu, Y. Xiao, Y. Mou, and H. Zheng Peroxisome proliferator-activated receptor delta is up-regulated during vascular lesion formation and promotes post-confluent cell proliferation in vascular smooth muscle cells J Biol Chem 277 2002 11505 11512
    • (2002) J Biol Chem , vol.277 , pp. 11505-11512
    • Zhang, J.1    Fu, M.2    Zhu, X.3    Xiao, Y.4    Mou, Y.5    Zheng, H.6
  • 234
    • 26844456319 scopus 로고    scopus 로고
    • The role of peroxisome proliferator-activated receptor-beta/delta in epithelial cell growth and differentiation
    • A.D. Burdick, D.J. Kim, M.A. Peraza, F.J. Gonzalez, and J.M. Peters The role of peroxisome proliferator-activated receptor-beta/delta in epithelial cell growth and differentiation Cell Signal 2005
    • (2005) Cell Signal
    • Burdick, A.D.1    Kim, D.J.2    Peraza, M.A.3    Gonzalez, F.J.4    Peters, J.M.5
  • 235
    • 20444497357 scopus 로고    scopus 로고
    • Receptor-independent actions of PPAR thiazolidinedione agonists: Is mitochondrial function the key?
    • D.L. Feinstein, A. Spagnolo, C. Akar, G. Weinberg, P. Murphy, and V. Gavrilyuk Receptor-independent actions of PPAR thiazolidinedione agonists: is mitochondrial function the key? Biochem Pharmacol 70 2005 177 188
    • (2005) Biochem Pharmacol , vol.70 , pp. 177-188
    • Feinstein, D.L.1    Spagnolo, A.2    Akar, C.3    Weinberg, G.4    Murphy, P.5    Gavrilyuk, V.6
  • 236
    • 4344568552 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma ligands as cell-cycle modulators
    • S. Theocharis, A. Margeli, P. Vielh, and G. Kouraklis Peroxisome proliferator-activated receptor-gamma ligands as cell-cycle modulators Cancer Treat Rev 30 2004 545 554
    • (2004) Cancer Treat Rev , vol.30 , pp. 545-554
    • Theocharis, S.1    Margeli, A.2    Vielh, P.3    Kouraklis, G.4
  • 237
    • 0030612740 scopus 로고    scopus 로고
    • PPARgamma induces cell cycle withdrawal: Inhibition of E2F/DP DNA-binding activity via down-regulation of PP2A
    • S. Altiok, M. Xu, and B.M. Spiegelman PPARgamma induces cell cycle withdrawal: inhibition of E2F/DP DNA-binding activity via down-regulation of PP2A Genes Dev 11 1997 1987 1998
    • (1997) Genes Dev , vol.11 , pp. 1987-1998
    • Altiok, S.1    Xu, M.2    Spiegelman, B.M.3
  • 238
    • 0033546003 scopus 로고    scopus 로고
    • Role of PPARgamma in regulating a cascade expression of cyclin-dependent kinase inhibitors, p18(INK4c) and p21(Waf1/Cip1), during adipogenesis
    • R.F. Morrison, and S.R. Farmer Role of PPARgamma in regulating a cascade expression of cyclin-dependent kinase inhibitors, p18(INK4c) and p21(Waf1/Cip1), during adipogenesis J Biol Chem 274 1999 17088 17097
    • (1999) J Biol Chem , vol.274 , pp. 17088-17097
    • Morrison, R.F.1    Farmer, S.R.2
  • 239
    • 0037374018 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma agonists induce proteasome-dependent degradation of cyclin D1 and estrogen receptor alpha in MCF-7 breast cancer cells
    • C. Qin, R. Burghardt, R. Smith, M. Wormke, J. Stewart, and S. Safe Peroxisome proliferator-activated receptor gamma agonists induce proteasome-dependent degradation of cyclin D1 and estrogen receptor alpha in MCF-7 breast cancer cells Cancer Res 63 2003 958 964
    • (2003) Cancer Res , vol.63 , pp. 958-964
    • Qin, C.1    Burghardt, R.2    Smith, R.3    Wormke, M.4    Stewart, J.5    Safe, S.6
  • 240
    • 0035839608 scopus 로고    scopus 로고
    • Target genes of peroxisome proliferator-activated receptor gamma in colorectal cancer cells
    • R.A. Gupta, J.A. Brockman, P. Sarraf, T.M. Willson, and R.N. DuBois Target genes of peroxisome proliferator-activated receptor gamma in colorectal cancer cells J Biol Chem 276 2001 29681 29687
    • (2001) J Biol Chem , vol.276 , pp. 29681-29687
    • Gupta, R.A.1    Brockman, J.A.2    Sarraf, P.3    Willson, T.M.4    Dubois, R.N.5
  • 241
    • 0037470070 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma and transforming growth factor-beta pathways inhibit intestinal epithelial cell growth by regulating levels of TSC-22
    • R.A. Gupta, P. Sarraf, J.A. Brockman, S.B. Shappell, L.A. Raftery, and T.M. Willson Peroxisome proliferator-activated receptor gamma and transforming growth factor-beta pathways inhibit intestinal epithelial cell growth by regulating levels of TSC-22 J Biol Chem 278 2003 7431 7438
    • (2003) J Biol Chem , vol.278 , pp. 7431-7438
    • Gupta, R.A.1    Sarraf, P.2    Brockman, J.A.3    Shappell, S.B.4    Raftery, L.A.5    Willson, T.M.6
  • 242
    • 0035873953 scopus 로고    scopus 로고
    • Tumor suppressor and anti-inflammatory actions of PPARgamma agonists are mediated via upregulation of PTEN
    • L. Patel, I. Pass, P. Coxon, C.P. Downes, S.A. Smith, and C.H. Macphee Tumor suppressor and anti-inflammatory actions of PPARgamma agonists are mediated via upregulation of PTEN Curr Biol 11 2001 764 768
    • (2001) Curr Biol , vol.11 , pp. 764-768
    • Patel, L.1    Pass, I.2    Coxon, P.3    Downes, C.P.4    Smith, S.A.5    MacPhee, C.H.6
  • 243
    • 20444439570 scopus 로고    scopus 로고
    • PPAR-gamma modulates allergic inflammation through up-regulation of PTEN
    • K.S. Lee, S.J. Park, P.H. Hwang, H.K. Yi, C.H. Song, and O.H. Chai PPAR-gamma modulates allergic inflammation through up-regulation of PTEN FASEB J 19 2005 1033 1035
    • (2005) FASEB J , vol.19 , pp. 1033-1035
    • Lee, K.S.1    Park, S.J.2    Hwang, P.H.3    Yi, H.K.4    Song, C.H.5    Chai, O.H.6
  • 244
    • 0037699445 scopus 로고    scopus 로고
    • PPARgamma controls cell proliferation and apoptosis in an RB-dependent manner
    • L. Fajas, V. Egler, R. Reiter, S. Miard, A.M. Lefebvre, and J. Auwerx PPARgamma controls cell proliferation and apoptosis in an RB-dependent manner Oncogene 22 2003 4186 4193
    • (2003) Oncogene , vol.22 , pp. 4186-4193
    • Fajas, L.1    Egler, V.2    Reiter, R.3    Miard, S.4    Lefebvre, A.M.5    Auwerx, J.6
  • 245
    • 0030831977 scopus 로고    scopus 로고
    • Peroxisome proliferator activated receptor gamma, CCAAT/enhancer-binding protein alpha, and cell cycle status regulate the commitment to adipocyte differentiation
    • D. Shao, and M.A. Lazar Peroxisome proliferator activated receptor gamma, CCAAT/enhancer-binding protein alpha, and cell cycle status regulate the commitment to adipocyte differentiation J Biol Chem 272 1997 21473 21478
    • (1997) J Biol Chem , vol.272 , pp. 21473-21478
    • Shao, D.1    Lazar, M.A.2
  • 246
    • 0034698074 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma ligands inhibit retinoblastoma phosphorylation and G1 → S transition in vascular smooth muscle cells
    • S. Wakino, U. Kintscher, S. Kim, F. Yin, W.A. Hsueh, and R.E. Law Peroxisome proliferator-activated receptor gamma ligands inhibit retinoblastoma phosphorylation and G1 → S transition in vascular smooth muscle cells J Biol Chem 275 2000 22435 22441
    • (2000) J Biol Chem , vol.275 , pp. 22435-22441
    • Wakino, S.1    Kintscher, U.2    Kim, S.3    Yin, F.4    Hsueh, W.A.5    Law, R.E.6
  • 247
    • 0037651115 scopus 로고    scopus 로고
    • PPAR-gamma receptor ligands: Novel therapy for pituitary adenomas
    • A.P. Heaney, M. Fernando, and S. Melmed PPAR-gamma receptor ligands: novel therapy for pituitary adenomas J Clin Invest 111 2003 1381 1388
    • (2003) J Clin Invest , vol.111 , pp. 1381-1388
    • Heaney, A.P.1    Fernando, M.2    Melmed, S.3
  • 249
    • 0036771764 scopus 로고    scopus 로고
    • Antiapoptotic role of PPARbeta in keratinocytes via transcriptional control of the Akt1 signaling pathway
    • N. Di-Poi, N.S. Tan, L. Michalik, W. Wahli, and B. Desvergne Antiapoptotic role of PPARbeta in keratinocytes via transcriptional control of the Akt1 signaling pathway Mol Cell 10 2002 721 733
    • (2002) Mol Cell , vol.10 , pp. 721-733
    • Di-Poi, N.1    Tan, N.S.2    Michalik, L.3    Wahli, W.4    Desvergne, B.5
  • 250
    • 14044265696 scopus 로고    scopus 로고
    • Epithelium-mesenchyme interactions control the activity of peroxisome proliferator-activated receptor beta/delta during hair follicle development
    • N. Di-Poi, C.Y. Ng, N.S. Tan, Z. Yang, B.A. Hemmings, and B. Desvergne Epithelium-mesenchyme interactions control the activity of peroxisome proliferator-activated receptor beta/delta during hair follicle development Mol Cell Biol 25 2005 1696 1712
    • (2005) Mol Cell Biol , vol.25 , pp. 1696-1712
    • Di-Poi, N.1    Ng, C.Y.2    Tan, N.S.3    Yang, Z.4    Hemmings, B.A.5    Desvergne, B.6
  • 251
    • 27944442216 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor {beta}/{delta} exerts a strong protection from ischemic acute renal failure
    • E. Letavernier, J. Perez, E. Joye, A. Bellocq, B. Fouqueray, and J.P. Haymann Peroxisome proliferator-activated receptor {beta}/{delta} exerts a strong protection from ischemic acute renal failure J Am Soc Nephrol 16 2005 2395 2402
    • (2005) J Am Soc Nephrol , vol.16 , pp. 2395-2402
    • Letavernier, E.1    Perez, J.2    Joye, E.3    Bellocq, A.4    Fouqueray, B.5    Haymann, J.P.6
  • 252
    • 0037077291 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor delta activation promotes cell survival following hypertonic stress
    • C.M. Hao, R. Redha, J. Morrow, and M.D. Breyer Peroxisome proliferator-activated receptor delta activation promotes cell survival following hypertonic stress J Biol Chem 277 2002 21341 21345
    • (2002) J Biol Chem , vol.277 , pp. 21341-21345
    • Hao, C.M.1    Redha, R.2    Morrow, J.3    Breyer, M.D.4
  • 253
  • 254
    • 0037134255 scopus 로고    scopus 로고
    • Apoptosis induced by activation of peroxisome-proliferator activated receptor-gamma is associated with Bcl-2 and NF-kappaB in human colon cancer
    • G.G. Chen, J.F. Lee, S.H. Wang, U.P. Chan, P.C. Ip, and W.Y. Lau Apoptosis induced by activation of peroxisome-proliferator activated receptor-gamma is associated with Bcl-2 and NF-kappaB in human colon cancer Life Sci 70 2002 2631 2646
    • (2002) Life Sci , vol.70 , pp. 2631-2646
    • Chen, G.G.1    Lee, J.F.2    Wang, S.H.3    Chan, U.P.4    Ip, P.C.5    Lau, W.Y.6
  • 255
    • 0033213637 scopus 로고    scopus 로고
    • PPAR gamma is required for placental, cardiac, and adipose tissue development
    • Y. Barak, M.C. Nelson, E.S. Ong, Y.Z. Jones, P. Ruiz-Lozano, and K.R. Chien PPAR gamma is required for placental, cardiac, and adipose tissue development Mol Cell 4 1999 585 595
    • (1999) Mol Cell , vol.4 , pp. 585-595
    • Barak, Y.1    Nelson, M.C.2    Ong, E.S.3    Jones, Y.Z.4    Ruiz-Lozano, P.5    Chien, K.R.6
  • 256
    • 10044235262 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma controls Muc1 transcription in trophoblasts
    • T. Shalom-Barak, J.M. Nicholas, Y. Wang, X. Zhang, E.S. Ong, and T.H. Young Peroxisome proliferator-activated receptor gamma controls Muc1 transcription in trophoblasts Mol Cell Biol 24 2004 10661 10669
    • (2004) Mol Cell Biol , vol.24 , pp. 10661-10669
    • Shalom-Barak, T.1    Nicholas, J.M.2    Wang, Y.3    Zhang, X.4    Ong, E.S.5    Young, T.H.6
  • 257
    • 0034801962 scopus 로고    scopus 로고
    • PPAR gamma/RXR alpha heterodimers are involved in human CG beta synthesis and human trophoblast differentiation
    • A. Tarrade, K. Schoonjans, J. Guibourdenche, J.M. Bidart, M. Vidaud, and J. Auwerx PPAR gamma/RXR alpha heterodimers are involved in human CG beta synthesis and human trophoblast differentiation Endocrinology 142 2001 4504 4514
    • (2001) Endocrinology , vol.142 , pp. 4504-4514
    • Tarrade, A.1    Schoonjans, K.2    Guibourdenche, J.3    Bidart, J.M.4    Vidaud, M.5    Auwerx, J.6
  • 258
    • 32644488882 scopus 로고    scopus 로고
    • PPARs: Lipid sensors that regulate cell differentiation processes
    • R. Brigelius-Flohe H.G. Joost Wiley-VCH Weinheim
    • F. Varnat, L. Michalik, B. Desvergne, and W. Wahli PPARs: lipid sensors that regulate cell differentiation processes R. Brigelius-Flohe H.G. Joost Nutritional genomics 2006 Wiley-VCH Weinheim 117 131
    • (2006) Nutritional Genomics , pp. 117-131
    • Varnat, F.1    Michalik, L.2    Desvergne, B.3    Wahli, W.4
  • 261
    • 0028871780 scopus 로고
    • Transdifferentiation of myoblasts by the adipogenic transcription factors PPAR gamma and C/EBP alpha
    • E. Hu, P. Tontonoz, and B.M. Spiegelman Transdifferentiation of myoblasts by the adipogenic transcription factors PPAR gamma and C/EBP alpha Proc Natl Acad Sci USA 92 1995 9856 9860
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9856-9860
    • Hu, E.1    Tontonoz, P.2    Spiegelman, B.M.3
  • 262
    • 0033213631 scopus 로고    scopus 로고
    • PPAR gamma is required for the differentiation of adipose tissue in vivo and in vitro
    • E.D. Rosen, P. Sarraf, A.E. Troy, G. Bradwin, K. Moore, and D.S. Milstone PPAR gamma is required for the differentiation of adipose tissue in vivo and in vitro Mol Cell 4 1999 611 617
    • (1999) Mol Cell , vol.4 , pp. 611-617
    • Rosen, E.D.1    Sarraf, P.2    Troy, A.E.3    Bradwin, G.4    Moore, K.5    Milstone, D.S.6
  • 263
    • 9144229185 scopus 로고    scopus 로고
    • Adipose-specific peroxisome proliferator-activated receptor gamma knockout causes insulin resistance in fat and liver but not in muscle
    • W. He, Y. Barak, A. Hevener, P. Olson, D. Liao, and J. Le Adipose-specific peroxisome proliferator-activated receptor gamma knockout causes insulin resistance in fat and liver but not in muscle Proc Natl Acad Sci USA 100 2003 15712 15717
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15712-15717
    • He, W.1    Barak, Y.2    Hevener, A.3    Olson, P.4    Liao, D.5    Le, J.6
  • 264
    • 12144291563 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma is required in mature white and brown adipocytes for their survival in the mouse
    • T. Imai, R. Takakuwa, S. Marchand, E. Dentz, J.M. Bornert, and N. Messaddeq Peroxisome proliferator-activated receptor gamma is required in mature white and brown adipocytes for their survival in the mouse Proc Natl Acad Sci USA 101 2004 4543 4547
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4543-4547
    • Imai, T.1    Takakuwa, R.2    Marchand, S.3    Dentz, E.4    Bornert, J.M.5    Messaddeq, N.6
  • 266
    • 9444288103 scopus 로고    scopus 로고
    • PPARbeta/delta potentiates PPARgamma-stimulated adipocyte differentiation
    • K. Matsusue, J.M. Peters, and F.J. Gonzalez PPARbeta/delta potentiates PPARgamma-stimulated adipocyte differentiation FASEB J 18 2004 1477 1479
    • (2004) FASEB J , vol.18 , pp. 1477-1479
    • Matsusue, K.1    Peters, J.M.2    Gonzalez, F.J.3
  • 267
    • 0034624046 scopus 로고    scopus 로고
    • Alterations of peroxisome proliferator-activated receptor delta activity affect fatty acid-controlled adipose differentiation
    • C. Bastie, S. Luquet, D. Holst, C. Jehl-Pietri, and P.A. Grimaldi Alterations of peroxisome proliferator-activated receptor delta activity affect fatty acid-controlled adipose differentiation J Biol Chem 275 2000 38768 38773
    • (2000) J Biol Chem , vol.275 , pp. 38768-38773
    • Bastie, C.1    Luquet, S.2    Holst, D.3    Jehl-Pietri, C.4    Grimaldi, P.A.5
  • 268
    • 0035793577 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor delta (PPARdelta)-mediated regulation of preadipocyte proliferation and gene expression is dependent on cAMP signaling
    • J.B. Hansen, H. Zhang, T.H. Rasmussen, R.K. Petersen, E.N. Flindt, and K. Kristiansen Peroxisome proliferator-activated receptor delta (PPARdelta)-mediated regulation of preadipocyte proliferation and gene expression is dependent on cAMP signaling J Biol Chem 276 2001 3175 3182
    • (2001) J Biol Chem , vol.276 , pp. 3175-3182
    • Hansen, J.B.1    Zhang, H.2    Rasmussen, T.H.3    Petersen, R.K.4    Flindt, E.N.5    Kristiansen, K.6
  • 269
    • 20444381246 scopus 로고    scopus 로고
    • Regulation of adipocyte differentiation and function by polyunsaturated fatty acids
    • L. Madsen, R.K. Petersen, and K. Kristiansen Regulation of adipocyte differentiation and function by polyunsaturated fatty acids Biochim Biophys Acta 1740 2005 266 286
    • (2005) Biochim Biophys Acta , vol.1740 , pp. 266-286
    • Madsen, L.1    Petersen, R.K.2    Kristiansen, K.3
  • 270
    • 2142652189 scopus 로고    scopus 로고
    • PPARgamma insufficiency enhances osteogenesis through osteoblast formation from bone marrow progenitors
    • T. Akune, S. Ohba, S. Kamekura, M. Yamaguchi, U.I. Chung, and N. Kubota PPARgamma insufficiency enhances osteogenesis through osteoblast formation from bone marrow progenitors J Clin Invest 113 2004 846 855
    • (2004) J Clin Invest , vol.113 , pp. 846-855
    • Akune, T.1    Ohba, S.2    Kamekura, S.3    Yamaguchi, M.4    Chung, U.I.5    Kubota, N.6
  • 272
    • 14244250617 scopus 로고    scopus 로고
    • Rosiglitazone causes bone loss in mice by suppressing osteoblast differentiation and bone formation
    • A.A. Ali, R.S. Weinstein, S.A. Stewart, A.M. Parfitt, S.C. Manolagas, and R.L. Jilka Rosiglitazone causes bone loss in mice by suppressing osteoblast differentiation and bone formation Endocrinology 146 2005 1226 1235
    • (2005) Endocrinology , vol.146 , pp. 1226-1235
    • Ali, A.A.1    Weinstein, R.S.2    Stewart, S.A.3    Parfitt, A.M.4    Manolagas, S.C.5    Jilka, R.L.6
  • 274
    • 2342579597 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor (PPAR)-beta/delta stimulates differentiation and lipid accumulation in keratinocytes
    • M. Schmuth, C.M. Haqq, W.J. Cairns, J.C. Holder, S. Dorsam, and S. Chang Peroxisome proliferator-activated receptor (PPAR)-beta/delta stimulates differentiation and lipid accumulation in keratinocytes J Invest Dermatol 122 2004 971 983
    • (2004) J Invest Dermatol , vol.122 , pp. 971-983
    • Schmuth, M.1    Haqq, C.M.2    Cairns, W.J.3    Holder, J.C.4    Dorsam, S.5    Chang, S.6
  • 275
    • 3242690411 scopus 로고    scopus 로고
    • Peroxisome-proliferator-activated receptor (PPAR)-gamma activation stimulates keratinocyte differentiation
    • M. Mao-Qiang, A.J. Fowler, M. Schmuth, P. Lau, S. Chang, and B.E. Brown Peroxisome-proliferator-activated receptor (PPAR)-gamma activation stimulates keratinocyte differentiation J Invest Dermatol 123 2004 305 312
    • (2004) J Invest Dermatol , vol.123 , pp. 305-312
    • Mao-Qiang, M.1    Fowler, A.J.2    Schmuth, M.3    Lau, P.4    Chang, S.5    Brown, B.E.6
  • 276
    • 12344281721 scopus 로고    scopus 로고
    • Functions of peroxisome proliferator-activated receptors (PPAR) in skin homeostasis
    • N. Di-Poi, L. Michalik, B. Desvergne, and W. Wahli Functions of peroxisome proliferator-activated receptors (PPAR) in skin homeostasis Lipids 39 2004 1093 1099
    • (2004) Lipids , vol.39 , pp. 1093-1099
    • Di-Poi, N.1    Michalik, L.2    Desvergne, B.3    Wahli, W.4
  • 277
    • 0032917283 scopus 로고    scopus 로고
    • Rat preputial sebocyte differentiation involves peroxisome proliferator-activated receptors
    • R.L. Rosenfield, A. Kentsis, D. Deplewski, and N. Ciletti Rat preputial sebocyte differentiation involves peroxisome proliferator-activated receptors J Invest Dermatol 112 1999 226 232
    • (1999) J Invest Dermatol , vol.112 , pp. 226-232
    • Rosenfield, R.L.1    Kentsis, A.2    Deplewski, D.3    Ciletti, N.4
  • 278
    • 0035204352 scopus 로고    scopus 로고
    • Limited cooperation between peroxisome proliferator-activated receptors and retinoid X receptor agonists in sebocyte growth and development
    • M.J. Kim, D. Deplewski, N. Ciletti, S. Michel, U. Reichert, and R.L. Rosenfield Limited cooperation between peroxisome proliferator-activated receptors and retinoid X receptor agonists in sebocyte growth and development Mol Genet Metab 74 2001 362 369
    • (2001) Mol Genet Metab , vol.74 , pp. 362-369
    • Kim, M.J.1    Deplewski, D.2    Ciletti, N.3    Michel, S.4    Reichert, U.5    Rosenfield, R.L.6
  • 279
    • 9144251051 scopus 로고    scopus 로고
    • Essential role of Smad3 in the inhibition of inflammation-induced PPARbeta/delta expression
    • N.S. Tan, L. Michalik, N. Di-Poi, C.Y. Ng, N. Mermod, and A.B. Roberts Essential role of Smad3 in the inhibition of inflammation-induced PPARbeta/delta expression EMBO J 23 2004 4211 4221
    • (2004) EMBO J , vol.23 , pp. 4211-4221
    • Tan, N.S.1    Michalik, L.2    Di-Poi, N.3    Ng, C.Y.4    Mermod, N.5    Roberts, A.B.6
  • 280
    • 24044477561 scopus 로고    scopus 로고
    • Genetic- or transforming growth factor-beta1-induced changes in epidermal peroxisome proliferator-activated receptor beta/delta expression dictate wound repair kinetics
    • N.S. Tan, L. Michalik, B. Desvergne, and W. Wahli Genetic- or transforming growth factor-beta1-induced changes in epidermal peroxisome proliferator-activated receptor beta/delta expression dictate wound repair kinetics J Biol Chem 280 2005 18163 18170
    • (2005) J Biol Chem , vol.280 , pp. 18163-18170
    • Tan, N.S.1    Michalik, L.2    Desvergne, B.3    Wahli, W.4
  • 281
    • 0032880826 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma is induced during differentiation of colon epithelium cells
    • M. Lefebvre, B. Paulweber, L. Fajas, J. Woods, C. McCrary, and J.F. Colombel Peroxisome proliferator-activated receptor gamma is induced during differentiation of colon epithelium cells J Endocrinol 162 1999 331 340
    • (1999) J Endocrinol , vol.162 , pp. 331-340
    • Lefebvre, M.1    Paulweber, B.2    Fajas, L.3    Woods, J.4    McCrary, C.5    Colombel, J.F.6
  • 282
    • 0031595670 scopus 로고    scopus 로고
    • Activation of PPARgamma leads to inhibition of anchorage-independent growth of human colorectal cancer cells
    • J.A. Brockman, R.A. Gupta, and R.N. Dubois Activation of PPARgamma leads to inhibition of anchorage-independent growth of human colorectal cancer cells Gastroenterology 115 1998 1049 1055
    • (1998) Gastroenterology , vol.115 , pp. 1049-1055
    • Brockman, J.A.1    Gupta, R.A.2    Dubois, R.N.3
  • 283
    • 0031671246 scopus 로고    scopus 로고
    • Differentiation and reversal of malignant changes in colon cancer through PPARgamma
    • P. Sarraf, E. Mueller, D. Jones, F.J. King, D.J. DeAngelo, and J.B. Partridge Differentiation and reversal of malignant changes in colon cancer through PPARgamma Nat Med 4 1998 1046 1052
    • (1998) Nat Med , vol.4 , pp. 1046-1052
    • Sarraf, P.1    Mueller, E.2    Jones, D.3    King, F.J.4    Deangelo, D.J.5    Partridge, J.B.6
  • 284
    • 0038265387 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma-mediated differentiation: A mutation in colon cancer cells reveals divergent and cell type-specific mechanisms
    • R.A. Gupta, P. Sarraf, E. Mueller, J.A. Brockman, J.J. Prusakiewicz, and C. Eng Peroxisome proliferator-activated receptor gamma-mediated differentiation: a mutation in colon cancer cells reveals divergent and cell type-specific mechanisms J Biol Chem 278 2003 22669 22677
    • (2003) J Biol Chem , vol.278 , pp. 22669-22677
    • Gupta, R.A.1    Sarraf, P.2    Mueller, E.3    Brockman, J.A.4    Prusakiewicz, J.J.5    Eng, C.6
  • 285
    • 0032540012 scopus 로고    scopus 로고
    • PPARgamma promotes monocyte/macrophage differentiation and uptake of oxidized LDL
    • P. Tontonoz, L. Nagy, J.G. Alvarez, V.A. Thomazy, and R.M. Evans PPARgamma promotes monocyte/macrophage differentiation and uptake of oxidized LDL Cell 93 1998 241 252
    • (1998) Cell , vol.93 , pp. 241-252
    • Tontonoz, P.1    Nagy, L.2    Alvarez, J.G.3    Thomazy, V.A.4    Evans, R.M.5
  • 286
    • 0035132330 scopus 로고    scopus 로고
    • PPAR-gamma dependent and independent effects on macrophage-gene expression in lipid metabolism and inflammation
    • A. Chawla, Y. Barak, L. Nagy, D. Liao, P. Tontonoz, and R.M. Evans PPAR-gamma dependent and independent effects on macrophage-gene expression in lipid metabolism and inflammation Nat Med 7 2001 48 52
    • (2001) Nat Med , vol.7 , pp. 48-52
    • Chawla, A.1    Barak, Y.2    Nagy, L.3    Liao, D.4    Tontonoz, P.5    Evans, R.M.6
  • 287
    • 0031788318 scopus 로고    scopus 로고
    • Differential expression of peroxisome proliferator-activated receptor-alpha, -beta, and -gamma during rat embryonic development
    • O. Braissant, and W. Wahli Differential expression of peroxisome proliferator-activated receptor-alpha, -beta, and -gamma during rat embryonic development Endocrinology 139 1998 2748 2754
    • (1998) Endocrinology , vol.139 , pp. 2748-2754
    • Braissant, O.1    Wahli, W.2
  • 288
    • 27944505915 scopus 로고    scopus 로고
    • PPARs in diseases: Control mechanisms of inflammation
    • R. Kostadinova, W. Wahli, and L. Michalik PPARs in diseases: control mechanisms of inflammation Curr Med Chem 12 2005 2413 2446
    • (2005) Curr Med Chem , vol.12 , pp. 2413-2446
    • Kostadinova, R.1    Wahli, W.2    Michalik, L.3
  • 290
    • 0037438377 scopus 로고    scopus 로고
    • Fibrates down-regulate IL-1-stimulated C-reactive protein gene expression in hepatocytes by reducing nuclear p50-NFkappa B-C/EBP-beta complex formation
    • R. Kleemann, P.P. Gervois, L. Verschuren, B. Staels, H.M. Princen, and T. Kooistra Fibrates down-regulate IL-1-stimulated C-reactive protein gene expression in hepatocytes by reducing nuclear p50-NFkappa B-C/EBP-beta complex formation Blood 101 2003 545 551
    • (2003) Blood , vol.101 , pp. 545-551
    • Kleemann, R.1    Gervois, P.P.2    Verschuren, L.3    Staels, B.4    Princen, H.M.5    Kooistra, T.6
  • 291
    • 0033134791 scopus 로고    scopus 로고
    • Fibrates suppress fibrinogen gene expression in rodents via activation of the peroxisome proliferator-activated receptor-alpha
    • M. Kockx, P.P. Gervois, P. Poulain, B. Derudas, J.M. Peters, and F.J. Gonzalez Fibrates suppress fibrinogen gene expression in rodents via activation of the peroxisome proliferator-activated receptor-alpha Blood 93 1999 2991 2998
    • (1999) Blood , vol.93 , pp. 2991-2998
    • Kockx, M.1    Gervois, P.P.2    Poulain, P.3    Derudas, B.4    Peters, J.M.5    Gonzalez, F.J.6
  • 292
    • 0031888958 scopus 로고    scopus 로고
    • PPAR-gamma agonists inhibit production of monocyte inflammatory cytokines
    • C. Jiang, A.T. Ting, and B. Seed PPAR-gamma agonists inhibit production of monocyte inflammatory cytokines Nature 391 1998 82 86
    • (1998) Nature , vol.391 , pp. 82-86
    • Jiang, C.1    Ting, A.T.2    Seed, B.3
  • 293
    • 24144465889 scopus 로고    scopus 로고
    • Molecular determinants of crosstalk between nuclear receptors and toll-like receptors
    • S. Ogawa, J. Lozach, C. Benner, G. Pascual, R.K. Tangirala, and S. Westin Molecular determinants of crosstalk between nuclear receptors and toll-like receptors Cell 122 2005 707 721
    • (2005) Cell , vol.122 , pp. 707-721
    • Ogawa, S.1    Lozach, J.2    Benner, C.3    Pascual, G.4    Tangirala, R.K.5    Westin, S.6
  • 294
    • 23744466617 scopus 로고    scopus 로고
    • Gaining weight: The keystone symposium on PPAR and LXR
    • M. Lehrke, G. Pascual, C.K. Glass, and M.A. Lazar Gaining weight: the keystone symposium on PPAR and LXR Genes Dev 19 2005 1737 1742
    • (2005) Genes Dev , vol.19 , pp. 1737-1742
    • Lehrke, M.1    Pascual, G.2    Glass, C.K.3    Lazar, M.A.4
  • 295
    • 12444256363 scopus 로고    scopus 로고
    • Cross-talk between peroxisome proliferator-activated receptor (PPAR) alpha and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. I. PPARs suppress sterol regulatory element binding protein-1c promoter through inhibition of LXR signaling
    • T. Yoshikawa, T. Ide, H. Shimano, N. Yahagi, M. Amemiya-Kudo, and T. Matsuzaka Cross-talk between peroxisome proliferator-activated receptor (PPAR) alpha and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. I. PPARs suppress sterol regulatory element binding protein-1c promoter through inhibition of LXR signaling Mol Endocrinol 17 2003 1240 1254
    • (2003) Mol Endocrinol , vol.17 , pp. 1240-1254
    • Yoshikawa, T.1    Ide, T.2    Shimano, H.3    Yahagi, N.4    Amemiya-Kudo, M.5    Matsuzaka, T.6
  • 296
    • 12444295462 scopus 로고    scopus 로고
    • Cross-talk between peroxisome proliferator-activated receptor (PPAR) alpha and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. II. LXRs suppress lipid degradation gene promoters through inhibition of PPAR signaling
    • T. Ide, H. Shimano, T. Yoshikawa, N. Yahagi, M. Amemiya-Kudo, and T. Matsuzaka Cross-talk between peroxisome proliferator-activated receptor (PPAR) alpha and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. II. LXRs suppress lipid degradation gene promoters through inhibition of PPAR signaling Mol Endocrinol 17 2003 1255 1267
    • (2003) Mol Endocrinol , vol.17 , pp. 1255-1267
    • Ide, T.1    Shimano, H.2    Yoshikawa, T.3    Yahagi, N.4    Amemiya-Kudo, M.5    Matsuzaka, T.6
  • 297
    • 0034669025 scopus 로고    scopus 로고
    • Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta
    • J.J. Repa, G. Liang, J. Ou, Y. Bashmakov, J.M. Lobaccaro, and I. Shimomura Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta Genes Dev 14 2000 2819 2830
    • (2000) Genes Dev , vol.14 , pp. 2819-2830
    • Repa, J.J.1    Liang, G.2    Ou, J.3    Bashmakov, Y.4    Lobaccaro, J.M.5    Shimomura, I.6
  • 298
    • 0029931972 scopus 로고    scopus 로고
    • The orphan nuclear hormone receptor LXR alpha interacts with the peroxisome proliferator-activated receptor and inhibits peroxisome proliferator signaling
    • K.S. Miyata, S.E. McCaw, H.V. Patel, R.A. Rachubinski, and J.P. Capone The orphan nuclear hormone receptor LXR alpha interacts with the peroxisome proliferator-activated receptor and inhibits peroxisome proliferator signaling J Biol Chem 271 1996 9189 9192
    • (1996) J Biol Chem , vol.271 , pp. 9189-9192
    • Miyata, K.S.1    McCaw, S.E.2    Patel, H.V.3    Rachubinski, R.A.4    Capone, J.P.5
  • 299
    • 0942279602 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma coactivator1alpha (PGC-1alpha) regulates triglyceride metabolism by activation of the nuclear receptor FXR
    • Y. Zhang, L.W. Castellani, C.J. Sinal, F.J. Gonzalez, and P.A. Edwards Peroxisome proliferator-activated receptor-gamma coactivator1alpha (PGC-1alpha) regulates triglyceride metabolism by activation of the nuclear receptor FXR Genes Dev 18 2004 157 169
    • (2004) Genes Dev , vol.18 , pp. 157-169
    • Zhang, Y.1    Castellani, L.W.2    Sinal, C.J.3    Gonzalez, F.J.4    Edwards, P.A.5
  • 300
    • 25644443217 scopus 로고    scopus 로고
    • Crosstalk between farnesoid X-receptor (FXR) and peroxisome proliferator-activated receptor (PPAR) {gamma} contributes to the anti-fibrotic activity of FXR ligands in rodent models of liver cirrhosis
    • S. Fiorucci, G. Rizzo, E. Antonelli, B. Renga, A. Mencarelli, and L. Riccardi Crosstalk between farnesoid X-receptor (FXR) and peroxisome proliferator-activated receptor (PPAR) {gamma} contributes to the anti-fibrotic activity of FXR ligands in rodent models of liver cirrhosis J Pharmacol Exp Ther 2005
    • (2005) J Pharmacol Exp Ther
    • Fiorucci, S.1    Rizzo, G.2    Antonelli, E.3    Renga, B.4    Mencarelli, A.5    Riccardi, L.6
  • 301
    • 0037315190 scopus 로고    scopus 로고
    • Bile acids induce the expression of the human peroxisome proliferator-activated receptor alpha gene via activation of the farnesoid X receptor
    • I. Pineda Torra, T. Claudel, C. Duval, V. Kosykh, J.C. Fruchart, and B. Staels Bile acids induce the expression of the human peroxisome proliferator-activated receptor alpha gene via activation of the farnesoid X receptor Mol Endocrinol 17 2003 259 272
    • (2003) Mol Endocrinol , vol.17 , pp. 259-272
    • Pineda Torra, I.1    Claudel, T.2    Duval, C.3    Kosykh, V.4    Fruchart, J.C.5    Staels, B.6
  • 303
    • 0035138625 scopus 로고    scopus 로고
    • PPAR-alpha and PPAR-gamma activators induce cholesterol removal from human macrophage foam cells through stimulation of the ABCA1 pathway
    • G. Chinetti, S. Lestavel, V. Bocher, A.T. Remaley, B. Neve, and I.P. Torra PPAR-alpha and PPAR-gamma activators induce cholesterol removal from human macrophage foam cells through stimulation of the ABCA1 pathway Nat Med 7 2001 53 58
    • (2001) Nat Med , vol.7 , pp. 53-58
    • Chinetti, G.1    Lestavel, S.2    Bocher, V.3    Remaley, A.T.4    Neve, B.5    Torra, I.P.6
  • 305
    • 17744376173 scopus 로고    scopus 로고
    • A PPAR gamma-LXR-ABCA1 pathway in macrophages is involved in cholesterol efflux and atherogenesis
    • A. Chawla, W.A. Boisvert, C.H. Lee, B.A. Laffitte, Y. Barak, and S.B. Joseph A PPAR gamma-LXR-ABCA1 pathway in macrophages is involved in cholesterol efflux and atherogenesis Mol Cell 7 2001 161 171
    • (2001) Mol Cell , vol.7 , pp. 161-171
    • Chawla, A.1    Boisvert, W.A.2    Lee, C.H.3    Laffitte, B.A.4    Barak, Y.5    Joseph, S.B.6
  • 306
    • 0036205326 scopus 로고    scopus 로고
    • Conditional disruption of the peroxisome proliferator-activated receptor gamma gene in mice results in lowered expression of ABCA1, ABCG1, and apoE in macrophages and reduced cholesterol efflux
    • T.E. Akiyama, S. Sakai, G. Lambert, C.J. Nicol, K. Matsusue, and S. Pimprale Conditional disruption of the peroxisome proliferator-activated receptor gamma gene in mice results in lowered expression of ABCA1, ABCG1, and apoE in macrophages and reduced cholesterol efflux Mol Cell Biol 22 2002 2607 2619
    • (2002) Mol Cell Biol , vol.22 , pp. 2607-2619
    • Akiyama, T.E.1    Sakai, S.2    Lambert, G.3    Nicol, C.J.4    Matsusue, K.5    Pimprale, S.6
  • 307
    • 4444337443 scopus 로고    scopus 로고
    • Transcriptional regulation of human CYP27 integrates retinoid, peroxisome proliferator-activated receptor, and liver X receptor signaling in macrophages
    • A. Szanto, S. Benko, I. Szatmari, B.L. Balint, I. Furtos, and R. Ruhl Transcriptional regulation of human CYP27 integrates retinoid, peroxisome proliferator-activated receptor, and liver X receptor signaling in macrophages Mol Cell Biol 24 2004 8154 8166
    • (2004) Mol Cell Biol , vol.24 , pp. 8154-8166
    • Szanto, A.1    Benko, S.2    Szatmari, I.3    Balint, B.L.4    Furtos, I.5    Ruhl, R.6
  • 308
    • 85047693466 scopus 로고    scopus 로고
    • Differential inhibition of macrophage foam-cell formation and atherosclerosis in mice by PPARalpha, beta/delta, and gamma
    • A.C. Li, C.J. Binder, A. Gutierrez, K.K. Brown, C.R. Plotkin, and J.W. Pattison Differential inhibition of macrophage foam-cell formation and atherosclerosis in mice by PPARalpha, beta/delta, and gamma J Clin Invest 114 2004 1564 1576
    • (2004) J Clin Invest , vol.114 , pp. 1564-1576
    • Li, A.C.1    Binder, C.J.2    Gutierrez, A.3    Brown, K.K.4    Plotkin, C.R.5    Pattison, J.W.6
  • 309
    • 0033999108 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha (PPARalpha) and agonist inhibit cholesterol 7alpha-hydroxylase gene (CYP7A1) transcription
    • M. Marrapodi, and J.Y. Chiang Peroxisome proliferator-activated receptor alpha (PPARalpha) and agonist inhibit cholesterol 7alpha-hydroxylase gene (CYP7A1) transcription J Lipid Res 41 2000 514 520
    • (2000) J Lipid Res , vol.41 , pp. 514-520
    • Marrapodi, M.1    Chiang, J.Y.2
  • 310
    • 0035570381 scopus 로고    scopus 로고
    • Fibrates suppress bile acid synthesis via peroxisome proliferator- activated receptor-alpha-mediated downregulation of cholesterol 7alpha-hydroxylase and sterol 27-hydroxylase expression
    • S.M. Post, H. Duez, P.P. Gervois, B. Staels, F. Kuipers, and H.M. Princen Fibrates suppress bile acid synthesis via peroxisome proliferator-activated receptor-alpha-mediated downregulation of cholesterol 7alpha-hydroxylase and sterol 27-hydroxylase expression Arterioscler Thromb Vasc Biol 21 2001 1840 1845
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 1840-1845
    • Post, S.M.1    Duez, H.2    Gervois, P.P.3    Staels, B.4    Kuipers, F.5    Princen, H.M.6
  • 311
    • 2542454565 scopus 로고    scopus 로고
    • Be fit or be sick: Peroxisome proliferator-activated receptors are down the road
    • B. Desvergne, L. Michalik, and W. Wahli Be fit or be sick: peroxisome proliferator-activated receptors are down the road Mol Endocrinol 18 2004 1321 1332
    • (2004) Mol Endocrinol , vol.18 , pp. 1321-1332
    • Desvergne, B.1    Michalik, L.2    Wahli, W.3
  • 312
    • 1942518840 scopus 로고    scopus 로고
    • PPARs and the complex journey to obesity
    • R.M. Evans, G.D. Barish, and Y.X. Wang PPARs and the complex journey to obesity Nat Med 10 2004 355 361
    • (2004) Nat Med , vol.10 , pp. 355-361
    • Evans, R.M.1    Barish, G.D.2    Wang, Y.X.3
  • 313
    • 0033708410 scopus 로고    scopus 로고
    • Adipose tissue is required for the antidiabetic, but not for the hypolipidemic, effect of thiazolidinediones
    • L. Chao, B. Marcus-Samuels, M.M. Mason, J. Moitra, C. Vinson, and E. Arioglu Adipose tissue is required for the antidiabetic, but not for the hypolipidemic, effect of thiazolidinediones J Clin Invest 106 2000 1221 1228
    • (2000) J Clin Invest , vol.106 , pp. 1221-1228
    • Chao, L.1    Marcus-Samuels, B.2    Mason, M.M.3    Moitra, J.4    Vinson, C.5    Arioglu, E.6
  • 316
    • 85047693638 scopus 로고    scopus 로고
    • Muscle-specific PPARgamma-deficient mice develop increased adiposity and insulin resistance but respond to thiazolidinediones
    • A.W. Norris, L. Chen, S.J. Fisher, I. Szanto, M. Ristow, and A.C. Jozsi Muscle-specific PPARgamma-deficient mice develop increased adiposity and insulin resistance but respond to thiazolidinediones J Clin Invest 112 2003 608 618
    • (2003) J Clin Invest , vol.112 , pp. 608-618
    • Norris, A.W.1    Chen, L.2    Fisher, S.J.3    Szanto, I.4    Ristow, M.5    Jozsi, A.C.6
  • 317
    • 0842263981 scopus 로고    scopus 로고
    • The biology of peroxisome proliferator-activated receptors: Relationship with lipid metabolism and insulin sensitivity
    • P. Ferre The biology of peroxisome proliferator-activated receptors: relationship with lipid metabolism and insulin sensitivity Diabetes 53 Suppl. 1
    • (2004) Diabetes , vol.53 , Issue.1 SUPPL.
    • Ferre, P.1
  • 318
    • 0035462629 scopus 로고    scopus 로고
    • PPARgamma ligands increase expression and plasma concentrations of adiponectin, an adipose-derived protein
    • N. Maeda, M. Takahashi, T. Funahashi, S. Kihara, H. Nishizawa, and K. Kishida PPARgamma ligands increase expression and plasma concentrations of adiponectin, an adipose-derived protein Diabetes 50 2001 2094 2099
    • (2001) Diabetes , vol.50 , pp. 2094-2099
    • Maeda, N.1    Takahashi, M.2    Funahashi, T.3    Kihara, S.4    Nishizawa, H.5    Kishida, K.6
  • 319
    • 0034595980 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha activators improve insulin sensitivity and reduce adiposity
    • M. Guerre-Millo, P. Gervois, E. Raspe, L. Madsen, P. Poulain, and B. Derudas Peroxisome proliferator-activated receptor alpha activators improve insulin sensitivity and reduce adiposity J Biol Chem 275 2000 16638 16642
    • (2000) J Biol Chem , vol.275 , pp. 16638-16642
    • Guerre-Millo, M.1    Gervois, P.2    Raspe, E.3    Madsen, L.4    Poulain, P.5    Derudas, B.6
  • 320
    • 9144271149 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptor delta induces fatty acid beta-oxidation in skeletal muscle and attenuates metabolic syndrome
    • T. Tanaka, J. Yamamoto, S. Iwasaki, H. Asaba, H. Hamura, and Y. Ikeda Activation of peroxisome proliferator-activated receptor delta induces fatty acid beta-oxidation in skeletal muscle and attenuates metabolic syndrome Proc Natl Acad Sci USA 100 2003 15924 15929
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15924-15929
    • Tanaka, T.1    Yamamoto, J.2    Iwasaki, S.3    Asaba, H.4    Hamura, H.5    Ikeda, Y.6
  • 321
    • 0034744590 scopus 로고    scopus 로고
    • PPARalpha deficiency reduces insulin resistance and atherosclerosis in apoE-null mice
    • K. Tordjman, C. Bernal-Mizrachi, L. Zemany, S. Weng, C. Feng, and F. Zhang PPARalpha deficiency reduces insulin resistance and atherosclerosis in apoE-null mice J Clin Invest 107 2001 1025 1034
    • (2001) J Clin Invest , vol.107 , pp. 1025-1034
    • Tordjman, K.1    Bernal-Mizrachi, C.2    Zemany, L.3    Weng, S.4    Feng, C.5    Zhang, F.6
  • 322
    • 0035653490 scopus 로고    scopus 로고
    • PPAR-alpha-null mice are protected from high-fat diet-induced insulin resistance
    • M. Guerre-Millo, C. Rouault, P. Poulain, J. Andre, V. Poitout, and J.M. Peters PPAR-alpha-null mice are protected from high-fat diet-induced insulin resistance Diabetes 50 2001 2809 2814
    • (2001) Diabetes , vol.50 , pp. 2809-2814
    • Guerre-Millo, M.1    Rouault, C.2    Poulain, P.3    Andre, J.4    Poitout, V.5    Peters, J.M.6
  • 323
    • 24144490615 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of peroxisome proliferator-activated receptor-{alpha} causes insulin resistance in heart and liver
    • S.Y. Park, Y.R. Cho, B.N. Finck, H.J. Kim, T. Higashimori, and E.G. Hong Cardiac-specific overexpression of peroxisome proliferator-activated receptor-{alpha} causes insulin resistance in heart and liver Diabetes 54 2005 2514 2524
    • (2005) Diabetes , vol.54 , pp. 2514-2524
    • Park, S.Y.1    Cho, Y.R.2    Finck, B.N.3    Kim, H.J.4    Higashimori, T.5    Hong, E.G.6
  • 324
    • 0034666157 scopus 로고    scopus 로고
    • Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene
    • S. Kersten, S. Mandard, N.S. Tan, P. Escher, D. Metzger, and P. Chambon Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene J Biol Chem 275 2000 28488 28493
    • (2000) J Biol Chem , vol.275 , pp. 28488-28493
    • Kersten, S.1    Mandard, S.2    Tan, N.S.3    Escher, P.4    Metzger, D.5    Chambon, P.6
  • 325
    • 0343060983 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma target gene encoding a novel angiopoietin-related protein associated with adipose differentiation
    • J.C. Yoon, T.W. Chickering, E.D. Rosen, B. Dussault, Y. Qin, and A. Soukas Peroxisome proliferator-activated receptor gamma target gene encoding a novel angiopoietin-related protein associated with adipose differentiation Mol Cell Biol 20 2000 5343 5349
    • (2000) Mol Cell Biol , vol.20 , pp. 5343-5349
    • Yoon, J.C.1    Chickering, T.W.2    Rosen, E.D.3    Dussault, B.4    Qin, Y.5    Soukas, A.6
  • 326
    • 13444250891 scopus 로고    scopus 로고
    • Inhibition of cardiac lipoprotein utilization by transgenic overexpression of Angptl4 in the heart
    • X. Yu, S.C. Burgess, H. Ge, K.K. Wong, R.H. Nassem, and D.J. Garry Inhibition of cardiac lipoprotein utilization by transgenic overexpression of Angptl4 in the heart Proc Natl Acad Sci USA 102 2005 1767 1772
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1767-1772
    • Yu, X.1    Burgess, S.C.2    Ge, H.3    Wong, K.K.4    Nassem, R.H.5    Garry, D.J.6
  • 327
    • 0036847133 scopus 로고    scopus 로고
    • Angiopoietin-like protein 4 is a potent hyperlipidemia-inducing factor in mice and inhibitor of lipoprotein lipase
    • K. Yoshida, T. Shimizugawa, M. Ono, and H. Furukawa Angiopoietin-like protein 4 is a potent hyperlipidemia-inducing factor in mice and inhibitor of lipoprotein lipase J Lipid Res 43 2002 1770 1772
    • (2002) J Lipid Res , vol.43 , pp. 1770-1772
    • Yoshida, K.1    Shimizugawa, T.2    Ono, M.3    Furukawa, H.4
  • 328
    • 13444302796 scopus 로고    scopus 로고
    • Oligomerization state-dependent hyperlipidemic effect of angiopoietin-like protein 4
    • H. Ge, G. Yang, X. Yu, T. Pourbahrami, and C. Li Oligomerization state-dependent hyperlipidemic effect of angiopoietin-like protein 4 J Lipid Res 45 2004 2071 2079
    • (2004) J Lipid Res , vol.45 , pp. 2071-2079
    • Ge, H.1    Yang, G.2    Yu, X.3    Pourbahrami, T.4    Li, C.5
  • 329
    • 26844540456 scopus 로고    scopus 로고
    • Transgenic Angptl4 overexpression and targeted disruption of Angptl4 and Angptl3: Regulation of triglyceride metabolism
    • A. Koster, Y.B. Chao, M. Mosior, A. Ford, P.A. Gonzalez-Dewhitt, and J.E. Hale Transgenic Angptl4 overexpression and targeted disruption of Angptl4 and Angptl3: regulation of triglyceride metabolism Endocrinology 2005
    • (2005) Endocrinology
    • Koster, A.1    Chao, Y.B.2    Mosior, M.3    Ford, A.4    Gonzalez-Dewhitt, P.A.5    Hale, J.E.6
  • 330
    • 32644454369 scopus 로고    scopus 로고
    • The fasting-induced adipose factor/angiopoietin-like protein 4 is physically associated with lipoproteins and governs plasma lipid levels and adiposity
    • S. Mandard, F. Zandbergen, E. van Straten, W. Wahli, F. Kuipers, and M. Müller The fasting-induced adipose factor/angiopoietin-like protein 4 is physically associated with lipoproteins and governs plasma lipid levels and adiposity J Biol Chem 281 2006 934 944
    • (2006) J Biol Chem , vol.281 , pp. 934-944
    • Mandard, S.1    Zandbergen, F.2    Van Straten, E.3    Wahli, W.4    Kuipers, F.5    Müller, M.6
  • 331
    • 20944447890 scopus 로고    scopus 로고
    • Angiopoietin-like protein 4 decreases blood glucose and improves glucose tolerance but induces hyperlipidemia and hepatic steatosis in mice
    • A. Xu, M.C. Lam, K.W. Chan, Y. Wang, J. Zhang, and R.L. Hoo Angiopoietin-like protein 4 decreases blood glucose and improves glucose tolerance but induces hyperlipidemia and hepatic steatosis in mice Proc Natl Acad Sci USA 102 2005 6086 6091
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6086-6091
    • Xu, A.1    Lam, M.C.2    Chan, K.W.3    Wang, Y.4    Zhang, J.5    Hoo, R.L.6
  • 332
    • 0028003839 scopus 로고
    • Regulation of the peroxisome proliferator-activated receptor alpha gene by glucocorticoids
    • T. Lemberger, B. Staels, R. Saladin, B. Desvergne, J. Auwerx, and W. Wahli Regulation of the peroxisome proliferator-activated receptor alpha gene by glucocorticoids J Biol Chem 269 1994 24527 24530
    • (1994) J Biol Chem , vol.269 , pp. 24527-24530
    • Lemberger, T.1    Staels, B.2    Saladin, R.3    Desvergne, B.4    Auwerx, J.5    Wahli, W.6
  • 333
    • 0030060358 scopus 로고    scopus 로고
    • Expression of the peroxisome proliferator-activated receptor alpha gene is stimulated by stress and follows a diurnal rhythm
    • T. Lemberger, R. Saladin, M. Vazquez, F. Assimacopoulos, B. Staels, and B. Desvergne Expression of the peroxisome proliferator-activated receptor alpha gene is stimulated by stress and follows a diurnal rhythm J Biol Chem 271 1996 1764 1769
    • (1996) J Biol Chem , vol.271 , pp. 1764-1769
    • Lemberger, T.1    Saladin, R.2    Vazquez, M.3    Assimacopoulos, F.4    Staels, B.5    Desvergne, B.6
  • 334
    • 0042967650 scopus 로고    scopus 로고
    • Dexamethasone induction of hypertension and diabetes is PPAR-alpha dependent in LDL receptor-null mice
    • C. Bernal-Mizrachi, S. Weng, C. Feng, B.N. Finck, R.H. Knutsen, and T.C. Leone Dexamethasone induction of hypertension and diabetes is PPAR-alpha dependent in LDL receptor-null mice Nat Med 9 2003 1069 1075
    • (2003) Nat Med , vol.9 , pp. 1069-1075
    • Bernal-Mizrachi, C.1    Weng, S.2    Feng, C.3    Finck, B.N.4    Knutsen, R.H.5    Leone, T.C.6
  • 335
    • 0035918143 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma ligands inhibit adipocyte 11beta -hydroxysteroid dehydrogenase type 1 expression and activity
    • J. Berger, M. Tanen, A. Elbrecht, A. Hermanowski-Vosatka, D.E. Moller, and S.D. Wright Peroxisome proliferator-activated receptor-gamma ligands inhibit adipocyte 11beta -hydroxysteroid dehydrogenase type 1 expression and activity J Biol Chem 276 2001 12629 12635
    • (2001) J Biol Chem , vol.276 , pp. 12629-12635
    • Berger, J.1    Tanen, M.2    Elbrecht, A.3    Hermanowski-Vosatka, A.4    Moller, D.E.5    Wright, S.D.6
  • 336
    • 18844401577 scopus 로고    scopus 로고
    • The human peroxisome proliferator-activated receptor delta gene is a primary target of 1alpha,25-dihydroxyvitamin D3 and its nuclear receptor
    • T.W. Dunlop, S. Vaisanen, C. Frank, F. Molnar, L. Sinkkonen, and C. Carlberg The human peroxisome proliferator-activated receptor delta gene is a primary target of 1alpha,25-dihydroxyvitamin D3 and its nuclear receptor J Mol Biol 349 2005 248 260
    • (2005) J Mol Biol , vol.349 , pp. 248-260
    • Dunlop, T.W.1    Vaisanen, S.2    Frank, C.3    Molnar, F.4    Sinkkonen, L.5    Carlberg, C.6
  • 337
    • 24344502005 scopus 로고    scopus 로고
    • Selective expression of a dominant-negative form of peroxisome proliferator-activated receptor in keratinocytes leads to impaired epidermal healing
    • L. Michalik, J.N. Feige, L. Gelman, T. Pedrazzini, H. Keller, and B. Desvergne Selective expression of a dominant-negative form of peroxisome proliferator-activated receptor in keratinocytes leads to impaired epidermal healing Mol Endocrinol 19 2005 2335 2348
    • (2005) Mol Endocrinol , vol.19 , pp. 2335-2348
    • Michalik, L.1    Feige, J.N.2    Gelman, L.3    Pedrazzini, T.4    Keller, H.5    Desvergne, B.6
  • 338
    • 32644487946 scopus 로고    scopus 로고
    • Transcriptional repression of peroxisome proliferator-activated receptor beta/delta in murine keratinocytes by CCAAT/enhancer-binding proteins
    • N. Di-Poi, B. Desvergne, L. Michalik, and W. Wahli Transcriptional repression of peroxisome proliferator-activated receptor beta/delta in murine keratinocytes by CCAAT/enhancer-binding proteins J Biol Chem 280 2005 38700 38710
    • (2005) J Biol Chem , vol.280 , pp. 38700-38710
    • Di-Poi, N.1    Desvergne, B.2    Michalik, L.3    Wahli, W.4


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