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Volumn 332, Issue 1-2, 2011, Pages 21-31

Transcriptional co-factors and hepatic energy metabolism

Author keywords

Liver; Metabolic Syndrome; Metabolism; Transcriptional co factors

Indexed keywords

ACYLTRANSFERASE; COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE; HISTONE ACETYLTRANSFERASE GCN5; HISTONE ACETYLTRANSFERASE PCAF; HISTONE ACETYLTRANSFERASE TRANSFORMATION TRANSCRIPTION DOMAIN ASSOCIATED PROTEIN; HISTONE DEACETYLASE; METHYLTRANSFERASE; NUCLEAR RECEPTOR COACTIVATOR 2; NUCLEAR RECEPTOR DAX 1; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; RECEPTOR INTERACTING PROTEIN 140; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR; SIRTUIN 1; STEROID RECEPTOR COACTIVATOR 1; TG INTERACTING FACTOR 1; TRANSDUCER OF REGULATED CREB ACTIVITY; TRIPARTITE MOTIF PROTEIN 24; UNCLASSIFIED DRUG;

EID: 78650523232     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2010.11.020     Document Type: Review
Times cited : (14)

References (164)
  • 2
    • 0032936343 scopus 로고    scopus 로고
    • Glucocorticoids and insulin resistance: old hormones, new targets
    • Andrews R.C., Walker B.R. Glucocorticoids and insulin resistance: old hormones, new targets. Clin. Sci. (Lond.) 1999, 96:513-523.
    • (1999) Clin. Sci. (Lond.) , vol.96 , pp. 513-523
    • Andrews, R.C.1    Walker, B.R.2
  • 3
    • 0035838957 scopus 로고    scopus 로고
    • Metabolic interrelationships between liver and skeletal muscle in pathological states
    • Argiles J.M., Busquets S., Lopez-Soriano F.J. Metabolic interrelationships between liver and skeletal muscle in pathological states. Life Sci. 2001, 69:1345-1361.
    • (2001) Life Sci. , vol.69 , pp. 1345-1361
    • Argiles, J.M.1    Busquets, S.2    Lopez-Soriano, F.J.3
  • 4
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister A.J., Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature 1996, 384:641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 5
    • 0037218786 scopus 로고    scopus 로고
    • Regulation of tumor necrosis factor alpha gene expression by mycobacteria involves the assembly of a unique enhanceosome dependent on the coactivator proteins CBP/p300
    • Barthel R., Tsytsykova A.V., Barczak A.K., Tsai E.Y., Dascher C.C., Brenner M.B., Goldfeld A.E. Regulation of tumor necrosis factor alpha gene expression by mycobacteria involves the assembly of a unique enhanceosome dependent on the coactivator proteins CBP/p300. Mol. Cell. Biol. 2003, 23:526-533.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 526-533
    • Barthel, R.1    Tsytsykova, A.V.2    Barczak, A.K.3    Tsai, E.Y.4    Dascher, C.C.5    Brenner, M.B.6    Goldfeld, A.E.7
  • 8
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation an emerging regulator of protein function
    • Bedford M.T., Richard S. Arginine methylation an emerging regulator of protein function. Mol. Cell 2005, 18:263-272.
    • (2005) Mol. Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 10
    • 0029558541 scopus 로고
    • A novel homeobox protein which recognizes a TGT core and functionally interferes with a retinoid-responsive motif
    • Bertolino E., Reimund B., Wildt-Perinic D., Clerc R.G. A novel homeobox protein which recognizes a TGT core and functionally interferes with a retinoid-responsive motif. J. Biol. Chem. 1995, 270:31178-31188.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31178-31188
    • Bertolino, E.1    Reimund, B.2    Wildt-Perinic, D.3    Clerc, R.G.4
  • 11
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell J.E., Zhou J., Ranalli T., Kobayashi R., Edmondson D.G., Roth S.Y., Allis C.D. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 1996, 84:843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 12
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001, 414:813-820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 13
    • 30944455145 scopus 로고    scopus 로고
    • Insulin resistance: a metabolic pathway to chronic liver disease
    • Bugianesi E., McCullough A.J., Marchesini G. Insulin resistance: a metabolic pathway to chronic liver disease. Hepatology 2005, 42:987-1000.
    • (2005) Hepatology , vol.42 , pp. 987-1000
    • Bugianesi, E.1    McCullough, A.J.2    Marchesini, G.3
  • 14
    • 0029694433 scopus 로고    scopus 로고
    • The gene responsible for adrenal hypoplasia congenita, DAX-1, encodes a nuclear hormone receptor that defines a new class within the superfamily
    • discussion 259-260
    • Burris T.P., Guo W., McCabe E.R. The gene responsible for adrenal hypoplasia congenita, DAX-1, encodes a nuclear hormone receptor that defines a new class within the superfamily. Recent Prog. Horm. Res. 1996, 51:241-259. discussion 259-260.
    • (1996) Recent Prog. Horm. Res. , vol.51 , pp. 241-259
    • Burris, T.P.1    Guo, W.2    McCabe, E.R.3
  • 15
    • 0026549217 scopus 로고
    • Regulation of the expression of the mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase gene. Its role in the control of ketogenesis
    • Casals N., Roca N., Guerrero M., Gil-Gomez G., Ayte J., Ciudad C.J., Hegardt F.G. Regulation of the expression of the mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase gene. Its role in the control of ketogenesis. Biochem. J. 1992, 283(Pt 1):261-264.
    • (1992) Biochem. J. , vol.283 , Issue.PART 1 , pp. 261-264
    • Casals, N.1    Roca, N.2    Guerrero, M.3    Gil-Gomez, G.4    Ayte, J.5    Ciudad, C.J.6    Hegardt, F.G.7
  • 22
    • 0142121328 scopus 로고    scopus 로고
    • DAX1 and its network partners: exploring complexity in development
    • Clipsham R., McCabe E.R. DAX1 and its network partners: exploring complexity in development. Mol. Genet. Metab. 2003, 80:81-120.
    • (2003) Mol. Genet. Metab. , vol.80 , pp. 81-120
    • Clipsham, R.1    McCabe, E.R.2
  • 24
    • 0026591523 scopus 로고
    • Role of liver in pathophysiology of NIDDM
    • Consoli A. Role of liver in pathophysiology of NIDDM. Diabetes Care 1992, 15:430-441.
    • (1992) Diabetes Care , vol.15 , pp. 430-441
    • Consoli, A.1
  • 26
    • 0027194913 scopus 로고
    • Insulin action on the internalization of the GLUT4 glucose transporter in isolated rat adipocytes
    • Czech M.P., Buxton J.M. Insulin action on the internalization of the GLUT4 glucose transporter in isolated rat adipocytes. J. Biol. Chem. 1993, 268:9187-9190.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9187-9190
    • Czech, M.P.1    Buxton, J.M.2
  • 27
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • Dentin R., Hedrick S., Xie J., Yates J., Montminy M. Hepatic glucose sensing via the CREB coactivator CRTC2. Science 2008, 319:1402-1405.
    • (2008) Science , vol.319 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3    Yates, J.4    Montminy, M.5
  • 28
    • 40949165722 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fatty acid oxidation in vivo only slightly suppresses gluconeogenesis but enhances clearance of glucose in mice
    • Derks T.G., van Dijk T.H., Grefhorst A., Rake J.P., Smit G.P., Kuipers F., Reijngoud D.J. Inhibition of mitochondrial fatty acid oxidation in vivo only slightly suppresses gluconeogenesis but enhances clearance of glucose in mice. Hepatology 2008, 47:1032-1042.
    • (2008) Hepatology , vol.47 , pp. 1032-1042
    • Derks, T.G.1    van Dijk, T.H.2    Grefhorst, A.3    Rake, J.P.4    Smit, G.P.5    Kuipers, F.6    Reijngoud, D.J.7
  • 29
    • 0033305213 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors: nuclear control of metabolism
    • Desvergne B., Wahli W. Peroxisome proliferator-activated receptors: nuclear control of metabolism. Endocr. Rev. 1999, 20:649-688.
    • (1999) Endocr. Rev. , vol.20 , pp. 649-688
    • Desvergne, B.1    Wahli, W.2
  • 30
    • 0038242819 scopus 로고    scopus 로고
    • TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver
    • Du K., Herzig S., Kulkarni R.N., Montminy M. TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver. Science 2003, 300:1574-1577.
    • (2003) Science , vol.300 , pp. 1574-1577
    • Du, K.1    Herzig, S.2    Kulkarni, R.N.3    Montminy, M.4
  • 31
    • 0024466571 scopus 로고
    • Regulation of very-low-density-lipoprotein lipid secretion in hepatocyte cultures derived from diabetic animals
    • Duerden J.M., Bartlett S.M., Gibbons G.F. Regulation of very-low-density-lipoprotein lipid secretion in hepatocyte cultures derived from diabetic animals. Biochem. J. 1989, 262:313-319.
    • (1989) Biochem. J. , vol.262 , pp. 313-319
    • Duerden, J.M.1    Bartlett, S.M.2    Gibbons, G.F.3
  • 32
    • 0034613316 scopus 로고    scopus 로고
    • Fatty acid regulation of gene transcription
    • Duplus E., Glorian M., Forest C. Fatty acid regulation of gene transcription. J. Biol. Chem. 2000, 275:30749-30752.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30749-30752
    • Duplus, E.1    Glorian, M.2    Forest, C.3
  • 33
    • 0022977874 scopus 로고
    • Apolipoprotein A-IV. A determinant for binding and uptake of high density lipoproteins by rat hepatocytes
    • Dvorin E., Gorder N.L., Benson D.M., Gotto A.M. Apolipoprotein A-IV. A determinant for binding and uptake of high density lipoproteins by rat hepatocytes. J. Biol. Chem. 1986, 261:15714-15718.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15714-15718
    • Dvorin, E.1    Gorder, N.L.2    Benson, D.M.3    Gotto, A.M.4
  • 34
    • 38949212965 scopus 로고    scopus 로고
    • Aging and anti-aging: unexpected side effects of everyday medication through sirtuin1 modulation
    • Engel N., Mahlknecht U. Aging and anti-aging: unexpected side effects of everyday medication through sirtuin1 modulation. Int. J. Mol. Med. 2008, 21:223-232.
    • (2008) Int. J. Mol. Med. , vol.21 , pp. 223-232
    • Engel, N.1    Mahlknecht, U.2
  • 39
    • 0027288233 scopus 로고
    • Glucocorticoids regulate the induction of phosphoenolpyruvate carboxykinase (GTP) gene transcription during diabetes
    • Friedman J.E., Yun J.S., Patel Y.M., McGrane M.M., Hanson R.W. Glucocorticoids regulate the induction of phosphoenolpyruvate carboxykinase (GTP) gene transcription during diabetes. J. Biol. Chem. 1993, 268:12952-12957.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12952-12957
    • Friedman, J.E.1    Yun, J.S.2    Patel, Y.M.3    McGrane, M.M.4    Hanson, R.W.5
  • 40
    • 0031438356 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxykinase (GTP) gene transcription and hyperglycemia are regulated by glucocorticoids in genetically obese db/db transgenic mice
    • Friedman J.E., Sun Y., Ishizuka T., Farrell C.J., McCormack S.E., Herron L.M., Hakimi P., Lechner P., Yun J.S. Phosphoenolpyruvate carboxykinase (GTP) gene transcription and hyperglycemia are regulated by glucocorticoids in genetically obese db/db transgenic mice. J. Biol. Chem. 1997, 272:31475-31481.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31475-31481
    • Friedman, J.E.1    Sun, Y.2    Ishizuka, T.3    Farrell, C.J.4    McCormack, S.E.5    Herron, L.M.6    Hakimi, P.7    Lechner, P.8    Yun, J.S.9
  • 42
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye R.A. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 1999, 260:273-279.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 45
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass C.K., Rosenfeld M.G. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 2000, 14:121-141.
    • (2000) Genes Dev. , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 46
    • 0024445798 scopus 로고
    • Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
    • Gonzalez G.A., Montminy M.R. Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133. Cell 1989, 59:675-680.
    • (1989) Cell , vol.59 , pp. 675-680
    • Gonzalez, G.A.1    Montminy, M.R.2
  • 47
    • 22744444561 scopus 로고    scopus 로고
    • Calorie restriction and SIR2 genes-towards a mechanism
    • Guarente L. Calorie restriction and SIR2 genes-towards a mechanism. Mech. Ageing Dev. 2005, 126:923-928.
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 923-928
    • Guarente, L.1
  • 48
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3
    • Guenther M.G., Barak O., Lazar M.A. The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol. Cell. Biol. 2001, 21:6091-6101.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6091-6101
    • Guenther, M.G.1    Barak, O.2    Lazar, M.A.3
  • 49
    • 1542328927 scopus 로고    scopus 로고
    • Structure, regulation and function of PKB/AKT-a major therapeutic target
    • Hanada M., Feng J., Hemmings B.A. Structure, regulation and function of PKB/AKT-a major therapeutic target. Biochim. Biophys. Acta 2004, 1697:3-16.
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 3-16
    • Hanada, M.1    Feng, J.2    Hemmings, B.A.3
  • 50
    • 33845596500 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma coactivator 1 coactivators, energy homeostasis, and metabolism
    • Handschin C., Spiegelman B.M. Peroxisome proliferator-activated receptor gamma coactivator 1 coactivators, energy homeostasis, and metabolism. Endocr. Rev. 2006, 27:728-735.
    • (2006) Endocr. Rev. , vol.27 , pp. 728-735
    • Handschin, C.1    Spiegelman, B.M.2
  • 51
    • 0030998776 scopus 로고    scopus 로고
    • Regulation of phosphoenolpyruvate carboxykinase (GTP) gene expression
    • Hanson R.W., Reshef L. Regulation of phosphoenolpyruvate carboxykinase (GTP) gene expression. Annu. Rev. Biochem. 1997, 66:581-611.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 581-611
    • Hanson, R.W.1    Reshef, L.2
  • 52
    • 0033559336 scopus 로고    scopus 로고
    • Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis
    • Hegardt F.G. Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis. Biochem. J. 1999, 338(Pt 3):569-582.
    • (1999) Biochem. J. , vol.338 , Issue.PART 3 , pp. 569-582
    • Hegardt, F.G.1
  • 54
    • 35649023189 scopus 로고    scopus 로고
    • The nuclear receptor cofactor, receptor-interacting protein 140, is required for the regulation of hepatic lipid and glucose metabolism by liver X receptor
    • Herzog B., Hallberg M., Seth A., Woods A., White R., Parker M.G. The nuclear receptor cofactor, receptor-interacting protein 140, is required for the regulation of hepatic lipid and glucose metabolism by liver X receptor. Mol. Endocrinol. 2007, 21:2687-2697.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 2687-2697
    • Herzog, B.1    Hallberg, M.2    Seth, A.3    Woods, A.4    White, R.5    Parker, M.G.6
  • 55
    • 0038517917 scopus 로고    scopus 로고
    • Liver X receptors interact with corepressors to regulate gene expression
    • Hu X., Li S., Wu J., Xia C., Lala D.S. Liver X receptors interact with corepressors to regulate gene expression. Mol. Endocrinol. 2003, 17:1019-1026.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1019-1026
    • Hu, X.1    Li, S.2    Wu, J.3    Xia, C.4    Lala, D.S.5
  • 56
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang E.Y., Zhang J., Miska E.A., Guenther M.G., Kouzarides T., Lazar M.A. Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 2000, 14:45-54.
    • (2000) Genes Dev. , vol.14 , pp. 45-54
    • Huang, E.Y.1    Zhang, J.2    Miska, E.A.3    Guenther, M.G.4    Kouzarides, T.5    Lazar, M.A.6
  • 57
    • 0034852862 scopus 로고    scopus 로고
    • Protein kinase C activation: isozyme-specific effects on metabolism and cardiovascular complications in diabetes
    • Idris I., Gray S., Donnelly R. Protein kinase C activation: isozyme-specific effects on metabolism and cardiovascular complications in diabetes. Diabetologia 2001, 44:659-673.
    • (2001) Diabetologia , vol.44 , pp. 659-673
    • Idris, I.1    Gray, S.2    Donnelly, R.3
  • 59
    • 67449118954 scopus 로고    scopus 로고
    • Impaired PRMT1 activity in the liver and pancreas of type 2 diabetic Goto-Kakizaki rats
    • Iwasaki H. Impaired PRMT1 activity in the liver and pancreas of type 2 diabetic Goto-Kakizaki rats. Life Sci. 2009, 85:161-166.
    • (2009) Life Sci. , vol.85 , pp. 161-166
    • Iwasaki, H.1
  • 60
    • 4944263717 scopus 로고    scopus 로고
    • Molecular mechanisms of DAX1 action
    • Iyer A.K., McCabe E.R. Molecular mechanisms of DAX1 action. Mol. Genet. Metab. 2004, 83:60-73.
    • (2004) Mol. Genet. Metab. , vol.83 , pp. 60-73
    • Iyer, A.K.1    McCabe, E.R.2
  • 62
    • 0026661997 scopus 로고
    • Effects of insulin on steady state kinetics of GLUT4 subcellular distribution in rat adipocytes. Evidence of constitutive GLUT4 recycling
    • Jhun B.H., Rampal A.L., Liu H., Lachaal M., Jung C.Y. Effects of insulin on steady state kinetics of GLUT4 subcellular distribution in rat adipocytes. Evidence of constitutive GLUT4 recycling. J. Biol. Chem. 1992, 267:17710-17715.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17710-17715
    • Jhun, B.H.1    Rampal, A.L.2    Liu, H.3    Lachaal, M.4    Jung, C.Y.5
  • 63
    • 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
    • Jia Y., Qi C., Kashireddi P., Surapureddi S., Zhu Y.J., Rao M.S., Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K. Transcription coactivator PBP, the peroxisome proliferator-activated receptor (PPAR)-binding protein, is required for PPARalpha-regulated gene expression in liver. J. Biol. Chem. 2004, 279:24427-24434.
    • (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    Le Roith, D.7    Chambon, P.8    Gonzalez, F.J.9    Reddy, J.K.10
  • 64
    • 68349159285 scopus 로고    scopus 로고
    • Conditional ablation of mediator subunit MED1 (MED1/PPARBP) gene in mouse liver attenuates glucocorticoid receptor agonist dexamethasone-induced hepatic steatosis
    • Jia Y., Viswakarma N., Fu T., Yu S., Rao M.S., Borensztajn J., Reddy J.K. Conditional ablation of mediator subunit MED1 (MED1/PPARBP) gene in mouse liver attenuates glucocorticoid receptor agonist dexamethasone-induced hepatic steatosis. Gene Expr. 2009, 14:291-306.
    • (2009) Gene Expr. , vol.14 , pp. 291-306
    • Jia, Y.1    Viswakarma, N.2    Fu, T.3    Yu, S.4    Rao, M.S.5    Borensztajn, J.6    Reddy, J.K.7
  • 65
    • 0035937783 scopus 로고    scopus 로고
    • Multiple N-CoR complexes contain distinct histone deacetylases
    • Jones P.L., Sachs L.M., Rouse N., Wade P.A., Shi Y.B. Multiple N-CoR complexes contain distinct histone deacetylases. J. Biol. Chem. 2001, 276:8807-8811.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8807-8811
    • Jones, P.L.1    Sachs, L.M.2    Rouse, N.3    Wade, P.A.4    Shi, Y.B.5
  • 66
    • 13844272212 scopus 로고    scopus 로고
    • Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation
    • Kaiser C., James S.R. Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation. BMC Biol. 2004, 2:23.
    • (2004) BMC Biol. , vol.2 , pp. 23
    • Kaiser, C.1    James, S.R.2
  • 67
    • 0141481039 scopus 로고    scopus 로고
    • Induction of intestinal ATP-binding cassette transporters by a phytosterol-derived liver X receptor agonist
    • Kaneko E., Matsuda M., Yamada Y., Tachibana Y., Shimomura I., Makishima M. Induction of intestinal ATP-binding cassette transporters by a phytosterol-derived liver X receptor agonist. J. Biol. Chem. 2003, 278:36091-36098.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36091-36098
    • Kaneko, E.1    Matsuda, M.2    Yamada, Y.3    Tachibana, Y.4    Shimomura, I.5    Makishima, M.6
  • 69
    • 57349132931 scopus 로고    scopus 로고
    • Trim24 (Tif1 alpha): an essential 'brake' for retinoic acid-induced transcription to prevent liver cancer
    • Khetchoumian K., Teletin M., Tisserand J., Herquel B., Ouararhni K., Losson R. Trim24 (Tif1 alpha): an essential 'brake' for retinoic acid-induced transcription to prevent liver cancer. Cell Cycle 2008, 7:3647-3652.
    • (2008) Cell Cycle , vol.7 , pp. 3647-3652
    • Khetchoumian, K.1    Teletin, M.2    Tisserand, J.3    Herquel, B.4    Ouararhni, K.5    Losson, R.6
  • 71
    • 41949120723 scopus 로고    scopus 로고
    • Liver-specific deletion of histone deacetylase 3 disrupts metabolic transcriptional networks
    • Knutson S.K., Chyla B.J., Amann J.M., Bhaskara S., Huppert S.S., Hiebert S.W. Liver-specific deletion of histone deacetylase 3 disrupts metabolic transcriptional networks. EMBO J. 2008, 27:1017-1028.
    • (2008) EMBO J. , vol.27 , pp. 1017-1028
    • Knutson, S.K.1    Chyla, B.J.2    Amann, J.M.3    Bhaskara, S.4    Huppert, S.S.5    Hiebert, S.W.6
  • 73
    • 0034116143 scopus 로고    scopus 로고
    • A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen
    • Knutti D., Kaul A., Kralli A. A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen. Mol. Cell. Biol. 2000, 20:2411-2422.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2411-2422
    • Knutti, D.1    Kaul, A.2    Kralli, A.3
  • 74
    • 73649108251 scopus 로고    scopus 로고
    • Stable chromatin binding prevents FoxA acetylation, preserving FoxA chromatin remodeling
    • Kohler S., Cirillo L.A. Stable chromatin binding prevents FoxA acetylation, preserving FoxA chromatin remodeling. J. Biol. Chem. 2010, 285:464-472.
    • (2010) J. Biol. Chem. , vol.285 , pp. 464-472
    • Kohler, S.1    Cirillo, L.A.2
  • 77
    • 0036094275 scopus 로고    scopus 로고
    • Nuclear receptor-dependent transcription with chromatin. Is it all about enzymes?
    • Kraus W.L., Wong J. Nuclear receptor-dependent transcription with chromatin. Is it all about enzymes?. Eur. J. Biochem. 2002, 269:2275-2283.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2275-2283
    • Kraus, W.L.1    Wong, J.2
  • 78
    • 33645649005 scopus 로고    scopus 로고
    • Signal-dependent control of gluconeogenic key enzyme genes through coactivator-associated arginine methyltransferase 1
    • Krones-Herzig A., Mesaros A., Metzger D., Ziegler A., Lemke U., Bruning J.C., Herzig S. Signal-dependent control of gluconeogenic key enzyme genes through coactivator-associated arginine methyltransferase 1. J. Biol. Chem. 2006, 281:3025-3029.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3025-3029
    • Krones-Herzig, A.1    Mesaros, A.2    Metzger, D.3    Ziegler, A.4    Lemke, U.5    Bruning, J.C.6    Herzig, S.7
  • 79
    • 0030253348 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of non-insulin dependent diabetes mellitus
    • Kruszynska Y.T., Olefsky J.M. Cellular and molecular mechanisms of non-insulin dependent diabetes mellitus. J. Investig. Med. 1996, 44:413-428.
    • (1996) J. Investig. Med. , vol.44 , pp. 413-428
    • Kruszynska, Y.T.1    Olefsky, J.M.2
  • 83
    • 0028295518 scopus 로고
    • Effects of dietary protein restriction on glucose and insulin metabolism in normal and diabetic humans
    • Lariviere F., Chiasson J.L., Schiffrin A., Taveroff A., Hoffer L.J. Effects of dietary protein restriction on glucose and insulin metabolism in normal and diabetic humans. Metabolism 1994, 43:462-467.
    • (1994) Metabolism , vol.43 , pp. 462-467
    • Lariviere, F.1    Chiasson, J.L.2    Schiffrin, A.3    Taveroff, A.4    Hoffer, L.J.5
  • 84
    • 70350417158 scopus 로고    scopus 로고
    • Akt2 is required for hepatic lipid accumulation in models of insulin resistance
    • Leavens K.F., Easton R.M., Shulman G.I., Previs S.F., Birnbaum M.J. Akt2 is required for hepatic lipid accumulation in models of insulin resistance. Cell Metab. 2009, 10:405-418.
    • (2009) Cell Metab. , vol.10 , pp. 405-418
    • Leavens, K.F.1    Easton, R.M.2    Shulman, G.I.3    Previs, S.F.4    Birnbaum, M.J.5
  • 85
    • 64749109224 scopus 로고    scopus 로고
    • Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation
    • Lee Y.H., Stallcup M.R. Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation. Mol. Endocrinol. 2009, 23:425-433.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 425-433
    • Lee, Y.H.1    Stallcup, M.R.2
  • 86
    • 0028890361 scopus 로고
    • Interaction of thyroid-hormone receptor with a conserved transcriptional mediator
    • Lee J.W., Ryan F., Swaffield J.C., Johnston S.A., Moore D.D. Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 1995, 374:91-94.
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.D.5
  • 88
    • 0028064656 scopus 로고
    • Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver
    • Lemaigre F.P., Rousseau G.G. Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver. Biochem. J. 1994, 303(Pt 1):1-14.
    • (1994) Biochem. J. , vol.303 , Issue.PART 1 , pp. 1-14
    • Lemaigre, F.P.1    Rousseau, G.G.2
  • 91
    • 33744534726 scopus 로고    scopus 로고
    • GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha
    • Lerin C., Rodgers J.T., Kalume D.E., Kim S.H., Pandey A., Puigserver P. GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha. Cell Metab. 2006, 3:429-438.
    • (2006) Cell Metab. , vol.3 , pp. 429-438
    • Lerin, C.1    Rodgers, J.T.2    Kalume, D.E.3    Kim, S.H.4    Pandey, A.5    Puigserver, P.6
  • 92
    • 0036217052 scopus 로고    scopus 로고
    • Disordered fat storage and mobilization in the pathogenesis of insulin resistance and type 2 diabetes
    • Lewis G.F., Carpentier A., Adeli K., Giacca A. Disordered fat storage and mobilization in the pathogenesis of insulin resistance and type 2 diabetes. Endocr. Rev. 2002, 23:201-229.
    • (2002) Endocr. Rev. , vol.23 , pp. 201-229
    • Lewis, G.F.1    Carpentier, A.2    Adeli, K.3    Giacca, A.4
  • 93
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3
    • Li J., Wang J., Nawaz Z., Liu J.M., Qin J., Wong J. Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3. EMBO J. 2000, 19:4342-4350.
    • (2000) EMBO J. , vol.19 , pp. 4342-4350
    • Li, J.1    Wang, J.2    Nawaz, Z.3    Liu, J.M.4    Qin, J.5    Wong, J.6
  • 94
    • 48349108293 scopus 로고    scopus 로고
    • Genome-wide coactivation analysis of PGC-1alpha identifies BAF60a as a regulator of hepatic lipid metabolism
    • Li S., Liu C., Li N., Hao T., Han T., Hill D.E., Vidal M., Lin J.D. Genome-wide coactivation analysis of PGC-1alpha identifies BAF60a as a regulator of hepatic lipid metabolism. Cell Metab. 2008, 8:105-117.
    • (2008) Cell Metab. , vol.8 , pp. 105-117
    • Li, S.1    Liu, C.2    Li, N.3    Hao, T.4    Han, T.5    Hill, D.E.6    Vidal, M.7    Lin, J.D.8
  • 95
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • Lin W.J., Gary J.D., Yang M.C., Clarke S., Herschman H.R. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J. Biol. Chem. 1996, 271:15034-15044.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 98
    • 0029798289 scopus 로고    scopus 로고
    • Effect of dietary protein intake on insulin secretion and glucose metabolism in insulin-dependent diabetes mellitus
    • Linn T., Geyer R., Prassek S., Laube H. Effect of dietary protein intake on insulin secretion and glucose metabolism in insulin-dependent diabetes mellitus. J. Clin. Endocrinol. Metab. 1996, 81:3938-3943.
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 3938-3943
    • Linn, T.1    Geyer, R.2    Prassek, S.3    Laube, H.4
  • 100
    • 0035213822 scopus 로고    scopus 로고
    • DAX-1 represses the high-density lipoprotein receptor through interaction with positive regulators sterol regulatory element-binding protein-1a and steroidogenic factor-1
    • Lopez D., Shea-Eaton W., Sanchez M.D., McLean M.P. DAX-1 represses the high-density lipoprotein receptor through interaction with positive regulators sterol regulatory element-binding protein-1a and steroidogenic factor-1. Endocrinology 2001, 142:5097-5106.
    • (2001) Endocrinology , vol.142 , pp. 5097-5106
    • Lopez, D.1    Shea-Eaton, W.2    Sanchez, M.D.3    McLean, M.P.4
  • 101
    • 34447122582 scopus 로고    scopus 로고
    • Critical role for transcription coactivator peroxisome proliferator-activated receptor (PPAR)-binding protein/TRAP220 in liver regeneration and PPARalpha ligand-induced liver tumor development
    • Matsumoto K., Yu S., Jia Y., Ahmed M.R., Viswakarma N., Sarkar J., Kashireddy P.V., Rao M.S., Karpus W., Gonzalez F.J., Reddy J.K. Critical role for transcription coactivator peroxisome proliferator-activated receptor (PPAR)-binding protein/TRAP220 in liver regeneration and PPARalpha ligand-induced liver tumor development. J. Biol. Chem. 2007, 282:17053-17060.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17053-17060
    • Matsumoto, K.1    Yu, S.2    Jia, Y.3    Ahmed, M.R.4    Viswakarma, N.5    Sarkar, J.6    Kashireddy, P.V.7    Rao, M.S.8    Karpus, W.9    Gonzalez, F.J.10    Reddy, J.K.11
  • 102
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna N.J., O'Malley B.W. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 2002, 108:465-474.
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 103
    • 33646141371 scopus 로고    scopus 로고
    • The Tgif2 gene contains a retained intron within the coding sequence
    • Melhuish T.A., Wotton D. The Tgif2 gene contains a retained intron within the coding sequence. BMC Mol. Biol. 2006, 7:2.
    • (2006) BMC Mol. Biol. , vol.7 , pp. 2
    • Melhuish, T.A.1    Wotton, D.2
  • 104
    • 0035943703 scopus 로고    scopus 로고
    • TGIF2 interacts with histone deacetylase 1 and represses transcription
    • Melhuish T.A., Gallo C.M., Wotton D. TGIF2 interacts with histone deacetylase 1 and represses transcription. J. Biol. Chem. 2001, 276:32109-32114.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32109-32114
    • Melhuish, T.A.1    Gallo, C.M.2    Wotton, D.3
  • 105
    • 77957262197 scopus 로고    scopus 로고
    • Tgif1 represses apolipoprotein gene expression in liver
    • Melhuish T.A., Chung D.D., Bjerke G.A., Wotton D. Tgif1 represses apolipoprotein gene expression in liver. J. Cell. Biochem. 2010, 111(2):380-390.
    • (2010) J. Cell. Biochem. , vol.111 , Issue.2 , pp. 380-390
    • Melhuish, T.A.1    Chung, D.D.2    Bjerke, G.A.3    Wotton, D.4
  • 106
    • 0033636523 scopus 로고    scopus 로고
    • Loss of insulin signaling in hepatocytes leads to severe insulin resistance and progressive hepatic dysfunction
    • Michael M.D., Kulkarni R.N., Postic C., Previs S.F., Shulman G.I., Magnuson M.A., Kahn C.R. Loss of insulin signaling in hepatocytes leads to severe insulin resistance and progressive hepatic dysfunction. Mol. Cell 2000, 6:87-97.
    • (2000) Mol. Cell , vol.6 , pp. 87-97
    • Michael, M.D.1    Kulkarni, R.N.2    Postic, C.3    Previs, S.F.4    Shulman, G.I.5    Magnuson, M.A.6    Kahn, C.R.7
  • 107
    • 0035857020 scopus 로고    scopus 로고
    • New drug targets for type 2 diabetes and the metabolic syndrome
    • Moller D.E. New drug targets for type 2 diabetes and the metabolic syndrome. Nature 2001, 414:821-827.
    • (2001) Nature , vol.414 , pp. 821-827
    • Moller, D.E.1
  • 108
    • 70350463602 scopus 로고    scopus 로고
    • DAX-1 acts as a novel corepressor of orphan nuclear receptor HNF4alpha and negatively regulates gluconeogenic enzyme gene expression
    • Nedumaran B., Hong S., Xie Y.B., Kim Y.H., Seo W.Y., Lee M.W., Lee C.H., Koo S.H., Choi H.S. DAX-1 acts as a novel corepressor of orphan nuclear receptor HNF4alpha and negatively regulates gluconeogenic enzyme gene expression. J. Biol. Chem. 2009, 284:27511-27523.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27511-27523
    • Nedumaran, B.1    Hong, S.2    Xie, Y.B.3    Kim, Y.H.4    Seo, W.Y.5    Lee, M.W.6    Lee, C.H.7    Koo, S.H.8    Choi, H.S.9
  • 109
    • 77950589655 scopus 로고    scopus 로고
    • Orphan nuclear receptor DAX-1 acts as a novel corepressor of liver X receptor alpha and inhibits hepatic lipogenesis
    • Nedumaran B., Kim G.S., Hong S., Yoon Y.S., Kim Y.H., Lee C.H., Lee Y.C., Koo S.H., Choi H.S. Orphan nuclear receptor DAX-1 acts as a novel corepressor of liver X receptor alpha and inhibits hepatic lipogenesis. J. Biol. Chem. 2010, 285:9221-9232.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9221-9232
    • Nedumaran, B.1    Kim, G.S.2    Hong, S.3    Yoon, Y.S.4    Kim, Y.H.5    Lee, C.H.6    Lee, Y.C.7    Koo, S.H.8    Choi, H.S.9
  • 111
    • 33748742725 scopus 로고    scopus 로고
    • Inhibition of hepatocyte nuclear factor 4 transcriptional activity by the nuclear factor kappaB pathway
    • Nikolaidou-Neokosmidou V., Zannis V.I., Kardassis D. Inhibition of hepatocyte nuclear factor 4 transcriptional activity by the nuclear factor kappaB pathway. Biochem. J. 2006, 398:439-450.
    • (2006) Biochem. J. , vol.398 , pp. 439-450
    • Nikolaidou-Neokosmidou, V.1    Zannis, V.I.2    Kardassis, D.3
  • 113
  • 114
    • 0025826137 scopus 로고
    • Regulation of gene expression by insulin
    • O'Brien R.M., Granner D.K. Regulation of gene expression by insulin. Biochem. J. 1991, 278(Pt 3):609-619.
    • (1991) Biochem. J. , vol.278 , Issue.PART 3 , pp. 609-619
    • O'Brien, R.M.1    Granner, D.K.2
  • 115
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 1996, 87:953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 116
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate S.A., Tsai S.Y., Tsai M.J., O'Malley B.W. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 1995, 270:1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 117
    • 74549167737 scopus 로고    scopus 로고
    • Dietary and genetic obesity promote liver inflammation and tumorigenesis by enhancing IL-6 and TNF expression
    • Park E.J., Lee J.H., Yu G.Y., He G., Ali S.R., Holzer R.G., Osterreicher C.H., Takahashi H., Karin M. Dietary and genetic obesity promote liver inflammation and tumorigenesis by enhancing IL-6 and TNF expression. Cell 2010, 140:197-208.
    • (2010) Cell , vol.140 , pp. 197-208
    • Park, E.J.1    Lee, J.H.2    Yu, G.Y.3    He, G.4    Ali, S.R.5    Holzer, R.G.6    Osterreicher, C.H.7    Takahashi, H.8    Karin, M.9
  • 119
    • 0026520193 scopus 로고
    • Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis
    • Pilkis S.J., Granner D.K. Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis. Annu. Rev. Physiol. 1992, 54:885-909.
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 885-909
    • Pilkis, S.J.1    Granner, D.K.2
  • 120
    • 0037326196 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator
    • Puigserver P., Spiegelman B.M. Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator. Endocr. Rev. 2003, 24:78-90.
    • (2003) Endocr. Rev. , vol.24 , pp. 78-90
    • Puigserver, P.1    Spiegelman, B.M.2
  • 121
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • Puigserver P., Wu Z., Park C.W., Graves R., Wright M., Spiegelman B.M. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 1998, 92:829-839.
    • (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
  • 125
    • 37349110355 scopus 로고    scopus 로고
    • Metabolic adaptations through the PGC-1 alpha and SIRT1 pathways
    • Rodgers J.T., Lerin C., Gerhart-Hines Z., Puigserver P. Metabolic adaptations through the PGC-1 alpha and SIRT1 pathways. FEBS Lett. 2008, 582:46-53.
    • (2008) FEBS Lett. , vol.582 , pp. 46-53
    • Rodgers, J.T.1    Lerin, C.2    Gerhart-Hines, Z.3    Puigserver, P.4
  • 126
    • 0035813090 scopus 로고    scopus 로고
    • Coregulator codes of transcriptional regulation by nuclear receptors
    • Rosenfeld M.G., Glass C.K. Coregulator codes of transcriptional regulation by nuclear receptors. J. Biol. Chem. 2001, 276:36865-36868.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36865-36868
    • Rosenfeld, M.G.1    Glass, C.K.2
  • 127
    • 0033982643 scopus 로고    scopus 로고
    • The hypothalamic-pituitary-adrenal axis activity as a predictor of cardiovascular disease, type 2 diabetes and stroke
    • Rosmond R., Bjorntorp P. The hypothalamic-pituitary-adrenal axis activity as a predictor of cardiovascular disease, type 2 diabetes and stroke. J. Intern. Med. 2000, 247:188-197.
    • (2000) J. Intern. Med. , vol.247 , pp. 188-197
    • Rosmond, R.1    Bjorntorp, P.2
  • 128
    • 0024446159 scopus 로고
    • Effect of dietary protein on in vivo insulin action and liver glycogen repletion
    • Rossetti L., Rothman D.L., DeFronzo R.A., Shulman G.I. Effect of dietary protein on in vivo insulin action and liver glycogen repletion. Am. J. Physiol. 1989, 257:E212-E219.
    • (1989) Am. J. Physiol. , vol.257
    • Rossetti, L.1    Rothman, D.L.2    DeFronzo, R.A.3    Shulman, G.I.4
  • 129
    • 0035936763 scopus 로고    scopus 로고
    • New perspectives into the molecular pathogenesis and treatment of type 2 diabetes
    • Saltiel A.R. New perspectives into the molecular pathogenesis and treatment of type 2 diabetes. Cell 2001, 104:517-529.
    • (2001) Cell , vol.104 , pp. 517-529
    • Saltiel, A.R.1
  • 130
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel A.R., Kahn C.R. Insulin signalling and the regulation of glucose and lipid metabolism. Nature 2001, 414:799-806.
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 131
    • 0027290847 scopus 로고
    • Use of bismannose photolabel to elucidate insulin-regulated GLUT4 subcellular trafficking kinetics in rat adipose cells. Evidence that exocytosis is a critical site of hormone action
    • Satoh S., Nishimura H., Clark A.E., Kozka I.J., Vannucci S.J., Simpson I.A., Quon M.J., Cushman S.W., Holman G.D. Use of bismannose photolabel to elucidate insulin-regulated GLUT4 subcellular trafficking kinetics in rat adipose cells. Evidence that exocytosis is a critical site of hormone action. J. Biol. Chem. 1993, 268:17820-17829.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17820-17829
    • Satoh, S.1    Nishimura, H.2    Clark, A.E.3    Kozka, I.J.4    Vannucci, S.J.5    Simpson, I.A.6    Quon, M.J.7    Cushman, S.W.8    Holman, G.D.9
  • 132
    • 0037216466 scopus 로고    scopus 로고
    • Hepatic de novo lipogenesis in normoinsulinemic and hyperinsulinemic subjects consuming high-fat, low-carbohydrate and low-fat, high-carbohydrate isoenergetic diets
    • Schwarz J.M., Linfoot P., Dare D., Aghajanian K. Hepatic de novo lipogenesis in normoinsulinemic and hyperinsulinemic subjects consuming high-fat, low-carbohydrate and low-fat, high-carbohydrate isoenergetic diets. Am. J. Clin. Nutr. 2003, 77:43-50.
    • (2003) Am. J. Clin. Nutr. , vol.77 , pp. 43-50
    • Schwarz, J.M.1    Linfoot, P.2    Dare, D.3    Aghajanian, K.4
  • 134
    • 0027454103 scopus 로고
    • Correlation of diacylglycerol level and protein kinase C activity in rat retina to retinal circulation
    • Shiba T., Inoguchi T., Sportsman J.R., Heath W.F., Bursell S., King G.L. Correlation of diacylglycerol level and protein kinase C activity in rat retina to retinal circulation. Am. J. Physiol. 1993, 265:E783-E793.
    • (1993) Am. J. Physiol. , vol.265
    • Shiba, T.1    Inoguchi, T.2    Sportsman, J.R.3    Heath, W.F.4    Bursell, S.5    King, G.L.6
  • 135
    • 0033927667 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance
    • Shulman G.I. Cellular mechanisms of insulin resistance. J. Clin. Invest. 2000, 106:171-176.
    • (2000) J. Clin. Invest. , vol.106 , pp. 171-176
    • Shulman, G.I.1
  • 136
    • 65649131624 scopus 로고    scopus 로고
    • Molecular determinants of the interactions between LXR/RXR heterodimers and TRAP220
    • Son Y.L., Lee Y.C. Molecular determinants of the interactions between LXR/RXR heterodimers and TRAP220. Biochem. Biophys. Res. Commun. 2009, 384:389-393.
    • (2009) Biochem. Biophys. Res. Commun. , vol.384 , pp. 389-393
    • Son, Y.L.1    Lee, Y.C.2
  • 137
    • 5444264003 scopus 로고    scopus 로고
    • Biological control through regulated transcriptional coactivators
    • Spiegelman B.M., Heinrich R. Biological control through regulated transcriptional coactivators. Cell 2004, 119:157-167.
    • (2004) Cell , vol.119 , pp. 157-167
    • Spiegelman, B.M.1    Heinrich, R.2
  • 138
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner D.E., Berger S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 2000, 64:435-459.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 140
    • 0019498093 scopus 로고
    • Glucagon and the A cell: physiology and pathophysiology (second of two parts)
    • Unger R.H., Orci L. Glucagon and the A cell: physiology and pathophysiology (second of two parts). N. Engl. J. Med. 1981, 304:1575-1580.
    • (1981) N. Engl. J. Med. , vol.304 , pp. 1575-1580
    • Unger, R.H.1    Orci, L.2
  • 142
    • 0028567884 scopus 로고
    • Transgenic mice overexpressing phosphoenolpyruvate carboxykinase develop non-insulin-dependent diabetes mellitus
    • Valera A., Pujol A., Pelegrin M., Bosch F. Transgenic mice overexpressing phosphoenolpyruvate carboxykinase develop non-insulin-dependent diabetes mellitus. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:9151-9154.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9151-9154
    • Valera, A.1    Pujol, A.2    Pelegrin, M.3    Bosch, F.4
  • 145
    • 67749135249 scopus 로고    scopus 로고
    • The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis
    • Wang Y., Vera L., Fischer W.H., Montminy M. The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis. Nature 2009, 460:534-537.
    • (2009) Nature , vol.460 , pp. 534-537
    • Wang, Y.1    Vera, L.2    Fischer, W.H.3    Montminy, M.4
  • 146
    • 0026641776 scopus 로고
    • Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection
    • Winston F., Carlson M. Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection. Trends Genet. 1992, 8:387-391.
    • (1992) Trends Genet. , vol.8 , pp. 387-391
    • Winston, F.1    Carlson, M.2
  • 147
    • 0029997378 scopus 로고    scopus 로고
    • Targeting chromatin disruption: transcription regulators that acetylate histones
    • Wolffe A.P., Pruss D. Targeting chromatin disruption: transcription regulators that acetylate histones. Cell 1996, 84:817-819.
    • (1996) Cell , vol.84 , pp. 817-819
    • Wolffe, A.P.1    Pruss, D.2
  • 148
    • 32444451567 scopus 로고    scopus 로고
    • Coactivation of Foxa2 through Pgc-1beta promotes liver fatty acid oxidation and triglyceride/VLDL secretion
    • Wolfrum C., Stoffel M. Coactivation of Foxa2 through Pgc-1beta promotes liver fatty acid oxidation and triglyceride/VLDL secretion. Cell Metab. 2006, 3:99-110.
    • (2006) Cell Metab. , vol.3 , pp. 99-110
    • Wolfrum, C.1    Stoffel, M.2
  • 149
    • 0033601272 scopus 로고    scopus 로고
    • Multiple modes of repression by the Smad transcriptional corepressor TGIF
    • Wotton D., Lo R.S., Swaby L.A., Massague J. Multiple modes of repression by the Smad transcriptional corepressor TGIF. J. Biol. Chem. 1999, 274:37105-37110.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37105-37110
    • Wotton, D.1    Lo, R.S.2    Swaby, L.A.3    Massague, J.4
  • 150
    • 0042334873 scopus 로고    scopus 로고
    • Review of the in vivo functions of the p160 steroid receptor coactivator family
    • Xu J., Li Q. Review of the in vivo functions of the p160 steroid receptor coactivator family. Mol. Endocrinol. 2003, 17:1681-1692.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1681-1692
    • Xu, J.1    Li, Q.2
  • 151
    • 0036744821 scopus 로고    scopus 로고
    • Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function
    • Xu J., O'Malley B.W. Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function. Rev. Endocr. Metab. Disord. 2002, 3:185-192.
    • (2002) Rev. Endocr. Metab. Disord. , vol.3 , pp. 185-192
    • Xu, J.1    O'Malley, B.W.2
  • 152
    • 34347250130 scopus 로고    scopus 로고
    • Nuclear corepressor is required for inhibition of phosphoenolpyruvate carboxykinase expression by tumor necrosis factor-alpha
    • Yan J., Gao Z., Yu G., He Q., Weng J., Ye J. Nuclear corepressor is required for inhibition of phosphoenolpyruvate carboxykinase expression by tumor necrosis factor-alpha. Mol. Endocrinol. 2007, 21:1630-1641.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 1630-1641
    • Yan, J.1    Gao, Z.2    Yu, G.3    He, Q.4    Weng, J.5    Ye, J.6
  • 153
    • 76549115542 scopus 로고    scopus 로고
    • Exchange of a nuclear corepressor between NF-kappaB and CREB mediates inhibition of phosphoenolpyruvate carboxykinase transcription by NF-kappaB
    • Yan J.H., Gao Z.G., Ye J.P., Weng J.P. Exchange of a nuclear corepressor between NF-kappaB and CREB mediates inhibition of phosphoenolpyruvate carboxykinase transcription by NF-kappaB. Chin. Med. J. (Engl.) 2010, 123:221-226.
    • (2010) Chin. Med. J. (Engl.) , vol.123 , pp. 221-226
    • Yan, J.H.1    Gao, Z.G.2    Ye, J.P.3    Weng, J.P.4
  • 156
    • 33644552474 scopus 로고    scopus 로고
    • C/EBPalpha and HNF6 protein complex formation stimulates HNF6-dependent transcription by CBP coactivator recruitment in HepG2 cells
    • Yoshida Y., Hughes D.E., Rausa F.M., Kim I.M., Tan Y., Darlington G.J., Costa R.H. C/EBPalpha and HNF6 protein complex formation stimulates HNF6-dependent transcription by CBP coactivator recruitment in HepG2 cells. Hepatology 2006, 43:276-286.
    • (2006) Hepatology , vol.43 , pp. 276-286
    • Yoshida, Y.1    Hughes, D.E.2    Rausa, F.M.3    Kim, I.M.4    Tan, Y.5    Darlington, G.J.6    Costa, R.H.7
  • 157
    • 77954832705 scopus 로고    scopus 로고
    • The interaction between nuclear receptor corepressor and histone deacetylase 3 regulates both positive and negative thyroid hormone action in vivo
    • You S.H., Liao X., Weiss R.E., Lazar M.A. The interaction between nuclear receptor corepressor and histone deacetylase 3 regulates both positive and negative thyroid hormone action in vivo. Mol. Endocrinol. 2010, 24(7):1359-1367.
    • (2010) Mol. Endocrinol. , vol.24 , Issue.7 , pp. 1359-1367
    • You, S.H.1    Liao, X.2    Weiss, R.E.3    Lazar, M.A.4
  • 158
    • 0030020697 scopus 로고    scopus 로고
    • Role of insulin in hepatic fatty acid partitioning: emerging concepts
    • Zammit V.A. Role of insulin in hepatic fatty acid partitioning: emerging concepts. Biochem. J. 1996, 314(Pt 1):1-14.
    • (1996) Biochem. J. , vol.314 , Issue.PART 1 , pp. 1-14
    • Zammit, V.A.1
  • 159
    • 0028024329 scopus 로고
    • Monitoring the partitioning of hepatic fatty acids in vivo: keeping track of control
    • Zammit V.A., Moir A.M. Monitoring the partitioning of hepatic fatty acids in vivo: keeping track of control. Trends Biochem. Sci. 1994, 19:313-317.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 313-317
    • Zammit, V.A.1    Moir, A.M.2
  • 160
    • 25144482864 scopus 로고    scopus 로고
    • Foxa2 integrates the transcriptional response of the hepatocyte to fasting
    • Zhang L., Rubins N.E., Ahima R.S., Greenbaum L.E., Kaestner K.H. Foxa2 integrates the transcriptional response of the hepatocyte to fasting. Cell Metab. 2005, 2:141-148.
    • (2005) Cell Metab. , vol.2 , pp. 141-148
    • Zhang, L.1    Rubins, N.E.2    Ahima, R.S.3    Greenbaum, L.E.4    Kaestner, K.H.5
  • 161
    • 33845984572 scopus 로고    scopus 로고
    • Aberrant hepatic expression of PPARgamma2 stimulates hepatic lipogenesis in a mouse model of obesity, insulin resistance, dyslipidemia, and hepatic steatosis
    • Zhang Y.L., Hernandez-Ono A., Siri P., Weisberg S., Conlon D., Graham M.J., Crooke R.M., Huang L.S., Ginsberg H.N. Aberrant hepatic expression of PPARgamma2 stimulates hepatic lipogenesis in a mouse model of obesity, insulin resistance, dyslipidemia, and hepatic steatosis. J. Biol. Chem. 2006, 281:37603-37615.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37603-37615
    • Zhang, Y.L.1    Hernandez-Ono, A.2    Siri, P.3    Weisberg, S.4    Conlon, D.5    Graham, M.J.6    Crooke, R.M.7    Huang, L.S.8    Ginsberg, H.N.9
  • 163
    • 0030771856 scopus 로고    scopus 로고
    • Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor
    • Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K. Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor. J. Biol. Chem. 1997, 272:25500-25506.
    • (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


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