메뉴 건너뛰기




Volumn 2011, Issue , 2011, Pages

Studies of complex biological systems with applications to molecular medicine: The need to integrate transcriptomic and proteomic approaches

Author keywords

[No Author keywords available]

Indexed keywords

LEVOTHYROXINE; LIOTHYRONINE; THYROID HORMONE; THYROXINE;

EID: 78349271277     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2011/810242     Document Type: Review
Times cited : (21)

References (117)
  • 1
    • 0028806048 scopus 로고
    • Quantitative monitoring of gene expression patterns with a complementary DNA microarray
    • Schena M., Shalon D., Davis R. W., Brown P. O., Quantitative monitoring of gene expression patterns with a complementary DNA microarray Science 1995 270 5235 467 470
    • (1995) Science , vol.270 , Issue.5235 , pp. 467-470
    • Schena, M.1    Shalon, D.2    Davis, R.W.3    Brown, P.O.4
  • 3
    • 0033966933 scopus 로고    scopus 로고
    • High-throughput gene expression analysis for drug discovery
    • Lennon G. G., High-throughput gene expression analysis for drug discovery Drug Discovery Today 2000 5 2 59 66
    • (2000) Drug Discovery Today , vol.5 , Issue.2 , pp. 59-66
    • Lennon, G.G.1
  • 6
    • 0033961734 scopus 로고    scopus 로고
    • Studying heart disease using the proteomic approach
    • Dunn M. J., Studying heart disease using the proteomic approach Drug Discovery Today 2000 5 2 76 84
    • (2000) Drug Discovery Today , vol.5 , Issue.2 , pp. 76-84
    • Dunn, M.J.1
  • 8
    • 10944228588 scopus 로고    scopus 로고
    • Proteomic approaches in the search for disease biomarkers
    • Vlahou A., Fountoulakis M., Proteomic approaches in the search for disease biomarkers Journal of Chromatography B 2005 814 1 11 19
    • (2005) Journal of Chromatography B , vol.814 , Issue.1 , pp. 11-19
    • Vlahou, A.1    Fountoulakis, M.2
  • 9
    • 0036136997 scopus 로고    scopus 로고
    • Aging of the human neuromuscular system
    • Vandervoort A. A., Aging of the human neuromuscular system Muscle and Nerve 2002 25 1 17 25
    • (2002) Muscle and Nerve , vol.25 , Issue.1 , pp. 17-25
    • Vandervoort, A.A.1
  • 11
    • 0037341605 scopus 로고    scopus 로고
    • Sarcopeniaconsequences, mechanisms, and potential therapies
    • Greenlund L. J. S., Nair K. S., Sarcopeniaconsequences, mechanisms, and potential therapies Mechanisms of Ageing and Development 2003 124 3 287 299
    • (2003) Mechanisms of Ageing and Development , vol.124 , Issue.3 , pp. 287-299
    • Greenlund, L.J.S.1    Nair, K.S.2
  • 13
    • 0031812237 scopus 로고    scopus 로고
    • The age-related motor disability: Underlying mechanisms in skeletal muscle at the motor unit, cellular and molecular level
    • Larsson L., The age-related motor disability: underlying mechanisms in skeletal muscle at the motor unit, cellular and molecular level Acta Physiologica Scandinavica 1998 163 3 S27 S29
    • (1998) Acta Physiologica Scandinavica , vol.163 , Issue.3
    • Larsson, L.1
  • 14
    • 0037288292 scopus 로고    scopus 로고
    • Influence of ageing, heat shock treatment and in vivo total antioxidant status on gene-expression profile and protein synthesis in human peripheral lymphocytes
    • Rao D. V., Boyle G. M., Parsons P. G., Watson K., Jones G. L., Influence of ageing, heat shock treatment and in vivo total antioxidant status on gene-expression profile and protein synthesis in human peripheral lymphocytes Mechanisms of Ageing and Development 2003 124 1 55 69
    • (2003) Mechanisms of Ageing and Development , vol.124 , Issue.1 , pp. 55-69
    • Rao, D.V.1    Boyle, G.M.2    Parsons, P.G.3    Watson, K.4    Jones, G.L.5
  • 15
    • 0034737456 scopus 로고    scopus 로고
    • Mitotic misregulation and human aging
    • Ly D. H., Lockhart D. J., Lerner R. A., Schultz P. G., Mitotic misregulation and human aging Science 2000 287 5462 2486 2492
    • (2000) Science , vol.287 , Issue.5462 , pp. 2486-2492
    • Ly, D.H.1    Lockhart, D.J.2    Lerner, R.A.3    Schultz, P.G.4
  • 17
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • Lu T., Pan Y., Kao S.-Y., Li C., Kohane I., Chan J., Yankner B. A., Gene regulation and DNA damage in the ageing human brain Nature 2004 429 6994 883 891
    • (2004) Nature , vol.429 , Issue.6994 , pp. 883-891
    • Lu, T.1    Pan, Y.2    Kao, S.-Y.3    Li, C.4    Kohane, I.5    Chan, J.6    Yankner, B.A.7
  • 20
    • 8344274464 scopus 로고    scopus 로고
    • Genome-scale expression profiling of Hutchinson-Gilford progeria syndrome reveals widespread transcriptional misregulation leading to mesodermal/mesenchymal defects and accelarated atherosclerosis
    • Csoka A. B., English S. B., Simkevich C. P., Ginzinger D. G., Butte A. J., Schatten G. P., Rothman F. G., Sedivy J. M., Genome-scale expression profiling of Hutchinson-Gilford progeria syndrome reveals widespread transcriptional misregulation leading to mesodermal/mesenchymal defects and accelarated atherosclerosis Aging Cell 2004 3 4 235 243
    • (2004) Aging Cell , vol.3 , Issue.4 , pp. 235-243
    • Csoka, A.B.1    English, S.B.2    Simkevich, C.P.3    Ginzinger, D.G.4    Butte, A.J.5    Schatten, G.P.6    Rothman, F.G.7    Sedivy, J.M.8
  • 24
    • 33746896640 scopus 로고    scopus 로고
    • Sex-specific regulation of aging and apoptosis
    • Tower J., Sex-specific regulation of aging and apoptosis Mechanisms of Ageing and Development 2006 127 9 705 718
    • (2006) Mechanisms of Ageing and Development , vol.127 , Issue.9 , pp. 705-718
    • Tower, J.1
  • 25
    • 0033610079 scopus 로고    scopus 로고
    • Gene expression profile of aging and its retardation by caloric restriction
    • Lee C.-K., Klopp R. G., Weindruch R., Prolla T. A., Gene expression profile of aging and its retardation by caloric restriction Science 1999 285 5432 1390 1393
    • (1999) Science , vol.285 , Issue.5432 , pp. 1390-1393
    • Lee, C.-K.1    Klopp, R.G.2    Weindruch, R.3    Prolla, T.A.4
  • 26
    • 63649164916 scopus 로고    scopus 로고
    • Defining the transcriptomic and proteomic profiles of rat ageing skeletal muscle by the use of a cDNA array, 2D- and Blue native-PAGE approach
    • Lombardi A., Silvestri E., Cioffi F., Senese R., Lanni A., Goglia F., de Lange P., Moreno M., Defining the transcriptomic and proteomic profiles of rat ageing skeletal muscle by the use of a cDNA array, 2D- and Blue native-PAGE approach Journal of Proteomics 2009 72 4 708 721
    • (2009) Journal of Proteomics , vol.72 , Issue.4 , pp. 708-721
    • Lombardi, A.1    Silvestri, E.2    Cioffi, F.3    Senese, R.4    Lanni, A.5    Goglia, F.6    De Lange, P.7    Moreno, M.8
  • 31
    • 0242321030 scopus 로고    scopus 로고
    • Proteomic identification of age-dependent protein nitration in rat skeletal muscle
    • Kanski J., Alterman M. A., Schneich C., Proteomic identification of age-dependent protein nitration in rat skeletal muscle Free Radical Biology and Medicine 2003 35 10 1229 1239
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.10 , pp. 1229-1239
    • Kanski, J.1    Alterman, M.A.2    Schneich, C.3
  • 32
    • 21244457292 scopus 로고    scopus 로고
    • Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry
    • Kanski J., Hong S. J., Schneich C., Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine- containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry The Journal of Biological Chemistry 2005 280 25 24261 24266
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 24261-24266
    • Kanski, J.1    Hong, S.J.2    Schneich, C.3
  • 33
    • 51249117834 scopus 로고    scopus 로고
    • Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation
    • O'Connell K., Doran P., Gannon J., Ohlendieck K., Lectin-based proteomic profiling of aged skeletal muscle: decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation European Journal of Cell Biology 2008 87 10 793 805
    • (2008) European Journal of Cell Biology , vol.87 , Issue.10 , pp. 793-805
    • O'Connell, K.1    Doran, P.2    Gannon, J.3    Ohlendieck, K.4
  • 35
    • 0033972709 scopus 로고    scopus 로고
    • Age-related changes of aqueous protein profiles in rat fast and slow twitch skeletal muscles
    • Cai D., Li M., Lee K., Lee K., Wong W., Chan K., Age-related changes of aqueous protein profiles in rat fast and slow twitch skeletal muscles Electrophoresis 2000 21 2 465 472
    • (2000) Electrophoresis , vol.21 , Issue.2 , pp. 465-472
    • Cai, D.1    Li, M.2    Lee, K.3    Lee, K.4    Wong, W.5    Chan, K.6
  • 37
    • 35449004149 scopus 로고    scopus 로고
    • Proteomic profiling reveals a severely perturbed protein expression pattern in aged skeletal muscle
    • O'Connell K., Gannon J., Doran P., Ohlendieck K., Proteomic profiling reveals a severely perturbed protein expression pattern in aged skeletal muscle International Journal of Molecular Medicine 2007 20 2 145 153
    • (2007) International Journal of Molecular Medicine , vol.20 , Issue.2 , pp. 145-153
    • O'Connell, K.1    Gannon, J.2    Doran, P.3    Ohlendieck, K.4
  • 38
    • 38949107303 scopus 로고    scopus 로고
    • Opposite pathobiochemical fate of pyruvate kinase and adenylate kinase in aged rat skeletal muscle as revealed by proteomic DIGE analysis
    • Doran P., O'Connell K., Gannon J., Kavanagh M., Ohlendieck K., Opposite pathobiochemical fate of pyruvate kinase and adenylate kinase in aged rat skeletal muscle as revealed by proteomic DIGE analysis Proteomics 2008 8 2 364 377
    • (2008) Proteomics , vol.8 , Issue.2 , pp. 364-377
    • Doran, P.1    O'Connell, K.2    Gannon, J.3    Kavanagh, M.4    Ohlendieck, K.5
  • 39
    • 0037289173 scopus 로고    scopus 로고
    • Comparative proteomics: Characterization of a two-dimensional gel electrophoresis system to study the effect of aging on mitochondrial proteins
    • Chang J., Van Remmen H., Cornell J., Richardson A., Ward W. F., Comparative proteomics: characterization of a two-dimensional gel electrophoresis system to study the effect of aging on mitochondrial proteins Mechanisms of Ageing and Development 2003 124 1 33 41
    • (2003) Mechanisms of Ageing and Development , vol.124 , Issue.1 , pp. 33-41
    • Chang, J.1    Van Remmen, H.2    Cornell, J.3    Richardson, A.4    Ward, W.F.5
  • 40
    • 0035866574 scopus 로고    scopus 로고
    • Parvalbumin expression is downregulated in rat fast-twitch skeletal muscles during aging
    • Cai D. Q., Li M., Lee K. K., Parvalbumin expression is downregulated in rat fast-twitch skeletal muscles during aging Archives of Biochemistry and Biophysics 2001 387 2 202 208
    • (2001) Archives of Biochemistry and Biophysics , vol.387 , Issue.2 , pp. 202-208
    • Cai, D.Q.1    Li, M.2    Lee, K.K.3
  • 42
    • 57149096282 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of muscle type-dependent and age-dependent protein carbonylation in rat skeletal muscle mitochondria
    • Feng J., Xie H., Meany D. L., Thompson L. V., Arriaga E. A., Griffin T. J., Quantitative proteomic profiling of muscle type-dependent and age-dependent protein carbonylation in rat skeletal muscle mitochondria Journals of Gerontology A 2008 63 11 1137 1152
    • (2008) Journals of Gerontology A , vol.63 , Issue.11 , pp. 1137-1152
    • Feng, J.1    Xie, H.2    Meany, D.L.3    Thompson, L.V.4    Arriaga, E.A.5    Griffin, T.J.6
  • 44
    • 0034464045 scopus 로고    scopus 로고
    • Thyroid hormone regulation of hepatic genes in vivo detected by complementary DNA microarray
    • Feng X., Jiang Y., Meltzer P., Yen P. M., Thyroid hormone regulation of hepatic genes in vivo detected by complementary DNA microarray Molecular Endocrinology 2000 14 7 947 955
    • (2000) Molecular Endocrinology , vol.14 , Issue.7 , pp. 947-955
    • Feng, X.1    Jiang, Y.2    Meltzer, P.3    Yen, P.M.4
  • 46
    • 4644310441 scopus 로고    scopus 로고
    • Multi-tissue gene-expression analysis in a mouse model of thyroid hormone resistance
    • article r31
    • Miller L. D., McPhie P., Suzuki H., Kato Y., Liu E. T., Cheng S. Y., Multi-tissue gene-expression analysis in a mouse model of thyroid hormone resistance Genome Biology 2004 5 5, article R31
    • (2004) Genome Biology , vol.5 , Issue.5
    • Miller, L.D.1    McPhie, P.2    Suzuki, H.3    Kato, Y.4    Liu, E.T.5    Cheng, S.Y.6
  • 47
    • 34250677676 scopus 로고    scopus 로고
    • Thyroid hormone responsive genes in the murine hepatocyte cell line AML 12
    • Ventura-Holman T., Mamoon A., Maher J. F., Thyroid hormone responsive genes in the murine hepatocyte cell line AML 12 Gene 2007 396 2 332 327
    • (2007) Gene , vol.396 , Issue.2 , pp. 332-327
    • Ventura-Holman, T.1    Mamoon, A.2    Maher, J.F.3
  • 48
    • 34547113767 scopus 로고    scopus 로고
    • Hepatic gene expression changes in hypothyroid juvenile mice: Characterization of a novel negative thyroid-responsive element
    • Dong H., Yauk C. L., Williams A., Lee A., Douglas G. R., Wade M. G., Hepatic gene expression changes in hypothyroid juvenile mice: characterization of a novel negative thyroid-responsive element Endocrinology 2007 148 8 3932 3940
    • (2007) Endocrinology , vol.148 , Issue.8 , pp. 3932-3940
    • Dong, H.1    Yauk, C.L.2    Williams, A.3    Lee, A.4    Douglas, G.R.5    Wade, M.G.6
  • 49
    • 0035945237 scopus 로고    scopus 로고
    • Two thyroid hormone-mediated gene expression patterns in vivo identified by cDNA expression arrays in rat
    • Weitzel J. M., Radtke C., Seitz H. J., Two thyroid hormone-mediated gene expression patterns in vivo identified by cDNA expression arrays in rat Nucleic Acids Research 2001 29 24 5148 5155
    • (2001) Nucleic Acids Research , vol.29 , Issue.24 , pp. 5148-5155
    • Weitzel, J.M.1    Radtke, C.2    Seitz, H.J.3
  • 50
    • 0034816497 scopus 로고    scopus 로고
    • Silencing of Wnt signaling and activation of multiple metabolic pathways in response to thyroid hormone-stimulated cell proliferation
    • Miller L. D., Park K. S., Guo Q. M., Alkharouf N. W., Malek R. L., Lee N. H., Liu E. T., Cheng S.-Y., Silencing of Wnt signaling and activation of multiple metabolic pathways in response to thyroid hormone-stimulated cell proliferation Molecular and Cellular Biology 2001 21 19 6626 6639
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.19 , pp. 6626-6639
    • Miller, L.D.1    Park, K.S.2    Guo, Q.M.3    Alkharouf, N.W.4    Malek, R.L.5    Lee, N.H.6    Liu, E.T.7    Cheng, S.-Y.8
  • 57
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M., Jensen O. N., Proteomic analysis of post-translational modifications Nature Biotechnology 2003 21 3 255 261
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 58
    • 33749662944 scopus 로고    scopus 로고
    • Protein modification in aging: An update
    • Schneich C., Protein modification in aging: an update Experimental Gerontology 2006 41 9 807 812
    • (2006) Experimental Gerontology , vol.41 , Issue.9 , pp. 807-812
    • Schneich, C.1
  • 59
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J. V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M., Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 2006 127 3 635 648
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    MacEk, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 60
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K., Marth J. D., Glycosylation in cellular mechanisms of health and disease Cell 2006 126 5 855 867
    • (2006) Cell , vol.126 , Issue.5 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 61
    • 33746266614 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • Freeze H. H., Genetic defects in the human glycome Nature Reviews Genetics 2006 7 8 660 674
    • (2006) Nature Reviews Genetics , vol.7 , Issue.8 , pp. 660-674
    • Freeze, H.H.1
  • 63
    • 0347134600 scopus 로고    scopus 로고
    • Thylakoid membrane at altered metabolic state: Challenging the forgotten realms of the proteome
    • Rexroth S., Meyer zu Tittingdorf J. M. W., Krause F., Dencher N. A., Seelert H., Thylakoid membrane at altered metabolic state: challenging the forgotten realms of the proteome Electrophoresis 2003 24 16 2814 2823
    • (2003) Electrophoresis , vol.24 , Issue.16 , pp. 2814-2823
    • Rexroth, S.1    Meyerzu Tittingdorf, J.M.W.2    Krause, F.3    Dencher, N.A.4    Seelert, H.5
  • 64
    • 33745943572 scopus 로고    scopus 로고
    • Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes
    • Krause F., Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes Electrophoresis 2006 27 13 2759 2781
    • (2006) Electrophoresis , vol.27 , Issue.13 , pp. 2759-2781
    • Krause, F.1
  • 66
    • 48949119270 scopus 로고    scopus 로고
    • Native-DIGE: A new look at the mitochondrial membrane proteome
    • Dani D., Dencher N. A., Native-DIGE: a new look at the mitochondrial membrane proteome Biotechnology Journal 2008 3 6 817 822
    • (2008) Biotechnology Journal , vol.3 , Issue.6 , pp. 817-822
    • Dani, D.1    Dencher, N.A.2
  • 68
    • 73149108205 scopus 로고    scopus 로고
    • Proteomic DIGE analysis of the mitochondria-enriched fraction from aged rat skeletal muscle
    • O'Connell K., Ohlendieck K., Proteomic DIGE analysis of the mitochondria-enriched fraction from aged rat skeletal muscle Proteomics 2009 9 24 5509 5524
    • (2009) Proteomics , vol.9 , Issue.24 , pp. 5509-5524
    • O'Connell, K.1    Ohlendieck, K.2
  • 69
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schgger H., Pfeiffer K., Supercomplexes in the respiratory chains of yeast and mammalian mitochondria The EMBO Journal 2000 19 8 1777 1783
    • (2000) The EMBO Journal , vol.19 , Issue.8 , pp. 1777-1783
    • Schgger, H.1    Pfeiffer, K.2
  • 73
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: Diversity for shared tasks
    • Robyr D., Wolffe A. P., Wahli W., Nuclear hormone receptor coregulators in action: diversity for shared tasks Molecular Endocrinology 2000 14 3 329 347
    • (2000) Molecular Endocrinology , vol.14 , Issue.3 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 74
    • 0033859843 scopus 로고    scopus 로고
    • The mechanism of action of thyroid hormones
    • Zhang J., Lazar M. A., The mechanism of action of thyroid hormones Annual Review of Physiology 2000 62 439 466
    • (2000) Annual Review of Physiology , vol.62 , pp. 439-466
    • Zhang, J.1    Lazar, M.A.2
  • 75
    • 33846647989 scopus 로고    scopus 로고
    • Thyroid hormones signaling is getting more complex: STORMs are coming
    • Flamant F., Gauthier K., Samarut J., Thyroid hormones signaling is getting more complex: STORMs are coming Molecular Endocrinology 2007 21 2 321 333
    • (2007) Molecular Endocrinology , vol.21 , Issue.2 , pp. 321-333
    • Flamant, F.1    Gauthier, K.2    Samarut, J.3
  • 76
    • 33745185772 scopus 로고    scopus 로고
    • Avian MyoD and c-Jun coordinately induce transcriptional activity of the 3,5,3′-triiodothyronine nuclear receptor c-ErbA 1 in proliferating myoblasts
    • Busson M., Daury L., Seyer P., Grandemange S., Pessemesse L., Casas F., Wrutniak-Cabello C., Cabello G., Avian MyoD and c-Jun coordinately induce transcriptional activity of the 3,5,3′-triiodothyronine nuclear receptor c-ErbA 1 in proliferating myoblasts Endocrinology 2006 147 7 3408 3418
    • (2006) Endocrinology , vol.147 , Issue.7 , pp. 3408-3418
    • Busson, M.1    Daury, L.2    Seyer, P.3    Grandemange, S.4    Pessemesse, L.5    Casas, F.6    Wrutniak-Cabello, C.7    Cabello, G.8
  • 77
    • 0025987831 scopus 로고
    • A novel mechanism of action for v-ErbA: Abrogation of the inactivation of transcription factor AP-1 by retinoic acid and thyroid hormone receptors
    • Desbois C., Aubert D., Legrand C., Pain B., Samarut J., A novel mechanism of action for v-ErbA: abrogation of the inactivation of transcription factor AP-1 by retinoic acid and thyroid hormone receptors Cell 1991 67 4 731 740
    • (1991) Cell , vol.67 , Issue.4 , pp. 731-740
    • Desbois, C.1    Aubert, D.2    Legrand, C.3    Pain, B.4    Samarut, J.5
  • 78
    • 0035900344 scopus 로고    scopus 로고
    • The triiodothyronine nuclear receptor c-ErbA 1 inhibits avian MyoD transcriptional activity in myoblasts
    • Daury L., Busson M., Casas F., Cassar-Malek I., Wrutniak-Cabello C., Cabello G., The triiodothyronine nuclear receptor c-ErbA 1 inhibits avian MyoD transcriptional activity in myoblasts FEBS Letters 2001 508 2 236 240
    • (2001) FEBS Letters , vol.508 , Issue.2 , pp. 236-240
    • Daury, L.1    Busson, M.2    Casas, F.3    Cassar-Malek, I.4    Wrutniak-Cabello, C.5    Cabello, G.6
  • 79
    • 0027416347 scopus 로고
    • Thyroid hormone receptors: Multiple forms, multiple possibilities
    • Lazar M. A., Thyroid hormone receptors: multiple forms, multiple possibilities Endocrine Reviews 1993 14 2 184 193
    • (1993) Endocrine Reviews , vol.14 , Issue.2 , pp. 184-193
    • Lazar, M.A.1
  • 80
    • 0028782187 scopus 로고
    • Mechanisms of disease: The molecular basis of thyroid hormone action
    • Brent G. A., Mechanisms of disease: the molecular basis of thyroid hormone action The New England Journal of Medicine 1994 331 13 847 853
    • (1994) The New England Journal of Medicine , vol.331 , Issue.13 , pp. 847-853
    • Brent, G.A.1
  • 81
    • 0023025178 scopus 로고
    • The c-erb-A protein is a high-affinity receptor for thyroid hormone
    • Sap J., Munoz A., Damm K., The c-erb-A protein is a high-affinity receptor for thyroid hormone Nature 1986 324 6098 635 640
    • (1986) Nature , vol.324 , Issue.6098 , pp. 635-640
    • Sap, J.1    Munoz, A.2    Damm, K.3
  • 82
    • 0042334868 scopus 로고    scopus 로고
    • Dominant inhibition of thyroid hormone action selectively in the pituitary of thyroid hormone-receptor- null mice abolishes the regulation of thyrotropin by thyroid hormone
    • Abel E. D., Moura E. G., Ahima R. S., Campos-Barros A., Pazos-Moura C. C., Boers M.-E., Kaulbach H. C., Forrest D., Wondisford F. E., Dominant inhibition of thyroid hormone action selectively in the pituitary of thyroid hormone-receptor- null mice abolishes the regulation of thyrotropin by thyroid hormone Molecular Endocrinology 2003 17 9 1767 1776
    • (2003) Molecular Endocrinology , vol.17 , Issue.9 , pp. 1767-1776
    • Abel, E.D.1    Moura, E.G.2    Ahima, R.S.3    Campos-Barros, A.4    Pazos-Moura, C.C.5    Boers, M.-E.6    Kaulbach, H.C.7    Forrest, D.8    Wondisford, F.E.9
  • 83
    • 0024535510 scopus 로고
    • Thyroid hormone regulation of the rat glycoprotein hormone α-subunit gene promoter activity
    • Burnside J., Sarling D. S., Carr F. E., Chin W. W., Thyroid hormone regulation of the rat glycoprotein hormone -subunit gene promoter activity The Journal of Biological Chemistry 1989 264 12 6886 6891 (Pubitemid 19114801)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.12 , pp. 6886-6891
    • Burnside, J.1    Sarling, D.S.2    Carr, F.E.3    Chin, W.W.4
  • 84
    • 0025837137 scopus 로고
    • A detailed functional and structural analysis of a major thyroid hormone inhibitory element in the human thyrotropin -subunit gene
    • Bodenner D. L., Mroczynski M. A., Weintraub B. D., Radovick S., Wondisford F. E., A detailed functional and structural analysis of a major thyroid hormone inhibitory element in the human thyrotropin -subunit gene The Journal of Biological Chemistry 1991 266 32 21666 21673
    • (1991) The Journal of Biological Chemistry , vol.266 , Issue.32 , pp. 21666-21673
    • Bodenner, D.L.1    Mroczynski, M.A.2    Weintraub, B.D.3    Radovick, S.4    Wondisford, F.E.5
  • 85
    • 0033950142 scopus 로고    scopus 로고
    • Functions of thyroid hormone receptors in mice
    • Forrest D., Vennstrm B., Functions of thyroid hormone receptors in mice Thyroid 2000 10 1 41 52
    • (2000) Thyroid , vol.10 , Issue.1 , pp. 41-52
    • Forrest, D.1    Vennstrm, B.2
  • 87
    • 0038731191 scopus 로고    scopus 로고
    • Thyroid hormone and uncoupling proteins
    • 8211;3
    • Lanni A., Moreno M., Lombardi A., Goglia F., Thyroid hormone and uncoupling proteins FEBS Letters 2003 543 1#8211;3 5 10
    • (2003) FEBS Letters , vol.543 , Issue.1 , pp. 5-10
    • Lanni, A.1    Moreno, M.2    Lombardi, A.3    Goglia, F.4
  • 89
    • 33645873573 scopus 로고    scopus 로고
    • Thermogenic mechanisms and their hormonal regulation
    • Silva J. E., Thermogenic mechanisms and their hormonal regulation Physiological Reviews 2006 86 2 435 464
    • (2006) Physiological Reviews , vol.86 , Issue.2 , pp. 435-464
    • Silva, J.E.1
  • 90
    • 0033040623 scopus 로고    scopus 로고
    • Action of thyroid hormones at the cellular level: The mitochondrial target
    • Goglia F., Moreno M., Lanni A., Action of thyroid hormones at the cellular level: the mitochondrial target FEBS Letters 1999 452 3 115 120
    • (1999) FEBS Letters , vol.452 , Issue.3 , pp. 115-120
    • Goglia, F.1    Moreno, M.2    Lanni, A.3
  • 92
    • 33645011201 scopus 로고    scopus 로고
    • Nuclear control of respiratory gene expression in mammalian cells
    • Scarpulla R. C., Nuclear control of respiratory gene expression in mammalian cells Journal of Cellular Biochemistry 2006 97 4 673 683
    • (2006) Journal of Cellular Biochemistry , vol.97 , Issue.4 , pp. 673-683
    • Scarpulla, R.C.1
  • 94
    • 32544445370 scopus 로고    scopus 로고
    • The mitochondrion as a primary site of action of steroid and thyroid hormones: Presence and action of steroid and thyroid hormone receptors in mitochondria of animal cells
    • Psarra A.-M. G., Solakidi S., Sekeris C. E., The mitochondrion as a primary site of action of steroid and thyroid hormones: presence and action of steroid and thyroid hormone receptors in mitochondria of animal cells Molecular and Cellular Endocrinology 2006 246 1-2 21 33
    • (2006) Molecular and Cellular Endocrinology , vol.246 , Issue.12 , pp. 21-33
    • Psarra, A.-M.G.1    Solakidi, S.2    Sekeris, C.E.3
  • 96
    • 0036667864 scopus 로고    scopus 로고
    • Thyroid hormone gene targets in ROS 17/2.8 osteoblast like cells identified by differential display analysis
    • Gouveia C. H., Schultz J. J., Jackson D. J., Williams G. R., Brent G. A., Thyroid hormone gene targets in ROS 17/2.8 osteoblast like cells identified by differential display analysis Thyroid 2002 12 8 663 671
    • (2002) Thyroid , vol.12 , Issue.8 , pp. 663-671
    • Gouveia, C.H.1    Schultz, J.J.2    Jackson, D.J.3    Williams, G.R.4    Brent, G.A.5
  • 97
    • 0029148491 scopus 로고
    • Identification of the mitochondrial NADH dehydrogenase subunit 3 (ND3) as a thyroid hormone regulated gene by whole genome PCR analysis
    • Iglesias T., Caubn J., Zaballos A., Bernal J., Munoz A., Identification of the mitochondrial NADH dehydrogenase subunit 3 (ND3) as a thyroid hormone regulated gene by whole genome PCR analysis Biochemical and Biophysical Research Communications 1995 210 3 995 1000
    • (1995) Biochemical and Biophysical Research Communications , vol.210 , Issue.3 , pp. 995-1000
    • Iglesias, T.1    Caubn, J.2    Zaballos, A.3    Bernal, J.4    Munoz, A.5
  • 98
    • 0026784329 scopus 로고
    • Regulation by thyroid hormone of nuclear and mitochondrial genes encoding subunits of cytochrome-c oxidase in rat liver and skeletal muscle
    • Wiesner R. J., Kurowski T. T., Zak R., Regulation by thyroid hormone of nuclear and mitochondrial genes encoding subunits of cytochrome-c oxidase in rat liver and skeletal muscle Molecular Endocrinology 1992 6 9 1458 1467
    • (1992) Molecular Endocrinology , vol.6 , Issue.9 , pp. 1458-1467
    • Wiesner, R.J.1    Kurowski, T.T.2    Zak, R.3
  • 100
    • 77953639982 scopus 로고    scopus 로고
    • Molecular aspects of thyroid hormone actions
    • Cheng S.-Y., Leonard J. L., Davis P. J., Molecular aspects of thyroid hormone actions Endocrine Reviews 2010 31 2 139 170
    • (2010) Endocrine Reviews , vol.31 , Issue.2 , pp. 139-170
    • Cheng, S.-Y.1    Leonard, J.L.2    Davis, P.J.3
  • 103
    • 0035752485 scopus 로고    scopus 로고
    • Thyroxine signal transduction in liver cells involves phospholipase C and phospholipase D activation. Genomic independent action of thyroid hormone
    • Kavok N. S., Krasilnikova O. A., Babenko N. A., Thyroxine signal transduction in liver cells involves phospholipase C and phospholipase D activation. Genomic independent action of thyroid hormone BMC Cell Biology 2001 2, article 5
    • (2001) BMC Cell Biology , vol.25
    • Kavok, N.S.1    Krasilnikova, O.A.2    Babenko, N.A.3
  • 104
    • 11244346968 scopus 로고    scopus 로고
    • Thyroid hormone induces rapid activation of Akt/protein kinase B-mammalian target of rapamycin-p70S6K cascade through phosphatidylinositol 3-kinase in human fibroblasts
    • Cao X., Kambe F., Moeller L. C., Refetoff S., Seo H., Thyroid hormone induces rapid activation of Akt/protein kinase B-mammalian target of rapamycin-p70S6K cascade through phosphatidylinositol 3-kinase in human fibroblasts Molecular Endocrinology 2005 19 1 102 112
    • (2005) Molecular Endocrinology , vol.19 , Issue.1 , pp. 102-112
    • Cao, X.1    Kambe, F.2    Moeller, L.C.3    Refetoff, S.4    Seo, H.5
  • 107
    • 36949022465 scopus 로고    scopus 로고
    • Thyroid hormone regulates the expression of SNAP-25 during rat brain development
    • Zhang H.-M., Su Q., Luo M., Thyroid hormone regulates the expression of SNAP-25 during rat brain development Molecular and Cellular Biochemistry 2008 307 1-2 169 175
    • (2008) Molecular and Cellular Biochemistry , vol.307 , Issue.12 , pp. 169-175
    • Zhang, H.-M.1    Su, Q.2    Luo, M.3
  • 108
    • 47949083180 scopus 로고    scopus 로고
    • Thyroid hormone action in the adult brain: Gene expression profiling of the effects of single and multiple doses of triiodo-L-thyronine in the rat striatum
    • Diez D., Grijota-Martinez C., Agretti P., De Marco G., Tonacchera M., Pinchera A., De Escobar G. M., Bernal J., Morte B., Thyroid hormone action in the adult brain: gene expression profiling of the effects of single and multiple doses of triiodo-L-thyronine in the rat striatum Endocrinology 2008 149 8 3989 4000
    • (2008) Endocrinology , vol.149 , Issue.8 , pp. 3989-4000
    • Diez, D.1    Grijota-Martinez, C.2    Agretti, P.3    De Marco, G.4    Tonacchera, M.5    Pinchera, A.6    De Escobar, G.M.7    Bernal, J.8    Morte, B.9
  • 112
    • 0027428750 scopus 로고
    • Developmental, nutritional, and hormonal regulation of tissue-specific expression of the genes encoding various acyl-CoA dehydrogenases and -subunit of electron transfer flavoprotein in rat
    • Nagao M., Parimoo B., Tanaka K., Developmental, nutritional, and hormonal regulation of tissue-specific expression of the genes encoding various acyl-CoA dehydrogenases and -subunit of electron transfer flavoprotein in rat The Journal of Biological Chemistry 1993 268 32 24114 24124
    • (1993) The Journal of Biological Chemistry , vol.268 , Issue.32 , pp. 24114-24124
    • Nagao, M.1    Parimoo, B.2    Tanaka, K.3
  • 114
    • 0019412170 scopus 로고
    • Regulation of pathways of ornithine metabolism. Effects of thyroid hormone and diabetes on the activity of enzymes at the ornithine crossroads in rat liver
    • Sochor M., McLean P., Brown J., Greenbaum A. L., Regulation of pathways of ornithine metabolism. Effects of thyroid hormone and diabetes on the activity of enzymes at the ornithine crossroads in rat liver Enzyme 1981 26 1 15 23
    • (1981) Enzyme , vol.26 , Issue.1 , pp. 15-23
    • Sochor, M.1    McLean, P.2    Brown, J.3    Greenbaum, A.L.4
  • 115
    • 0024477921 scopus 로고
    • Effect of hypothyroidism on the sensitivity of glycolysis and glycogen synthesis to insulin in the soleus muscle of the rat
    • Dimitriadis G. D., Leighton B., Parry-Billings M., West D., Newsholme E. A., Effect of hypothyroidism on the sensitivity of glycolysis and glycogen synthesis to insulin in the soleus muscle of the rat Biochemical Journal 1989 257 2 369 373
    • (1989) Biochemical Journal , vol.257 , Issue.2 , pp. 369-373
    • Dimitriadis, G.D.1    Leighton, B.2    Parry-Billings, M.3    West, D.4    Newsholme, E.A.5
  • 116
    • 2442610624 scopus 로고    scopus 로고
    • Tropomyosin interacts with phosphorylated HSP27 in agonist-induced contraction of smooth muscle
    • Somara S., Bitar K. N., Tropomyosin interacts with phosphorylated HSP27 in agonist-induced contraction of smooth muscle American Journal of Physiology 2004 286 6 C1290 C1301
    • (2004) American Journal of Physiology , vol.286 , Issue.6
    • Somara, S.1    Bitar, K.N.2
  • 117
    • 30344477634 scopus 로고    scopus 로고
    • Induction of heat shock proteins may combat insulin resistance
    • McCarty M. F., Induction of heat shock proteins may combat insulin resistance Medical Hypotheses 2006 66 3 527 534
    • (2006) Medical Hypotheses , vol.66 , Issue.3 , pp. 527-534
    • McCarty, M.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.