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Volumn 2012, Issue , 2012, Pages

Role of transcription factor modifications in the pathogenesis of insulin resistance

Author keywords

[No Author keywords available]

Indexed keywords

ADIPOCYTOKINE; CASEIN KINASE I; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE 1; N ACETYLGLUCOSAMINE; SIRTUIN 1; STEROL REGULATORY ELEMENT BINDING PROTEIN 1C; STRESS ACTIVATED PROTEIN KINASE 1; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR SP1; UBIQUITIN; DNA; FATTY ACID; TRANSCRIPTION FACTOR;

EID: 84855176031     PISSN: 16875214     EISSN: 16875303     Source Type: Journal    
DOI: 10.1155/2012/716425     Document Type: Review
Times cited : (20)

References (196)
  • 1
    • 0020474084 scopus 로고
    • Variety in the level of gene control in eukaryotic cells
    • Darnell J. E. Jr., Variety in the level of gene control in eukaryotic cells Nature 1982 297 5865 365 371
    • (1982) Nature , vol.297 , Issue.5865 , pp. 365-371
    • Darnell Jr., J.E.1
  • 2
    • 0021099154 scopus 로고
    • Very short repeats and coordinate induction of genes
    • Davidson E. H., Jacobs H. T., Britten R. J., Very short repeats and coordinate induction of genes Nature 1983 301 5900 468 470
    • (1983) Nature , vol.301 , Issue.5900 , pp. 468-470
    • Davidson, E.H.1    Jacobs, H.T.2    Britten, R.J.3
  • 3
    • 0025900438 scopus 로고
    • In situ distinction between steroid receptor binding and transactivation at a target gene
    • McDonnell D. P., Nawaz Z., O'Malley B. W., In situ distinction between steroid receptor binding and transactivation at a target gene Molecular and Cellular Biology 1991 11 9 4350 4355 (Pubitemid 21895828)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.9 , pp. 4350-4355
    • McDonnell, D.P.1    Nawaz, Z.2    O'Malley, B.W.3
  • 5
    • 34147112806 scopus 로고    scopus 로고
    • Regulation of SRC family coactivators by post-translational modifications
    • DOI 10.1016/j.cellsig.2007.02.002, PII S0898656807000484
    • Li S., Shang Y., Regulation of SRC family coactivators by post-translational modifications Cellular Signalling 2007 19 6 1101 1112 (Pubitemid 46561570)
    • (2007) Cellular Signalling , vol.19 , Issue.6 , pp. 1101-1112
    • Li, S.1    Shang, Y.2
  • 6
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • DOI 10.1038/414782a
    • Zimmet P., Alberti K. G. M. M., Shaw J., Global and societal implications of the diabetes epidemic Nature 2001 414 6865 782 787 (Pubitemid 34000780)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.M.M.2    Shaw, J.3
  • 7
    • 0026110135 scopus 로고
    • Banting lecture 1990. -cells in type II diabetes mellitus
    • Porte D. Jr., Banting lecture 1990. -cells in type II diabetes mellitus Diabetes 1991 40 2 166 180
    • (1991) Diabetes , vol.40 , Issue.2 , pp. 166-180
    • Porte Jr., D.1
  • 8
    • 0027953703 scopus 로고
    • Banting lecture: Insulin action, diabetogenes, and the cause of type II diabetes
    • Kahn C. R., Banting lecture: insulin action, diabetogenes, and the cause of type II diabetes Diabetes 1994 43 8 1066 1084 (Pubitemid 24230714)
    • (1994) Diabetes , vol.43 , Issue.8 , pp. 1066-1084
    • Kahn, C.R.1
  • 9
    • 0029037649 scopus 로고
    • Pathophysiology of insulin resistance in human disease
    • Reaven G. M., Pathophysiology of insulin resistance in human disease Physiological Reviews 1995 75 3 473 486
    • (1995) Physiological Reviews , vol.75 , Issue.3 , pp. 473-486
    • Reaven, G.M.1
  • 10
    • 39749147110 scopus 로고    scopus 로고
    • Mechanisms of disease: Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes
    • DOI 10.1038/nrm2327, PII NRM2327
    • Muoio D. M., Newgard C. B., Mechanisms of disease: molecular and metabolic mechanisms of insulin resistance and -cell failure in type 2 diabetes Nature Reviews Molecular Cell Biology 2008 9 3 193 205 (Pubitemid 351301824)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.3 , pp. 193-205
    • Muoio, D.M.1    Newgard, C.B.2
  • 11
    • 41949114990 scopus 로고    scopus 로고
    • Role of mitochondrial dysfunction in insulin resistance
    • DOI 10.1161/CIRCRESAHA.107.165472, PII 0000301220080229000005
    • Kim J. A., Wei Y., Sowers J. R., Role of mitochondrial dysfunction in insulin resistance Circulation Research 2008 102 4 401 414 (Pubitemid 351651099)
    • (2008) Circulation Research , vol.102 , Issue.4 , pp. 401-414
    • Kim, J.-A.1    Wei, Y.2    Sowers, J.R.3
  • 12
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • DOI 10.1210/er.2007-0015
    • Eizirik D. L., Cardozo A. K., Cnop M., The role for endoplasmic reticulum stress in diabetes mellitus Endocrine Reviews 2008 29 1 42 61 (Pubitemid 351252746)
    • (2008) Endocrine Reviews , vol.29 , Issue.1 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 15
    • 13244287966 scopus 로고    scopus 로고
    • Regulation of FoxO activity by CBP/p300-mediated acetylation
    • DOI 10.1016/j.tibs.2004.12.002, PII S0968000404003019
    • van der Heide L. P., Smidt M. P., Regulation of FoxO activity by CBP/p300-mediated acetylation Trends in Biochemical Sciences 2005 30 2 81 86 (Pubitemid 40187300)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.2 , pp. 81-86
    • Van Der Heide, L.P.1    Smidt, M.P.2
  • 16
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter T., Karin M., The regulation of transcription by phosphorylation Cell 1992 70 3 375 387
    • (1992) Cell , vol.70 , Issue.3 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 17
    • 0033845842 scopus 로고    scopus 로고
    • Regulation of transcription factor function by phosphorylation
    • Whitmarsh A. J., Davis R. J., Regulation of transcription factor function by phosphorylation Cellular and Molecular Life Sciences 2000 57 8-9 1172 1183 (Pubitemid 30663475)
    • (2000) Cellular and Molecular Life Sciences , vol.57 , Issue.8-9 , pp. 1172-1183
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 18
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
    • DOI 10.1038/nature05815, PII NATURE05815
    • Hart G. W., Housley M. P., Slawson C., Cycling of O-linked -N-acetylglucosamine on nucleocytoplasmic proteins Nature 2007 446 7139 1017 1022 (Pubitemid 46676063)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 20
    • 0037442984 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase
    • DOI 10.1242/jcs.00246
    • Love D. C., Kochran J., Cathey R. L., Shin S. H., Hanover J. A., Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase Journal of Cell Science 2003 116, part 4 647 654 (Pubitemid 36231303)
    • (2003) Journal of Cell Science , vol.116 , Issue.4 , pp. 647-654
    • Love, D.C.1    Kochran, J.2    Cathey, R.L.3    Shin, S.-H.4    Hanover, J.A.5
  • 21
    • 55649110871 scopus 로고    scopus 로고
    • O-GlcNAc modification of transcription factors, glucose sensing and glucotoxicity
    • Issad T., Kuo M., O-GlcNAc modification of transcription factors, glucose sensing and glucotoxicity Trends in Endocrinology and Metabolism 2008 19 10 380 389
    • (2008) Trends in Endocrinology and Metabolism , vol.19 , Issue.10 , pp. 380-389
    • Issad, T.1    Kuo, M.2
  • 23
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • DOI 10.1126/science.1067466
    • Conaway R. C., Brower C. S., Conaway J. W., Emerging roles of ubiquitin in transcription regulation Science 2002 296 5571 1254 1258 (Pubitemid 34522769)
    • (2002) Science , vol.296 , Issue.5571 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 24
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman M. H., Ciechanover A., The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiological Reviews 2002 82 2 373 428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 25
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • DOI 10.1038/nrm1049
    • Muratani M., Tansey W. P., How the ubiquitin-proteasome system controls transcription Nature Reviews Molecular Cell Biology 2003 4 3 192 201 (Pubitemid 36288041)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 26
    • 24344445216 scopus 로고    scopus 로고
    • Something about SUMO inhibits transcription
    • DOI 10.1016/j.gde.2005.07.004, PII S0959437X05001309
    • Gill G., Something about SUMO inhibits transcription Current Opinion in Genetics and Development 2005 15 5 536 541 (Pubitemid 41262410)
    • (2005) Current Opinion in Genetics and Development , vol.15 , Issue.5 SPEC. ISS. , pp. 536-541
    • Gill, G.1
  • 27
    • 0037382641 scopus 로고    scopus 로고
    • Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity
    • DOI 10.1016/S0959-437X(03)00021-2
    • Gill G., Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity Current Opinion in Genetics and Development 2003 13 2 108 113 (Pubitemid 36369733)
    • (2003) Current Opinion in Genetics and Development , vol.13 , Issue.2 , pp. 108-113
    • Gill, G.1
  • 28
    • 0041837510 scopus 로고    scopus 로고
    • Nuclear and unclear functions of sumo
    • DOI 10.1038/nrm1200
    • Seeler J. S., Dejean A., Nuclear and unclear functions of SUMO Nature Reviews Molecular Cell Biology 2003 4 9 690 699 (Pubitemid 37082184)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.9 , pp. 690-699
    • Seeler, J.-S.1    Dejean, A.2
  • 29
    • 0035945243 scopus 로고    scopus 로고
    • Transcription factor Sp3 is regulated by acetylation
    • Braun H., Koop R., Ertmer A., Nacht S., Suske G., Transcription factor Sp3 is regulated by acetylation Nucleic Acids Research 2001 29 24 4994 5000 (Pubitemid 34065414)
    • (2001) Nucleic Acids Research , vol.29 , Issue.24 , pp. 4994-5000
    • Braun, H.1    Koop, R.2    Ertmer, A.3    Nacht, S.4    Suske, G.5
  • 30
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of i B inhibits NF- B activation
    • Desterro J. M. P., Rodriguez M. S., Hay R. T., SUMO-1 modification of I B inhibits NF- B activation Molecular Cell 1998 2 2 233 239
    • (1998) Molecular Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 31
    • 22744459667 scopus 로고    scopus 로고
    • Is insulin signaling molecules misguided in diabetes for ubiquitin-proteasome mediated degradation?
    • DOI 10.1007/s11010-005-1083-y
    • Balasubramanyam M., Sampathkumar R., Mohan V., Is insulin signaling molecules misguided in diabetes for ubiquitin-proteasome mediated degradation? Molecular and Cellular Biochemistry 2005 275 1-2 117 125 (Pubitemid 41030987)
    • (2005) Molecular and Cellular Biochemistry , vol.275 , Issue.1-2 , pp. 117-125
    • Balasubramanyam, M.1    Sampathkumar, R.2    Mohan, V.3
  • 32
    • 0032769911 scopus 로고    scopus 로고
    • Insulin regulates expression of metabolic genes through divergent signaling pathways
    • Hall R. K., Granner D. K., Insulin regulates expression of metabolic genes through divergent signaling pathways Journal of Basic and Clinical Physiology and Pharmacology 1999 10 2 119 133 (Pubitemid 29387586)
    • (1999) Journal of Basic and Clinical Physiology and Pharmacology , vol.10 , Issue.2 , pp. 119-133
    • Hall, R.K.1    Granner, D.K.2
  • 34
    • 0033522897 scopus 로고    scopus 로고
    • Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a wortmannin-sensitive pathway
    • Nakae J., Park B. C., Accili D., Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a wortmannin-sensitive pathway Journal of Biological Chemistry 1999 274 23 15982 15985
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.23 , pp. 15982-15985
    • Nakae, J.1    Park, B.C.2    Accili, D.3
  • 35
    • 25444442080 scopus 로고    scopus 로고
    • Triple layer control: Phosphorylation, acetylation and ubiquitination of FOXO proteins
    • Vogt P. K., Jiang H., Aoki M., Triple layer control: phosphorylation, acetylation and ubiquitination of FOXO proteins Cell Cycle 2005 4 7 908 913 (Pubitemid 41359756)
    • (2005) Cell Cycle , vol.4 , Issue.7 , pp. 908-913
    • Vogt, P.K.1    Jiang, H.2    Aoki, M.3
  • 36
    • 0032830572 scopus 로고    scopus 로고
    • Conservation of an insulin response unit between mouse and human glucose-6-phosphatase catalytic subunit gene promoters: Transcription factor FKHR binds the insulin response sequence
    • DOI 10.2337/diabetes.48.9.1885
    • Ayala J. E., Streeper R. S., Desgrosellier J. S., Durham S. K., Suwanichkul A., Svitek C. A., Goldman J. K., Barr F. G., Powell D. R., O'Brien R. M., Conservation of an insulin response unit between mouse and human glucose-6-phosphatase catalytic subunit gene promoters: transcription factor FKHR binds the insulin response sequence Diabetes 1999 48 9 1885 1889 (Pubitemid 29415214)
    • (1999) Diabetes , vol.48 , Issue.9 , pp. 1885-1889
    • Ayala, J.E.1    Streeper, R.S.2    Desgrosellier, J.S.3    Durham, S.K.4    Suwanichkul, A.5    Svitek, C.A.6    Goldman, J.K.7    Barr, F.G.8    Powell, D.R.9    O'Brien, R.M.10
  • 37
    • 0034806293 scopus 로고    scopus 로고
    • Differential regulation of endogenous glucose-6-phosphatase and phosphoenolpyruvate carboxykinase gene expression by the forkhead transcription factor FKHR in H4IIE-hepatoma cells
    • DOI 10.1006/bbrc.2001.5261
    • Barthel A., Schmoll D., Krger K. D., Bahrenberg G., Walther R., Roth R. A., Joost H. G., Differential regulation of endogenous glucose-6-phosphatase and phosphoenolpyruvate carboxykinase gene expression by the forkhead transcription factor FKHR in H4IIE-hepatoma cells Biochemical and Biophysical Research Communications 2001 285 4 897 902 (Pubitemid 32918020)
    • (2001) Biochemical and Biophysical Research Communications , vol.285 , Issue.4 , pp. 897-902
    • Barthel, A.1    Schmoll, D.2    Kruger, K.-D.3    Bahrenberg, G.4    Walther, R.5    Roth, R.A.6    Joost, H.-G.7
  • 38
    • 0037342151 scopus 로고    scopus 로고
    • Regulation of PGC-1 promoter activity by protein kinase B and the forkhead transcription factor FKHR
    • DOI 10.2337/diabetes.52.3.642
    • Daitoku H., Yamagata K., Matsuzaki H., Hatta M., Fukamizu A., Regulation of PGC-1 promoter activity by protein kinase B and the forkhead transcription factor FKHR Diabetes 2003 52 3 642 649 (Pubitemid 36323569)
    • (2003) Diabetes , vol.52 , Issue.3 , pp. 642-649
    • Daitoku, H.1    Yamagata, K.2    Matsuzaki, H.3    Hatta, M.4    Fukamizu, A.5
  • 39
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • Rena G., Shaodong G., Cichy S. C., Unterman T. G., Cohen P., Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B Journal of Biological Chemistry 1999 274 24 17179 17183
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.24 , pp. 17179-17183
    • Rena, G.1    Shaodong, G.2    Cichy, S.C.3    Unterman, T.G.4    Cohen, P.5
  • 40
    • 33750032892 scopus 로고    scopus 로고
    • CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage
    • DOI 10.1126/science.1130512
    • Huang H., Regan K. M., Lou Z., Chen J., Tindall D. J., CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage Science 2006 314 5797 294 297 (Pubitemid 44571973)
    • (2006) Science , vol.314 , Issue.5797 , pp. 294-297
    • Huang, H.1    Regan, K.M.2    Lou, Z.3    Chen, J.4    Tindall, D.J.5
  • 41
    • 1242276189 scopus 로고    scopus 로고
    • D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a
    • DOI 10.1038/sj.embor.7400048
    • Rena G., Bain J., Elliott M., Cohen P., D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a EMBO Reports 2004 5 1 60 65 (Pubitemid 38228529)
    • (2004) EMBO Reports , vol.5 , Issue.1 , pp. 60-65
    • Rena, G.1    Bain, J.2    Elliott, M.3    Cohen, P.4
  • 43
    • 0035868368 scopus 로고    scopus 로고
    • Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targetting
    • DOI 10.1042/0264-6021:3540605
    • Rena G., Prescott A. R., Guo S., Cohen P., Unterman T. G., Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targetting Biochemical Journal 2001 354, part 3 605 612 (Pubitemid 32269724)
    • (2001) Biochemical Journal , vol.354 , Issue.3 , pp. 605-612
    • Rena, G.1    Prescott, A.R.2    Guo, S.3    Cohen, P.4    Unterman, T.G.5
  • 44
    • 4544312844 scopus 로고    scopus 로고
    • Proteasomal degradation of the FoxO1 transcriptional regulator in cells transformed by the P3k and Akt oncoproteins
    • DOI 10.1073/pnas.0405454101
    • Aoki M., Jiang H., Vogt P. K., Proteasomal degradation of the FoxO1 transcriptional regulator in cells transformed by the P3k and Akt oncoproteins Proceedings of the National Academy of Sciences of the United States of America 2004 101 37 13613 13617 (Pubitemid 39238451)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.37 , pp. 13613-13617
    • Aoki, M.1    Jiang, H.2    Vogt, P.K.3
  • 49
    • 77956260966 scopus 로고    scopus 로고
    • Uncoupling of acetylation from phosphorylation regulates FoxO1 function independent of its subcellular localization
    • Qiang L., Banks A. S., Accili D., Uncoupling of acetylation from phosphorylation regulates FoxO1 function independent of its subcellular localization Journal of Biological Chemistry 2010 285 35 27396 27401
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.35 , pp. 27396-27401
    • Qiang, L.1    Banks, A.S.2    Accili, D.3
  • 50
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via sirt-dependent deacetylation promotes expression of glucogenetic genes
    • DOI 10.1074/jbc.M412357200
    • Frescas D., Valenti L., Accili D., Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes Journal of Biological Chemistry 2005 280 21 20589 20595 (Pubitemid 40776761)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 53
    • 39749171700 scopus 로고    scopus 로고
    • O-glycosylation of FoxO1 increases its transcriptional activity towards the glucose 6-phosphatase gene
    • Kuo M., Zilberfarb V., Gangneux N., Christeff N., Issad T., O-glycosylation of FoxO1 increases its transcriptional activity towards the glucose 6-phosphatase gene FEBS Letters 2008 582 5 829 834
    • (2008) FEBS Letters , vol.582 , Issue.5 , pp. 829-834
    • Kuo, M.1    Zilberfarb, V.2    Gangneux, N.3    Christeff, N.4    Issad, T.5
  • 54
    • 42649105106 scopus 로고    scopus 로고
    • O-GlcNAc modification of FoxO1 increases its transcriptional activity: A role in the glucotoxicity phenomenon?
    • Kuo M., Zilberfarb V., Gangneux N., Christeff N., Issad T., O-GlcNAc modification of FoxO1 increases its transcriptional activity: a role in the glucotoxicity phenomenon? Biochimie 2008 90 5 679 685
    • (2008) Biochimie , vol.90 , Issue.5 , pp. 679-685
    • Kuo, M.1    Zilberfarb, V.2    Gangneux, N.3    Christeff, N.4    Issad, T.5
  • 58
    • 0024445798 scopus 로고
    • Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
    • DOI 10.1016/0092-8674(89)90013-5
    • Gonzalez G. A., Montminy M. R., Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133 Cell 1989 59 4 675 680 (Pubitemid 19282874)
    • (1989) Cell , vol.59 , Issue.4 , pp. 675-680
    • Gonzalez, G.A.1    Montminy, M.R.2
  • 60
    • 0027166104 scopus 로고
    • Coupling of hormonal stimulation and transcription via the cyclic AMP- responsive factor CREB is rate limited by nuclear entry of protein kinase A
    • Hagiwara M., Brindle P., Harootunian A., Armstrong R., Rivier J., Vale W., Tsien R., Montminy M. R., Coupling of hormonal stimulation and transcription via the cyclic AMP- responsive factor CREB is rate limited by nuclear entry of protein kinase A Molecular and Cellular Biology 1993 13 8 4852 4859 (Pubitemid 23220391)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.8 , pp. 4852-4859
    • Hagiwara, M.1    Brindle, P.2    Harootunian, A.3    Armstrong, R.4    Rivier, J.5    Vale, W.6    Tsien, R.7    Montminy, M.R.8
  • 61
    • 0027433708 scopus 로고
    • Phosphorylated CREB binds specifically to the nuclear protein CBP
    • DOI 10.1038/365855a0
    • Chrivia J. C., Kwok R. P. S., Lamb N., Hagiwara M., Montminy M. R., Goodman R. H., Phosphorylated CREB binds specifically to the nuclear protein CBP Nature 1993 365 6449 855 859 (Pubitemid 23341031)
    • (1993) Nature , vol.365 , Issue.6449 , pp. 855-859
    • Chrivia, J.C.1    Kwok, R.P.S.2    Lamb, N.3    Hagiwara, M.4    Montminy, M.R.5    Goodman, R.H.6
  • 62
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • DOI 10.1038/384641a0
    • Bannister A. J., Kouzarides T., The CBP co-activator is a histone acetyltransferase Nature 1996 384 6610 641 643 (Pubitemid 27021517)
    • (1996) Nature , vol.384 , Issue.6610 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 63
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • DOI 10.1016/S0092-8674(00)82001-2
    • 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 5 953 959 (Pubitemid 26404293)
    • (1996) Cell , vol.87 , Issue.5 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 64
    • 0000735813 scopus 로고    scopus 로고
    • Efficient recruitment of TFIIB and CBP-RNA polymerase II holoenzyme by an interferon-β enhanceosome in vitro
    • DOI 10.1073/pnas.95.21.12191
    • Kim T. K., Kim T. H., Maniatis T., Efficient recruitment of TFIIB and CBP-RNA polymerase II holoenzyme by an interferon- enhanceosome in vitro Proceedings of the National Academy of Sciences of the United States of America 1998 95 21 12191 12196 (Pubitemid 28483741)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.21 , pp. 12191-12196
    • Kim, T.K.1    Kim, T.H.2    Maniatis, T.3
  • 65
    • 0030029419 scopus 로고    scopus 로고
    • Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator
    • DOI 10.1074/jbc.271.5.2373
    • Kee B. L., Arias J., Montminy M. R., Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator Journal of Biological Chemistry 1996 271 5 2373 2375 (Pubitemid 26047835)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.5 , pp. 2373-2375
    • Kee, B.L.1    Arias, J.2    Montminy, M.R.3
  • 66
    • 0027943988 scopus 로고
    • Differential activation of CREB by Ca2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity
    • Sun P., Enslen H., Myung P. S., Maurer R. A., Differential activation of CREB by Ca2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity Genes and Development 1994 8 21 2527 2539
    • (1994) Genes and Development , vol.8 , Issue.21 , pp. 2527-2539
    • Sun, P.1    Enslen, H.2    Myung, P.S.3    Maurer, R.A.4
  • 67
    • 0032161642 scopus 로고    scopus 로고
    • Analysis of an activator:Coactivator complex reveals an essential role for secondary structure in transcriptional activation
    • Parker D., Jhala U. S., Radhakrishnan I., Yaffe M. B., Reyes C., Shulman A. I., Cantley L. C., Wright P. E., Montminy M., Analysis of an activator: coactivator complex reveals an essential role for secondary structure in transcriptional activation Molecular Cell 1998 2 3 353 359 (Pubitemid 128379275)
    • (1998) Molecular Cell , vol.2 , Issue.3 , pp. 353-359
    • Parker, D.1    Jhala, U.S.2    Radhakrishnan, I.3    Yaffe, M.B.4    Reyes, C.5    Shulman, A.I.6    Cantley, L.C.7    Wright, P.E.8    Montminy, M.9
  • 69
    • 34250375258 scopus 로고    scopus 로고
    • Coregulated ataxia telangiectasia-mutated and casein kinase sites modulate cAMP-response element-binding protein-coactivator interactions in response to DNA damage
    • DOI 10.1074/jbc.M610674200
    • Shanware N. P., Trinh A. T., Williams L. M., Tibbetts R. S., Coregulated ataxia telangiectasia-mutated and casein kinase sites modulate cAMP-response element-binding protein-coactivator interactions in response to DNA damage Journal of Biological Chemistry 2007 282 9 6283 6291 (Pubitemid 47100879)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6283-6291
    • Shanware, N.P.1    Trinh, A.T.2    Williams, L.M.3    Tibbetts, R.S.4
  • 74
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • DOI 10.1126/science.1151363
    • Dentin R., Hedrick S., Xie J., Yates J. III, Montminy M., Hepatic glucose sensing via the CREB coactivator CRTC2 Science 2008 319 5868 1402 1405 (Pubitemid 351354877)
    • (2008) Science , vol.319 , Issue.5868 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3    Yates III, J.4    Montminy, M.5
  • 75
    • 0344874201 scopus 로고    scopus 로고
    • Contribution of hepatic de novo lipogenesis and reesterification of plasma non esterified fatty acids to plasma triglyceride synthesis during non-alcoholic fatty liver disease
    • Diraison F., Moulin P. H., Beylot M., Contribution of hepatic de novo lipogenesis and reesterification of plasma non esterified fatty acids to plasma triglyceride synthesis during non-alcoholic fatty liver disease Diabetes and Metabolism 2003 29 5 478 485 (Pubitemid 37474259)
    • (2003) Diabetes and Metabolism , vol.29 , Issue.5 , pp. 478-485
    • Diraison, F.1    Moulin, P.H.2    Beylot, M.3
  • 76
    • 0031887281 scopus 로고    scopus 로고
    • Role of human liver lipogenesis and reesterification in triglycerides secretion and in FFA reesterification
    • Diraison F., Beylot M., Role of human liver lipogenesis and reesterification in triglycerides secretion and in FFA reesterification American Journal of PhysiologyEndocrinology and Metabolism 1998 274 2, part 1 E321 E327
    • (1998) American Journal of PhysiologyEndocrinology and Metabolism , vol.274 , Issue.2 PART 1
    • Diraison, F.1    Beylot, M.2
  • 77
    • 14544289119 scopus 로고    scopus 로고
    • Carbohydrate responsive element binding protein (ChREBP) and sterol regulatory element binding protein-1c (SREBP-1c): Two key regulators of glucose metabolism and lipid synthesis in liver
    • DOI 10.1016/j.biochi.2004.11.008
    • Dentin R., Girard J., Postic C., Carbohydrate responsive element binding protein (ChREBP) and sterol regulatory element binding protein-1c (SREBP-1c): two key regulators of glucose metabolism and lipid synthesis in liver Biochimie 2005 87 1 81 86 (Pubitemid 40298769)
    • (2005) Biochimie , vol.87 , Issue.1 SPEC. ISS. , pp. 81-86
    • Dentin, R.1    Girard, J.2    Postic, C.3
  • 78
    • 66349134748 scopus 로고    scopus 로고
    • Cholesterol feedback: From Schoenheimer's bottle to Scap's MELADL
    • Brown M. S., Goldstein J. L., Cholesterol feedback: from Schoenheimer's bottle to Scap's MELADL Journal of Lipid Research 2009 50 S15 S27
    • (2009) Journal of Lipid Research , vol.50
    • Brown, M.S.1    Goldstein, J.L.2
  • 80
    • 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 Metabolism 2009 10 5 405 418
    • (2009) Cell Metabolism , vol.10 , Issue.5 , pp. 405-418
    • Leavens, K.F.1    Easton, R.M.2    Shulman, G.I.3    Previs, S.F.4    Birnbaum, M.J.5
  • 82
    • 65549140251 scopus 로고    scopus 로고
    • A phosphorylation cascade controls the degradation of active SREBP1
    • Bengoechea-Alonso M. T., Ericsson J., A phosphorylation cascade controls the degradation of active SREBP1 Journal of Biological Chemistry 2009 284 9 5885 5895
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.9 , pp. 5885-5895
    • Bengoechea-Alonso, M.T.1    Ericsson, J.2
  • 84
    • 33744821064 scopus 로고    scopus 로고
    • Sterol regulatory element-binding protein 1 is negatively modulated by PKA phosphorylation
    • Lu M., Shyy J. Y. J., Sterol regulatory element-binding protein 1 is negatively modulated by PKA phosphorylation American Journal of PhysiologyCell Physiology 2006 290 6 C1477 C1486
    • (2006) American Journal of PhysiologyCell Physiology , vol.290 , Issue.6
    • Lu, M.1    Shyy, J.Y.J.2
  • 86
    • 67449084097 scopus 로고    scopus 로고
    • Salt-inducible kinase regulates hepatic lipogenesis by controlling SREBP-1c phosphorylation
    • Yoon Y. S., Seo W. Y., Lee M. W., Kim S. T., Koo S. H., Salt-inducible kinase regulates hepatic lipogenesis by controlling SREBP-1c phosphorylation Journal of Biological Chemistry 2009 284 16 10446 10452
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.16 , pp. 10446-10452
    • Yoon, Y.S.1    Seo, W.Y.2    Lee, M.W.3    Kim, S.T.4    Koo, S.H.5
  • 87
    • 0037930875 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins are negatively regulated through SUMO-1 modification independent of the ubiquitin/26 S proteasome pathway
    • DOI 10.1074/jbc.M212448200
    • Hirano Y., Murata S., Tanaka K., Shimizu M., Sato R., Sterol regulatory element-binding proteins are negatively regulated through SUMO-1 modification independent of the ubiquitin/26 S proteasome pathway Journal of Biological Chemistry 2003 278 19 16809 16819 (Pubitemid 36799550)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16809-16819
    • Hirano, Y.1    Murata, S.2    Tanaka, K.3    Shimizu, M.4    Sato, R.5
  • 88
    • 0037378516 scopus 로고    scopus 로고
    • Coactivator-dependent acetylation stabilizes members of the SREBP family of transcription factors
    • DOI 10.1128/MCB.23.7.2587-2599.2003
    • Giandomenico V., Simonsson M., Grnroos E., Ericsson J., Coactivator-dependent acetylation stabilizes members of the SREBP family of transcription factors Molecular and Cellular Biology 2003 23 7 2587 2599 (Pubitemid 36351037)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.7 , pp. 2587-2599
    • Giandomenico, V.1    Simonsson, M.2    Gronroos, E.3    Ericsson, J.4
  • 90
    • 38449087713 scopus 로고    scopus 로고
    • ChREBP, a transcriptional regulator of glucose and lipid metabolism
    • DOI 10.1146/annurev.nutr.27.061406.093618
    • Postic C., Dentin R., Denechaud P. D., Girard J., ChREBP, a transcriptional regulator of glucose and lipid metabolism Annual Review of Nutrition 2007 27 179 192 (Pubitemid 351373354)
    • (2007) Annual Review of Nutrition , vol.27 , pp. 179-192
    • Postic, C.1    Dentin, R.2    Denechaud, P.-D.3    Girard, J.4
  • 91
    • 0030753971 scopus 로고    scopus 로고
    • Regulation of the expression of lipogenic enzyme genes by carbohydrate
    • DOI 10.1146/annurev.nutr.17.1.405
    • Towle H. C., Kaytor E. N., Shih H. M., Regulation of the expression of lipogenic enzyme genes by carbohydrate Annual Review of Nutrition 1997 17 405 433 (Pubitemid 27328807)
    • (1997) Annual Review of Nutrition , vol.17 , pp. 405-433
    • Towle, H.C.1    Kaytor, E.N.2    Shih, H.-M.3
  • 92
    • 0035923516 scopus 로고    scopus 로고
    • Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein
    • DOI 10.1073/pnas.231370798
    • Kawaguchi T., Takenoshita M., Kabashima T., Uyeda K., Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein Proceedings of the National Academy of Sciences of the United States of America 2001 98 24 13710 13715 (Pubitemid 33115963)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.24 , pp. 13710-13715
    • Kawaguchi, T.1    Takenoshita, M.2    Kabashima, T.3    Uyeda, K.4
  • 93
    • 0037040185 scopus 로고    scopus 로고
    • Mechanism for fatty acid "sparing" effect on glucose-induced transcription: Regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase
    • DOI 10.1074/jbc.M107895200
    • Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K., Mechanism for fatty acid sparing effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase Journal of Biological Chemistry 2002 277 6 3829 3835 (Pubitemid 34968632)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 3829-3835
    • Kawaguchi, T.1    Osatomi, K.2    Yamashita, H.3    Kabashima, T.4    Uyeda, K.5
  • 95
    • 33745297834 scopus 로고    scopus 로고
    • Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module
    • DOI 10.2337/db05-0822
    • Li M. V., Chang B., Imamura M., Poungvarin N., Chan L., Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module Diabetes 2006 55 5 1179 1189 (Pubitemid 44195353)
    • (2006) Diabetes , vol.55 , Issue.5 , pp. 1179-1189
    • Li, M.V.1    Chang, B.2    Imamura, M.3    Poungvarin, N.4    Chan, L.5
  • 96
    • 29644446917 scopus 로고    scopus 로고
    • Glucose activation of ChREBP in hepatocytes occurs via a two-step mechanism
    • DOI 10.1016/j.bbrc.2005.12.029, PII S0006291X05027610
    • Tsatsos N. G., Towle H. C., Glucose activation of ChREBP in hepatocytes occurs via a two-step mechanism Biochemical and Biophysical Research Communications 2006 340 2 449 456 (Pubitemid 43021769)
    • (2006) Biochemical and Biophysical Research Communications , vol.340 , Issue.2 , pp. 449-456
    • Tsatsos, N.G.1    Towle, H.C.2
  • 98
    • 33745863033 scopus 로고    scopus 로고
    • Islet β cell failure in type 2 diabetes
    • DOI 10.1172/JCI29103
    • Prentki M., Nolan C. J., Islet cell failure in type 2 diabetes Journal of Clinical Investigation 2006 116 7 1802 1812 (Pubitemid 44033300)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.7 , pp. 1802-1812
    • Prentki, M.1    Nolan, C.J.2
  • 99
    • 34548670709 scopus 로고    scopus 로고
    • Role of FoxO proteins in pancreatic β cells
    • DOI 10.1507/endocrj.KR-109
    • Kitamura T., Kitamura Y. I., Role of FoxO proteins in pancreatic cells Endocrine Journal 2007 54 4 507 515 (Pubitemid 47414596)
    • (2007) Endocrine Journal , vol.54 , Issue.4 , pp. 507-515
    • Kitamura, T.1    Ido Kitamura, Y.2
  • 100
    • 35148877285 scopus 로고    scopus 로고
    • Regulation of pancreatic β-cell function by the forkhead protein FoxO1
    • DOI 10.1111/j.1463-1326.2007.00782.x
    • Buteau J., Accili D., Regulation of pancreatic -cell function by the forkhead protein FoxO1 Diabetes, Obesity and Metabolism 2007 9 supplement 2 140 146 (Pubitemid 47543136)
    • (2007) Diabetes, Obesity and Metabolism , vol.9 , Issue.SUPPL. 2 , pp. 140-146
    • Buteau, J.1    Accili, D.2
  • 102
    • 0036787607 scopus 로고    scopus 로고
    • Regulation of insulin action and pancreatic -cell function by mutated alleles of the gene encoding forkhead transcription factor Foxo1
    • Nakae J., Biggs W. H. III, Kitamura T., Cavenee W. K., Wright C. V. E., Arden K. C., Accili D., Regulation of insulin action and pancreatic -cell function by mutated alleles of the gene encoding forkhead transcription factor Foxo1 Nature Genetics 2002 32 2 245 253
    • (2002) Nature Genetics , vol.32 , Issue.2 , pp. 245-253
    • Nakae, J.1    Biggs III, W.H.2    Kitamura, T.3    Cavenee, W.K.4    Wright, C.V.E.5    Arden, K.C.6    Accili, D.7
  • 103
    • 33845270456 scopus 로고    scopus 로고
    • Transcription factors regulating β-cell function
    • DOI 10.1530/eje.1.02277
    • Cerf M. E., Transcription factors regulating -cell function European Journal of Endocrinology 2006 155 5 671 679 (Pubitemid 44857490)
    • (2006) European Journal of Endocrinology , vol.155 , Issue.5 , pp. 671-679
    • Cerf, M.E.1
  • 104
    • 33644865024 scopus 로고    scopus 로고
    • The forkhead transcription factor Foxo1 bridges the JNK pathway and the transcription factor PDX-1 through its intracellular translocation
    • Kawamori D., Kaneto H., Nakatani Y., Matsuoka T. A., Matsuhisa M., Hori M., Yamasaki Y., The forkhead transcription factor Foxo1 bridges the JNK pathway and the transcription factor PDX-1 through its intracellular translocation Journal of Biological Chemistry 2006 281 2 1091 1098
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.2 , pp. 1091-1098
    • Kawamori, D.1    Kaneto, H.2    Nakatani, Y.3    Matsuoka, T.A.4    Matsuhisa, M.5    Hori, M.6    Yamasaki, Y.7
  • 108
    • 0037709390 scopus 로고    scopus 로고
    • The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 β-cells
    • DOI 10.1016/S0003-9861(03)00234-0
    • Gao Y., Miyazaki J. I., Hart G. W., The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 -cells Archives of Biochemistry and Biophysics 2003 415 2 155 163 (Pubitemid 36794127)
    • (2003) Archives of Biochemistry and Biophysics , vol.415 , Issue.2 , pp. 155-163
    • Gao, Y.1    Miyazaki, J.-I.2    Hart, G.W.3
  • 109
    • 34447515852 scopus 로고    scopus 로고
    • Glucose mediates the translocation of neuroD1 by O-linked glycosylation
    • DOI 10.1074/jbc.M701762200
    • Andrali S. S., Qian Q., zcan S., Glucose mediates the translocation of neuroD1 by O-linked glycosylation Journal of Biological Chemistry 2007 282 21 15589 15596 (Pubitemid 47093263)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.21 , pp. 15589-15596
    • Andrali, S.S.1    Qian, Q.2    Ozcan, S.3
  • 110
    • 33846488647 scopus 로고    scopus 로고
    • Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats
    • DOI 10.1093/glycob/cwl067
    • Akimoto Y., Hart G. W., Wells L., Vosseller K., Yamamoto K., Munetomo E., Ohara-Imaizumi M., Nishiwaki C., Nagamatsu S., Hirano H., Kawakami H., Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats Glycobiology 2007 17 2 127 140 (Pubitemid 46152531)
    • (2007) Glycobiology , vol.17 , Issue.2 , pp. 127-140
    • Akimoto, Y.1    Hart, G.W.2    Wells, L.3    Vosseller, K.4    Yamamoto, K.5    Munetomo, E.6    Ohara-Imaizumi, M.7    Nishiwaki, C.8    Nagamatsu, S.9    Hirano, H.10    Kawakami, H.11
  • 111
    • 14544298788 scopus 로고    scopus 로고
    • NeuroD: The predicted and the suprising
    • Chae J. H., Stein G. H., Lee J. E., NeuroD: the predicted and the suprising Molecules and Cells 2004 18 3 271 288 (Pubitemid 40298021)
    • (2004) Molecules and Cells , vol.18 , Issue.3 , pp. 271-288
    • Chae, J.H.1    Stein, G.H.2    Lee, J.E.3
  • 113
    • 0030846574 scopus 로고    scopus 로고
    • The p38/reactivating kinase mitogen-activated protein kinase cascade mediates the activation of the transcription factor insulin upstream factor 1 and insulin gene transcription by high glucose in pancreatic β-cells
    • DOI 10.1074/jbc.272.33.20936
    • Macfarlane W. M., Smith S. B., James R. F. L., Clifton A. D., Doza Y. N., Cohen P., Docherty K., The p38/reactivating kinase mitogen-activated protein kinase cascade mediates the activation of the transcription factor insulin upstream factor 1 and insulin gene transcription by high glucose in pancreatic -cells Journal of Biological Chemistry 1997 272 33 20936 20944 (Pubitemid 27355666)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20936-20944
    • Macfarlane, W.M.1    Smith, S.B.2    James, R.F.L.3    Clifton, A.D.4    Doza, Y.N.5    Cohen, P.6    Docherty, K.7
  • 114
    • 0033534620 scopus 로고    scopus 로고
    • Glucose stimulates translocation of the homeodomain transcription factor PDX1 from the cytoplasm to the nucleus in pancreatic -cells
    • Macfarlane W. M., McKinnon C. M., Felton-Edkins Z. A., Cragg H., James R. F. L., Docherty K., Glucose stimulates translocation of the homeodomain transcription factor PDX1 from the cytoplasm to the nucleus in pancreatic -cells Journal of Biological Chemistry 1999 274 2 1011 1016
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.2 , pp. 1011-1016
    • MacFarlane, W.M.1    McKinnon, C.M.2    Felton-Edkins, Z.A.3    Cragg, H.4    James, R.F.L.5    Docherty, K.6
  • 115
    • 0034717337 scopus 로고    scopus 로고
    • Glucose-stimulated preproinsulin gene expression and nuclear trans- location of pancreatic duodenum homeobox-1 require activation of phosphatidylinositol 3-kinase but not p38 MAPK/SAPK2
    • DOI 10.1074/jbc.275.21.15977
    • Rafiq I., da Silva Xavier G., Hooper S., Rutter G. A., Glucose-stimulated preproinsulin gene expression and nuclear translocation of pancreatic duodenum homeobox-1 require activation of phosphatidylinositol 3-kinase but not p38 MAPK/SAPK2 Journal of Biological Chemistry 2000 275 21 15977 15984 (Pubitemid 30366902)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 15977-15984
    • Rafiq, I.1    Da Silva Xavier, G.2    Hooper, S.3    Rutter, G.A.4
  • 117
    • 33646549635 scopus 로고    scopus 로고
    • Phosphorylation marks IPF1/PDX1 protein for degradation by glycogen synthase kinase 3-dependent mechanisms
    • DOI 10.1074/jbc.M511597200
    • Boucher M. J., Selander L., Carlsson L., Edlund H., Phosphorylation marks IPF1/PDX1 protein for degradation by glycogen synthase kinase 3-dependent mechanisms Journal of Biological Chemistry 2006 281 10 6395 6403 (Pubitemid 43847571)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6395-6403
    • Boucher, M.-J.1    Selander, L.2    Carlsson, L.3    Edlund, H.4
  • 118
    • 14644427890 scopus 로고    scopus 로고
    • Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB
    • DOI 10.1038/nm1166
    • Cai D., Yuan M., Frantz D. F., Melendez P. A., Hansen L., Lee J., Shoelson S. E., Local and systemic insulin resistance resulting from hepatic activation of IKK- and NF- B Nature Medicine 2005 11 2 183 190 (Pubitemid 40321354)
    • (2005) Nature Medicine , vol.11 , Issue.2 , pp. 183-190
    • Cai, D.1    Yuan, M.2    Frantz, D.F.3    Melendez, P.A.4    Hansen, L.5    Lee, J.6    Shoelson, S.E.7
  • 119
    • 79151478555 scopus 로고    scopus 로고
    • Type 2 diabetes as an inflammatory disease
    • Donath M. Y., Shoelson S. E., Type 2 diabetes as an inflammatory disease Nature Reviews Immunology 2011 11 2 98 107
    • (2011) Nature Reviews Immunology , vol.11 , Issue.2 , pp. 98-107
    • Donath, M.Y.1    Shoelson, S.E.2
  • 121
    • 35148854599 scopus 로고    scopus 로고
    • Hypoxia is a potential risk factor for chronic inflammation and adiponectin reduction in adipose tissue of ob/ob and dietary obese mice
    • Ye J., Gao Z., Yin J., He Q., Hypoxia is a potential risk factor for chronic inflammation and adiponectin reduction in adipose tissue of ob/ob and dietary obese mice American Journal of PhysiologyEndocrinology and Metabolism 2007 293 4 E1118 E1128
    • (2007) American Journal of PhysiologyEndocrinology and Metabolism , vol.293 , Issue.4
    • Ye, J.1    Gao, Z.2    Yin, J.3    He, Q.4
  • 124
    • 33846026712 scopus 로고    scopus 로고
    • Obesity induces a phenotypic switch in adipose tissue macrophage polarization
    • DOI 10.1172/JCI29881
    • Lumeng C. N., Bodzin J. L., Saltiel A. R., Obesity induces a phenotypic switch in adipose tissue macrophage polarization Journal of Clinical Investigation 2007 117 1 175 184 (Pubitemid 46048464)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.1 , pp. 175-184
    • Lumeng, C.N.1    Bodzin, J.L.2    Saltiel, A.R.3
  • 125
    • 33847073149 scopus 로고    scopus 로고
    • Increased inflammatory properties of adipose tissue macrophages recruited during diet-induced obesity
    • Lumeng C. N., DeYoung S. M., Bodzin J. L., Saltiel A. R., Increased inflammatory properties of adipose tissue macrophages recruited during diet-induced obesity Diabetes 2007 56 1 16 23
    • (2007) Diabetes , vol.56 , Issue.1 , pp. 16-23
    • Lumeng, C.N.1    Deyoung, S.M.2    Bodzin, J.L.3    Saltiel, A.R.4
  • 128
    • 51349156218 scopus 로고    scopus 로고
    • Insulin sensitivity: Modulation by nutrients and inflammation
    • Schenk S., Saberi M., Olefsky J. M., Insulin sensitivity: modulation by nutrients and inflammation Journal of Clinical Investigation 2008 118 9 2992 3002
    • (2008) Journal of Clinical Investigation , vol.118 , Issue.9 , pp. 2992-3002
    • Schenk, S.1    Saberi, M.2    Olefsky, J.M.3
  • 129
    • 34247857663 scopus 로고    scopus 로고
    • Obesity, Inflammation, and Insulin Resistance
    • DOI 10.1053/j.gastro.2007.03.059, PII S0016508507005859
    • Shoelson S. E., Herrero L., Naaz A., Obesity, inflammation, and insulin resistance Gastroenterology 2007 132 6 2169 2180 (Pubitemid 46693756)
    • (2007) Gastroenterology , vol.132 , Issue.6 , pp. 2169-2180
    • Shoelson, S.E.1    Herrero, L.2    Naaz, A.3
  • 130
    • 33750457370 scopus 로고    scopus 로고
    • Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway
    • DOI 10.1038/sj.onc.1209937, PII 1209937
    • Perkins N. D., Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway Oncogene 2006 25 51 6717 6730 (Pubitemid 44657848)
    • (2006) Oncogene , vol.25 , Issue.51 , pp. 6717-6730
    • Perkins, N.D.1
  • 131
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-κB action regulated by reversible acetylation
    • DOI 10.1126/science.1062374
    • Chen L. F., Fischle W., Verdin E., Greene W. C., Duration of nuclear NF- B action regulated by reversible acetylation Science 2001 293 5535 1653 1657 (Pubitemid 32807844)
    • (2001) Science , vol.293 , Issue.5535 , pp. 1653-1657
    • Chen, L.-F.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 132
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
    • DOI 10.1038/sj.emboj.7600244
    • Yeung F., Hoberg J. E., Ramsey C. S., Keller M. D., Jones D. R., Frye R. A., Mayo M. W., Modulation of NF- B-dependent transcription and cell survival by the SIRT1 deacetylase EMBO Journal 2004 23 12 2369 2380 (Pubitemid 38954844)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 133
    • 0033527448 scopus 로고    scopus 로고
    • The nuclear factor- B engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter
    • Berghe W. V., de Bosscher K., Boone E., Plaisance S., Haegeman G., The nuclear factor- B engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter Journal of Biological Chemistry 1999 274 45 32091 32098
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.45 , pp. 32091-32098
    • Berghe, W.V.1    De Bosscher, K.2    Boone, E.3    Plaisance, S.4    Haegeman, G.5
  • 137
    • 5644235488 scopus 로고    scopus 로고
    • NF-κB: A multifaceted transcription factor regulated at several levels
    • DOI 10.1002/cbic.200400144
    • Schmitz M. L., Mattioli I., Buss H., Kracht M., NF- B: a multifaceted transcription factor regulated at several levels ChemBioChem 2004 5 10 1348 1358 (Pubitemid 39371504)
    • (2004) ChemBioChem , vol.5 , Issue.10 , pp. 1348-1358
    • Schmitz, M.L.1    Mattioli, I.2    Buss, H.3    Kracht, M.4
  • 138
    • 0037451357 scopus 로고    scopus 로고
    • Transcriptional activation of the NF-κB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)
    • DOI 10.1093/emboj/cdg139
    • Vermeulen L., de Wilde G., van Damme P., Berghe W. V., Haegeman G., Transcriptional activation of the NF- B p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1) EMBO Journal 2003 22 6 1313 1324 (Pubitemid 36362695)
    • (2003) EMBO Journal , vol.22 , Issue.6 , pp. 1313-1324
    • Vermeulen, L.1    De Wilde, G.2    Van Damme, P.3    Vanden Berghe, W.4    Haegeman, G.5
  • 139
    • 0042525909 scopus 로고    scopus 로고
    • Essential role of RelA Ser311 phosphorylation by ζPKC in NF-κB transcriptional activation
    • DOI 10.1093/emboj/cdg370
    • Duran A., Diaz-Meco M. T., Moscat J., Essential role of RelA Ser311 phosphorylation by PKC in NF- B transcriptional activation EMBO Journal 2003 22 15 3910 3918 (Pubitemid 36975717)
    • (2003) EMBO Journal , vol.22 , Issue.15 , pp. 3910-3918
    • Duran, A.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 141
    • 0034693133 scopus 로고    scopus 로고
    • Tumor necrosis factor -induced phosphorylation of RelA/p65 on ser 529 is controlled by casein kinase II
    • Wang D., Westerheide S. D., Hanson J. L., Baldwin A. S. Jr., Tumor necrosis factor -induced phosphorylation of RelA/p65 on Ser 529 is controlled by casein kinase II Journal of Biological Chemistry 2000 275 42 32592 32597
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.42 , pp. 32592-32597
    • Wang, D.1    Westerheide, S.D.2    Hanson, J.L.3    Baldwin Jr., A.S.4
  • 143
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-κB Signaling by Pin1-Dependent Prolyl Isomerization and Ubiquitin-Mediated Proteolysis of p65/RelA
    • DOI 10.1016/S1097-2765(03)00490-8
    • Ryo A., Suizu F., Yoshida Y., Perrem K., Liou Y. C., Wulf G., Rottapel R., Yamaoka S., Lu K. P., Regulation of NF- B signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA Molecular Cell 2003 12 6 1413 1426 (Pubitemid 38037011)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1413-1426
    • Ryo, A.1    Suizu, F.2    Yoshida, Y.3    Perrem, K.4    Liou, Y.-C.5    Wulf, G.6    Rottapel, R.7    Yamaoka, S.8    Lu, K.P.9
  • 144
  • 145
    • 0037016688 scopus 로고    scopus 로고
    • Tumor necrosis factor α increases the expression of glycosyltransferases and sulfotransferases responsible for the biosynthesis of sialylated and/or sulfated Lewis x epitopes in the human bronchial mucosa
    • DOI 10.1074/jbc.M109958200
    • Delmotte P., Degroote S., Lafitte J. J., Lamblin G., Perini J. M., Roussel P., Tumor necrosis factor increases the expression of glycosyltransferases and sulfotransferases responsible for the biosynthesis of sialylated and/or sulfated Lewis x epitopes in the human bronchial mucosa Journal of Biological Chemistry 2002 277 1 424 431 (Pubitemid 34952075)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 424-431
    • Delmotte, P.1    Degroote, S.2    Lafitte, J.-J.3    Lamblin, G.4    Perini, J.-M.5    Roussel, P.6
  • 146
    • 0036231781 scopus 로고    scopus 로고
    • Flux through the hexosamine pathway is a determinant of nuclear factor κB-dependent promoter activation
    • James L. R., Tang D., Ingram A., Ly H., Thai K., Cai L., Seholey J. W., Flux through the hexosamine pathway is a determinant of nuclear factor B-dependent promoter activation Diabetes 2002 51 4 1146 1156 (Pubitemid 34438362)
    • (2002) Diabetes , vol.51 , Issue.4 , pp. 1146-1156
    • James, L.R.1    Tang, D.2    Ingram, A.3    Ly, H.4    Thai, K.5    Cai, L.6    Seholey, J.W.7
  • 148
    • 77951918926 scopus 로고    scopus 로고
    • Macrophages, inflammation, and insulin resistance
    • Olefsky J. M., Glass C. K., Macrophages, inflammation, and insulin resistance Annual Review of Physiology 2010 72 219 246
    • (2010) Annual Review of Physiology , vol.72 , pp. 219-246
    • Olefsky, J.M.1    Glass, C.K.2
  • 150
    • 0031014830 scopus 로고    scopus 로고
    • Role of fatty acids in the pathogenesis of insulin resistance and NIDDM
    • Boden G., Role of fatty acids in the pathogenesis of insulin resistance and NIDDM Diabetes 1997 46 1 3 10 (Pubitemid 27009941)
    • (1997) Diabetes , vol.46 , Issue.1 , pp. 3-10
    • Boden, G.1
  • 153
    • 0034076660 scopus 로고    scopus 로고
    • Fuel selection in human skeletal muscle in insulin resistance: A reexamination
    • Kelley D. E., Mandarino L. J., Fuel selection in human skeletal muscle in insulin resistance: a reexamination Diabetes 2000 49 5 677 683 (Pubitemid 30339979)
    • (2000) Diabetes , vol.49 , Issue.5 , pp. 677-683
    • Kelley, D.E.1    Mandarino, L.J.2
  • 154
    • 0036300538 scopus 로고    scopus 로고
    • Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IκB-α
    • Itani S. I., Ruderman N. B., Schmieder F., Boden G., Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and I B- Diabetes 2002 51 7 2005 2011 (Pubitemid 34729001)
    • (2002) Diabetes , vol.51 , Issue.7 , pp. 2005-2011
    • Itani, S.I.1    Ruderman, N.B.2    Schmieder, F.3    Boden, G.4
  • 155
    • 1642377274 scopus 로고    scopus 로고
    • Impaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes
    • DOI 10.1056/NEJMoa031314
    • Petersen K. F., Dufour S., Befroy D., Garcia R., Shulman G. I., Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes The New England Journal of Medicine 2004 350 7 664 671 (Pubitemid 38364625)
    • (2004) New England Journal of Medicine , vol.350 , Issue.7 , pp. 664-671
    • Petersen, K.F.1    Dufour, S.2    Befroy, D.3    Garcia, R.4    Shulman, G.I.5
  • 157
    • 0035979775 scopus 로고    scopus 로고
    • Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkβ
    • DOI 10.1126/science.1061620
    • Yuan M., Konstantopoulos N., Lee J., Hansen L., Li Z. W., Karin M., Shoelson S. E., Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikk Science 2001 293 5535 1673 1677 (Pubitemid 32807849)
    • (2001) Science , vol.293 , Issue.5535 , pp. 1673-1677
    • Yuan, M.1    Konstantopoulos, N.2    Lee, J.3    Hansen, L.4    Li, Z.-W.5    Karin, M.6    Shoelson, S.E.7
  • 158
    • 33645860825 scopus 로고    scopus 로고
    • Reactive oxygen species have a causal role in multiple forms of insulin resistance
    • Houstis N., Rosen E. D., Lander E. S., Reactive oxygen species have a causal role in multiple forms of insulin resistance Nature 2006 440 7086 944 948
    • (2006) Nature , vol.440 , Issue.7086 , pp. 944-948
    • Houstis, N.1    Rosen, E.D.2    Lander, E.S.3
  • 160
    • 29944445284 scopus 로고    scopus 로고
    • Increased intramuscular lipid storage in the insulin-resistant and endurance-trained state
    • DOI 10.1007/s00424-005-1509-0
    • van Loon L. J. C., Goodpaster B. H., Increased intramuscular lipid storage in the insulin-resistant and endurance-trained state Pflugers Archiv 2006 451 5 606 616 (Pubitemid 43042172)
    • (2006) Pflugers Archiv European Journal of Physiology , vol.451 , Issue.5 , pp. 606-616
    • Van Loon, L.J.C.1    Goodpaster, B.H.2
  • 162
    • 77955274518 scopus 로고    scopus 로고
    • PPAR in adipocyte differentiation and metabolismnovel insights from genome-wide studies
    • Siersbk R., Nielsen R., Mandrup S., PPAR in adipocyte differentiation and metabolismnovel insights from genome-wide studies FEBS Letters 2010 584 15 3242 3249
    • (2010) FEBS Letters , vol.584 , Issue.15 , pp. 3242-3249
    • Siersbk, R.1    Nielsen, R.2    Mandrup, S.3
  • 163
    • 0033200389 scopus 로고    scopus 로고
    • Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation
    • DOI 10.1101/gad.13.17.2231
    • Tang Q. Q., Lane M. D., Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation Genes and Development 1999 13 17 2231 2241 (Pubitemid 29426728)
    • (1999) Genes and Development , vol.13 , Issue.17 , pp. 2231-2241
    • Tang, Q.-Q.1    Lane, M.D.2
  • 164
    • 0029062839 scopus 로고
    • Transcriptional regulation of gene expression during adipocyte differentiation
    • MacDougald O. A., Lane M. D., Transcriptional regulation of gene expression during adipocyte differentiation Annual Review of Biochemistry 1995 64 345 373
    • (1995) Annual Review of Biochemistry , vol.64 , pp. 345-373
    • MacDougald, O.A.1    Lane, M.D.2
  • 165
    • 0033083803 scopus 로고    scopus 로고
    • Cross-regulation of C/EBPα and PPARγ controls the transcriptional pathway of adipogenesis and insulin sensitivity
    • DOI 10.1016/S1097-2765(00)80306-8
    • Wu Z., Rosen E. D., Brun R., Hauser S., Adelmant G., Troy A. E., McKeon C., Darlington G. J., Spiegelman B. M., Cross-regulation of C/EBP and PPAR controls the transcriptional pathway of adipogenesis and insulin sensitivity Molecular Cell 1999 3 2 151 158 (Pubitemid 29292616)
    • (1999) Molecular Cell , vol.3 , Issue.2 , pp. 151-158
    • Wu, Z.1    Rosen, E.D.2    Brun, R.3    Hauser, S.4    Adelmant, G.5    Troy, A.E.6    McKeon, C.7    Darlington, G.J.8    Spiegelman, B.M.9
  • 167
    • 0038776380 scopus 로고    scopus 로고
    • Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARγ
    • DOI 10.1126/science.274.5295.2100
    • Hu E., Kim J. B., Sarraf P., Spiegelman B. M., Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPAR Science 1996 274 5295 2100 2103 (Pubitemid 27020707)
    • (1996) Science , vol.274 , Issue.5295 , pp. 2100-2103
    • Hu, E.1    Kim, J.B.2    Sarraf, P.3    Spiegelman, B.M.4
  • 168
    • 33947430960 scopus 로고    scopus 로고
    • Endocrine functions of adipose tissue
    • DOI 10.1146/annurev.pathol.2.010506.091859, Annual Review of Pathology: Mechanisms of Disease
    • Waki H., Tontonoz P., Endocrine functions of adipose tissue Annual Review of Pathology 2007 2 31 56 (Pubitemid 46448059)
    • (2007) Annual Review of Pathology , vol.2 , pp. 31-56
    • Waki, H.1    Tontonoz, P.2
  • 169
    • 0037237279 scopus 로고    scopus 로고
    • The forkhead transcription factor Fox01 regulates adipocyte differentiation
    • DOI 10.1016/S1534-5807(02)00401-X, PII S153458070200401X
    • Nakae J., Kitamura T., Kitamura Y., Biggs W. H. III, Arden K. C., Accili D., The forkhead transcription factor Foxo1 regulates adipocyte differentiation Developmental Cell 2003 4 1 119 129 (Pubitemid 36105338)
    • (2003) Developmental Cell , vol.4 , Issue.1 , pp. 119-129
    • Nakae, J.1    Kitamura, T.2    Kitamura, Y.3    Biggs III, W.H.4    Arden, K.C.5    Accili, D.6
  • 170
    • 33845985335 scopus 로고    scopus 로고
    • SIRT1 regulates adiponectin gene expression through Foxo1-C/enhancer- binding protein α transcriptional complex
    • DOI 10.1074/jbc.M607215200
    • Qiao L., Shao J., SIRT1 regulates adiponectin gene expression through Foxo1-C/enhancer- binding protein transcriptional complex Journal of Biological Chemistry 2006 281 52 39915 39924 (Pubitemid 46041795)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 39915-39924
    • Qiao, L.1    Shao, J.2
  • 171
    • 33745834319 scopus 로고    scopus 로고
    • Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome
    • DOI 10.1172/JCI29126
    • Kadowaki T., Yamauchi T., Kubota N., Hara K., Ueki K., Tobe K., Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome Journal of Clinical Investigation 2006 116 7 1784 1792 (Pubitemid 44033298)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.7 , pp. 1784-1792
    • Kadowaki, T.1    Yamauchi, T.2    Kubota, N.3    Hara, K.4    Ueki, K.5    Tobe, K.6
  • 172
    • 44749090905 scopus 로고    scopus 로고
    • Sp1: Emerging roles-beyond constitutive activation of TATA-less housekeeping genes
    • Wierstra I., Sp1: emerging roles-beyond constitutive activation of TATA-less housekeeping genes Biochemical and Biophysical Research Communications 2008 372 1 1 13
    • (2008) Biochemical and Biophysical Research Communications , vol.372 , Issue.1 , pp. 1-13
    • Wierstra, I.1
  • 173
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation
    • Jackson S. P., Tjian R., O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation Cell 1988 55 1 125 133
    • (1988) Cell , vol.55 , Issue.1 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 174
    • 33746457809 scopus 로고    scopus 로고
    • Post-translational modification by O-GlcNAc: Another way to change protein function
    • DOI 10.1002/jcb.20926
    • Kudlow J. E., Post-translational modification by O-GlcNAc: another way to change protein function Journal of Cellular Biochemistry 2006 98 5 1062 1075 (Pubitemid 44128349)
    • (2006) Journal of Cellular Biochemistry , vol.98 , Issue.5 , pp. 1062-1075
    • Kudlow, J.E.1
  • 176
    • 0036141208 scopus 로고    scopus 로고
    • Hexosamines regulate leptin production in 3T3-L1 adipocytes through transcriptional mechanisms
    • DOI 10.1210/en.143.1.99
    • Zhang P., Klenk E. S., Lazzaro M. A., Williams L. B., Considine R. V., Hexosamines regulate leptin production in 3T3-L1 adipocytes through transcriptional mechanisms Endocrinology 2002 143 1 99 106 (Pubitemid 34056408)
    • (2002) Endocrinology , vol.143 , Issue.1 , pp. 99-106
    • Zhang, P.1    Klenk, E.S.2    Lazzaro, M.A.3    Williams, L.B.4    Considine, R.V.5
  • 177
    • 2442618838 scopus 로고    scopus 로고
    • The weight of leptin in immunity
    • La Cava A., Matarese G., The weight of leptin in immunity Nature Reviews Immunology 2004 4 5 371 379 (Pubitemid 38649279)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.5 , pp. 371-379
    • La Cava, A.1    Matarese, G.2
  • 178
    • 14644417152 scopus 로고    scopus 로고
    • Differential responses of visceral and subcutaneous fat depots to nutrients
    • DOI 10.2337/diabetes.54.3.672
    • Einstein F. H., Atzmon G., Yang X. M., Ma X. H., Rincon M., Rudin E., Muzumdar R., Barzilai N., Differential responses of visceral and subcutaneous fat depots to nutrients Diabetes 2005 54 3 672 678 (Pubitemid 40322069)
    • (2005) Diabetes , vol.54 , Issue.3 , pp. 672-678
    • Einstein, F.H.1    Atzmon, G.2    Yang, X.-M.3    Ma, X.-H.4    Rincon, M.5    Rudin, E.6    Muzumdar, R.7    Barzilai, N.8
  • 179
    • 33746669265 scopus 로고    scopus 로고
    • Sp1 mediates repression of the resistin gene by PPARγ agonists in 3T3-L1 adipocytes
    • DOI 10.1016/j.bbrc.2006.07.048, PII S0006291X06015968
    • Chung S. S., Choi H. H., Cho Y. M., Lee H. K., Park K. S., Sp1 mediates repression of the resistin gene by PPAR agonists in 3T3-L1 adipocytes Biochemical and Biophysical Research Communications 2006 348 1 253 258 (Pubitemid 44163507)
    • (2006) Biochemical and Biophysical Research Communications , vol.348 , Issue.1 , pp. 253-258
    • Chung, S.S.1    Choi, H.H.2    Cho, Y.M.3    Lee, H.K.4    Park, K.S.5
  • 181
    • 0034730660 scopus 로고    scopus 로고
    • Regulation of phosphoenolpyruvate carboxykinase and insulin-like growth factor-binding protein-1 gene expression by insulin. The role of winged helix/forkhead proteins
    • Hall R. K., Yamasaki T., Kucera T., Waltner-Law M., O'Brien R., Granner D. K., Regulation of phosphoenolpyruvate carboxykinase and insulin-like growth factor-binding protein-1 gene expression by insulin. The role of winged helix/forkhead proteins Journal of Biological Chemistry 2000 275 39 30169 30175
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.39 , pp. 30169-30175
    • Hall, R.K.1    Yamasaki, T.2    Kucera, T.3    Waltner-Law, M.4    O'Brien, R.5    Granner, D.K.6
  • 182
    • 0034725048 scopus 로고    scopus 로고
    • Transcriptional regulation of the ATP citrate-lyase gene by sterol regulatory element-binding proteins
    • DOI 10.1074/jbc.275.17.12497
    • Sato R., Okamoto A., Inoue J., Miyamoto W., Sakai Y., Emoto N., Shimano H., Maeda M., Transcriptional regulation of the ATP citrate-lyase gene by sterol regulatory element-binding proteins Journal of Biological Chemistry 2000 275 17 12497 12502 (Pubitemid 30241393)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.17 , pp. 12497-12502
    • Sato, R.1    Okamoto, A.2    Inoue, J.3    Miyamoto, W.4    Sakai, Y.5    Emoto, N.6    Shimano, H.7    Maeda, M.8
  • 183
    • 0034730504 scopus 로고    scopus 로고
    • The roles of sterol regulatory element-binding proteins in the transactivation of the rat ATP citrate-lyase promoter
    • Moon Y. A., Lee J. J., Park S. W., Ahn Y. H., Kim K. S., The roles of sterol regulatory element-binding proteins in the transactivation of the rat ATP citrate-lyase promoter Journal of Biological Chemistry 2000 275 39 30280 30286
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.39 , pp. 30280-30286
    • Moon, Y.A.1    Lee, J.J.2    Park, S.W.3    Ahn, Y.H.4    Kim, K.S.5
  • 184
    • 0030868519 scopus 로고    scopus 로고
    • Sterol regulation of acetyl coenzyme A carboxylase promoter requires two interdependent binding sites for sterol regulatory element binding proteins
    • Magaa M. M., Lin S. S., Dooley K. A., Osborne T. F., Sterol regulation of acetyl coenzyme A carboxylase promoter requires two interdependent binding sites for sterol regulatory element binding proteins Journal of Lipid Research 1997 38 8 1630 1638 (Pubitemid 27427660)
    • (1997) Journal of Lipid Research , vol.38 , Issue.8 , pp. 1630-1638
    • Magana, M.M.1    Lin, S.S.2    Dooley, K.A.3    Osborne, T.F.4
  • 185
    • 0043210499 scopus 로고    scopus 로고
    • Acetyl-CoA carboxylase gene is regulated by sterol regulatory element-binding protein-1 in liver
    • Oh S. Y., Park S. K., Kim J. W., Ahn Y. H., Park S. W., Kim K. S., Acetyl-CoA carboxylase gene is regulated by sterol regulatory element-binding protein-1 in liver Journal of Biological Chemistry 2003 278 31 28410 28417
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28410-28417
    • Oh, S.Y.1    Park, S.K.2    Kim, J.W.3    Ahn, Y.H.4    Park, S.W.5    Kim, K.S.6
  • 186
    • 0028875426 scopus 로고
    • Sterol regulation of fatty acid synthase promoter. Coordinate feedback regulation of two major lipid pathways
    • Bennett M. K., Lopez J. M., Sanchez H. B., Osborne T. F., Sterol regulation of fatty acid synthase promoter. Coordinate feedback regulation of two major lipid pathways Journal of Biological Chemistry 1995 270 43 25578 25583
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.43 , pp. 25578-25583
    • Bennett, M.K.1    Lopez, J.M.2    Sanchez, H.B.3    Osborne, T.F.4
  • 187
    • 0040799893 scopus 로고    scopus 로고
    • Identification of conserved cis-elements and transcription factors required for sterol-regulated transcription of stearoyl-CoA desaturase 1 and 2
    • Tabor D. E., Kim J. B., Spiegelman B. M., Edwards P. A., Identification of conserved cis-elements and transcription factors required for sterol-regulated transcription of stearoyl-CoA desaturase 1 and 2 Journal of Biological Chemistry 1999 274 29 20603 20610
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.29 , pp. 20603-20610
    • Tabor, D.E.1    Kim, J.B.2    Spiegelman, B.M.3    Edwards, P.A.4
  • 189
    • 0029094172 scopus 로고
    • Two CACGTG motifs with proper spacing dictate the carbohydrate regulation of hepatic gene transcription
    • Shih H. M., Liu Z., Towle H. C., Two CACGTG motifs with proper spacing dictate the carbohydrate regulation of hepatic gene transcription Journal of Biological Chemistry 1995 270 37 21991 21997
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.37 , pp. 21991-21997
    • Shih, H.M.1    Liu, Z.2    Towle, H.C.3
  • 190
  • 191
    • 0035877604 scopus 로고    scopus 로고
    • Involvement of a unique carbohydrate-responsive factor in the glucose regulation of rat liver fatty-acid synthase gene transcription
    • Rufo C., Teran-Garcia M., Nakamura M. T., Koo S. H., Towle H. C., Clarke S. D., Involvement of a unique carbohydrate-responsive factor in the glucose regulation of rat liver fatty-acid synthase gene transcription Journal of Biological Chemistry 2001 276 24 21969 21975
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.24 , pp. 21969-21975
    • Rufo, C.1    Teran-Garcia, M.2    Nakamura, M.T.3    Koo, S.H.4    Towle, H.C.5    Clarke, S.D.6
  • 193
    • 0027363297 scopus 로고
    • Transcriptional activation of the interleukin-6 gene by HTLV-1 p40tax through an NF-κB-like binding site
    • DOI 10.1016/0165-2478(93)90026-X
    • Muraoka O., Kaisho T., Tanabe M., Hirano T., Transcriptional activation of the interleukin-6 gene by HTLV-1 p40tax through an NF- B-like binding site Immunology Letters 1993 37 2-3 159 165 (Pubitemid 23303730)
    • (1993) Immunology Letters , vol.37 , Issue.2-3 , pp. 159-165
    • Muraoka, O.1    Kaisho, T.2    Tanabe, M.3    Hirano, T.4
  • 194
    • 0030962525 scopus 로고    scopus 로고
    • Cytokine induction of monocyte chemoattractant protein-1 gene expression in human endothelial cells depends on the cooperative action of NF-κB and AP-1
    • Martin T., Cardarelli P. M., Parry G. C. N., Felts K. A., Cobb R. R., Cytokine induction of monocyte chemoattractant protein-1 gene expression in human endothelial cells depends on the cooperative action of NF- B and AP-1 European Journal of Immunology 1997 27 5 1091 1097 (Pubitemid 27197210)
    • (1997) European Journal of Immunology , vol.27 , Issue.5 , pp. 1091-1097
    • Martin, T.1    Cardarelli, P.M.2    Parry, G.C.N.3    Felts, K.A.4    Cobb, R.R.5
  • 195
    • 0030813619 scopus 로고    scopus 로고
    • Identification of a placental enhancer for the human leptin gene
    • DOI 10.1074/jbc.272.48.30583
    • Bi S., Gavrilova O., Gong D. W., Mason M. M., Reitman M., Identification of a placental enhancer for the human leptin gene Journal of Biological Chemistry 1997 272 48 30583 30588 (Pubitemid 27512274)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.48 , pp. 30583-30588
    • Bi, S.1    Gavrilova, O.2    Gong, D.-W.3    Mason, M.M.4    Reitman, M.5


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