Cited by 1,384Thyroid Disorders and TreatmentsEstrogen and related hormone effectsThyroid Cancer Diagnosis and Treatment

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Molecular Aspects of Thyroid Hormone Actions

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Cheng, Sheue-Yann, Leonard, Jack L., Davis, Paul J.·2010·Endocrine Reviews

DOI 10.1210/er.2009-0007PMC PMC2852208

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Abstract

Cellular actions of thyroid hormone may be initiated within the cell nucleus, at the plasma membrane, in cytoplasm, and at the mitochondrion. Thyroid hormone nuclear receptors (TRs) mediate the biological activities of T(3) via transcriptional regulation. Two TR genes, alpha and beta, encode four T(3)-binding receptor isoforms (alpha1, beta1, beta2, and beta3). The transcriptional activity of TRs is regulated at multiple levels. Besides being regulated by T(3), transcriptional activity is regulated by the type of thyroid hormone response elements located on the promoters of T(3) target genes, by the developmental- and tissue-dependent expression of TR isoforms, and by a host of nuclear coregulatory proteins. These nuclear coregulatory proteins modulate the transcription activity of TRs in a T(3)-dependent manner. In the absence of T(3), corepressors act to repress the basal transcriptional activity, whereas in the presence of T(3), coactivators function to activate transcription. The critical role of TRs is evident in that mutations of the TRbeta gene cause resistance to thyroid hormones to exhibit an array of symptoms due to decreasing the sensitivity of target tissues to T(3). Genetically engineered knockin mouse models also reveal that mutations of the TRs could lead to other abnormalities beyond resistance to thyroid hormones, including thyroid cancer, pituitary tumors, dwarfism, and metabolic abnormalities. Thus, the deleterious effects of mutations of TRs are more severe than previously envisioned. These genetic-engineered mouse models provide valuable tools to ascertain further the molecular actions of unliganded TRs in vivo that could underlie the pathogenesis of hypothyroidism. Actions of thyroid hormone that are not initiated by liganding of the hormone to intranuclear TR are termed nongenomic. They may begin at the plasma membrane or in cytoplasm. Plasma membrane-initiated actions begin at a receptor on integrin alphavbeta3 that activates ERK1/2 and culminate in local membrane actions on ion transport systems, such as the Na(+)/H(+) exchanger, or complex cellular events such as cell proliferation. Concentration of the integrin on cells of the vasculature and on tumor cells explains recently described proangiogenic effects of iodothyronines and proliferative actions of thyroid hormone on certain cancer cells, including gliomas. Thus, hormonal events that begin nongenomically result in effects in DNA-dependent effects. l-T(4) is an agonist at the plasma membrane without conversion to T(3). Tetraiodothyroacetic acid is a T(4) analog that inhibits the actions of T(4) and T(3) at the integrin, including angiogenesis and tumor cell proliferation. T(3) can activate phosphatidylinositol 3-kinase by a mechanism that may be cytoplasmic in origin or may begin at integrin alphavbeta3. Downstream consequences of phosphatidylinositol 3-kinase activation by T(3) include specific gene transcription and insertion of Na, K-ATPase in the plasma membrane and modulation of the activity of the ATPase. Thyroid hormone, chiefly T(3) and diiodothyronine, has important effects on mitochondrial energetics and on the cytoskeleton. Modulation by the hormone of the basal proton leak in mitochondria accounts for heat production caused by iodothyronines and a substantial component of cellular oxygen consumption. Thyroid hormone also acts on the mitochondrial genome via imported isoforms of nuclear TRs to affect several mitochondrial transcription factors. Regulation of actin polymerization by T(4) and rT(3), but not T(3), is critical to cell migration. This effect has been prominently demonstrated in neurons and glial cells and is important to brain development. The actin-related effects in neurons include fostering neurite outgrowth. A truncated TRalpha1 isoform that resides in the extranuclear compartment mediates the action of thyroid hormone on the cytoskeleton.

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Lin, H., Tang, H.-Y., Shih, A., Keating, T., Cao, G., Davis, P. J., & Davis, F. B. (2006) · Steroids · doi:10.1016/j.steroids.2006.11.014 · Cited by 132
Self-citation
Retracted
The Proangiogenic Action of Thyroid Hormone Analogue GC-1 Is Initiated at an Integrin: [RETRACTED]
(2005) · Journal of Cardiovascular Pharmacology · doi:10.1097/01.fjc.0000175438.94906.a0 · Cited by 85
Retracted
Integrins: Versatility, modulation, and signaling in cell adhesion
Hynes, R. O. (1992) · Cell · doi:10.1016/0092-8674(92)90115-s · Cited by 9,857
The Steroid and Thyroid Hormone Receptor Superfamily
Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,394
Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
The Molecular Biology of Axon Guidance
Tessier‐Lavigne, M., & Goodman, C. S. (1996) · Science · doi:10.1126/science.274.5290.1123 · Cited by 3,311
Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily
Oñate, S. A., Tsai, S. Y., Tsai, M., & O’Malley, B. W. (1995) · Science · doi:10.1126/science.270.5240.1354 · Cited by 2,398
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
EGFR Antagonists in Cancer Treatment
Ciardiello, F., & Tortora, G. (2008) · New England Journal of Medicine · doi:10.1056/nejmra0707704 · Cited by 2,095
Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
Hörlein, A., Näär, A. M., Heinzel, T., Torchia, J., Gloss, B. R., Kurokawa, R., Ryan, A. K., Kamei, Y., Söderström, M., Glass, C. K., et al. (1995) · Nature · doi:10.1038/377397a0 · Cited by 2,072
Physiological and Molecular Basis of Thyroid Hormone Action
Yen, P. M. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.3.1097 · Cited by 2,011
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994
Nuclear Receptor Coregulators: Cellular and Molecular Biology
McKenna, N. J., Lanz, R. B., & O’Malley, B. W. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.3.0366 · Cited by 1,941
Transcriptional control of human p53-regulated genes
Riley, T., Sontag, E., Chen, P., & Levine, A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2395 · Cited by 1,921
A transcriptional co-repressor that interacts with nuclear hormone receptors
Chen, J. D., & Evans, R. M. (1995) · Nature · doi:10.1038/377454a0 · Cited by 1,794
The c-erb-A gene encodes a thyroid hormone receptor
Weinberger, C., Thompson, C. C., Ong, E. S., Lebo, R. V., Gruol, D. J., & Evans, R. M. (1986) · Nature · doi:10.1038/324641a0 · Cited by 1,477
Combinatorial Control of Gene Expression by Nuclear Receptors and Coregulators
McKenna, N. J., & O'Malley, B. W. (2002) · Cell · doi:10.1016/s0092-8674(02)00641-4 · Cited by 1,463
Integrins.
Ruoslahti, E. I. (1991) · Journal of Clinical Investigation · doi:10.1172/jci114957 · Cited by 1,391
Ligand Binding to Integrins
Plow, E. F., Haas, T. A., Zhang, L., Loftus, J. C., & Smith, J. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000003200 · Cited by 1,359
The c-erb-A protein is a high-affinity receptor for thyroid hormone
Sap, J., Múñoz, A., Damm, K., Goldberg, Y., Ghysdael, J., Leutz, A., Beug, H., & Vennström, B. (1986) · Nature · doi:10.1038/324635a0 · Cited by 1,314
The Promise and Perils of Wnt Signaling Through β-Catenin
Moon, R. T., Bowerman, B. A., Boutros, M., & Perrimon, N. (2002) · Science · doi:10.1126/science.1071549 · Cited by 970
A structural role for hormone in the thyroid hormone receptor
Wagner, R. L., Apriletti, J. W., McGrath, M. E., West, B. L., Baxter, J. D., & Fletterick, R. J. (1995) · Nature · doi:10.1038/378690a0 · Cited by 928
Structure and specificity of nuclear receptor–coactivator interactionsPreprint
Darimont, B. D., Wagner, R. L., Apriletti, J. W., Stallcup, M. R., Kushner, P. J., Baxter, J. D., Fletterick, R. J., & Yamamoto, K. R. (1998) · Genes & Development · doi:10.1101/gad.12.21.3343 · Cited by 921
Cellular and Molecular Basis of Deiodinase-Regulated Thyroid Hormone Signaling1
Gereben, B., Zavacki, A. M., Ribich, S., Kim, B. W., Huang, S. A., Simonides, W. S., Zeöld, A., & Bianco, A. C. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0019 · Cited by 891
Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone.
Forscher, P., & Smith, S. J. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.4.1505 · Cited by 854
PAX8-PPAR γ 1 Fusion in Oncogene Human Thyroid Carcinoma
Kroll, T. G., Sarraf, P., Pecciarini, L., Chen, C., Mueller, E., Spiegelman, B. M., & Fletcher, J. A. (2000) · Science · doi:10.1126/science.289.5483.1357 · Cited by 780
Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor.
Cavaillès, V., Dauvois, S., L’Horset, F., Lopez, G. N., Hoare, S., Kushner, P. J., & Parker, M. G. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00044.x · Cited by 740
Thyroid Hormone Action in the Heart
Kahaly, G. J., & DILLMANN, W. H. (2005) · Endocrine Reviews · doi:10.1210/er.2003-0033 · Cited by 710
Epidermal Growth Factor Receptor Targeting in Cancer
Mendelsohn, J. M., & Baselga, J. M. (2006) · Seminars in Oncology · doi:10.1053/j.seminoncol.2006.04.003 · Cited by 705
Axon Guidance and the Patterning of Neuronal Projections in Vertebrates
Dodd, J., & Jessell, T. M. (1988) · Science · doi:10.1126/science.3055291 · Cited by 699
The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors
Hu, X., & Lazar, M. A. (1999) · Nature · doi:10.1038/47069 · Cited by 642
The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3
Guenther, M. G., Barak, O., & Lazar, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6091-6101.2001 · Cited by 611
Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activationPreprint
McInerney, E. M., Rose, D. W., Flynn, S. E., Westin, S. K., Mullen, T.-M., Krones, A., Inostroza, J. A., Torchia, J., Nolte, R. T., Assa‐Munt, N., et al. (1998) · Genes & Development · doi:10.1101/gad.12.21.3357 · Cited by 610
Hormone-Dependent Coactivator Binding to a Hydrophobic Cleft on Nuclear Receptors
Feng, W., Ribeiro, R. C. J., Wagner, R. L., Nguyen, H. T., Apriletti, J. W., Fletterick, R. J., Baxter, J. D., Kushner, P. J., & West, B. L. (1998) · Science · doi:10.1126/science.280.5370.1747 · Cited by 579
Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex.
Fondell, J. D., Ge, H., & Roeder, R. G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8329 · Cited by 578
Isolation and Characterization of a Pituitary Tumor-Transforming Gene (PTTG)
Pei, L., & Melmed, S. K. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.4.9911 · Cited by 568
Integrin αVβ3 Contains a Cell Surface Receptor Site for Thyroid Hormone that Is Linked to Activation of Mitogen-Activated Protein Kinase and Induction of Angiogenesis
Bergh, J. J., Lin, H., Lansing, L., Mohamed, S. N., Davis, F. B., Mousa, S. A., & Davis, P. J. (2005) · Endocrinology · doi:10.1210/en.2005-0102 · Cited by 563
Self-citation
Distinct interactions of PML-RARα and PLZF-RARα with co-repressors determine differential responses to RA in APL
He, L.-Z., Guidez, F., Tribioli, C., Peruzzi, D., Ruthardt, M., Zelent, A., & Pandolfi, P. P. (1998) · Nature Genetics · doi:10.1038/ng0298-126 · Cited by 555
Spatial and temporal expression of alpha- and beta-thyroid hormone receptor mRNAs, including the beta 2-subtype, in the developing mammalian nervous system
Bradley, D. J., Towle, H. C., & Young, W. S. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-06-02288.1992 · Cited by 530
The SRC family of nuclear receptor coactivators
Leo, C., & Chen, J. D. (2000) · Gene · doi:10.1016/s0378-1119(00)00024-x · Cited by 519
Molecular determinants of nuclear receptor-corepressor interactionPreprint
Perissi, V., Staszewski, L. M., McInerney, E. M., Kurokawa, R., Krones, A., Rose, D. W., L., L. M., Milburn, M. V., Glass, C. K., & Rosenfeld, M. G. (1999) · Genes & Development · doi:10.1101/gad.13.24.3198 · Cited by 514
Abnormal heart rate and body temperature in mice lacking thyroid hormone receptor α1
Wikström, L., Johansson, C., Saltó, C., Barlow, C., Campos‐Barros, Á., Baas, F., Forrest, D., Thorén, P., & Vennström, B. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.455 · Cited by 513
Combinatorial Roles of the Nuclear Receptor Corepressor in Transcription and Development
Jepsen, K., Hermanson, O., Onami, T. M., Gleiberman, A. S., Lunyak, V. V., McEvilly, R. J., Kurokawa, R., Kumar, V., Liu, F. C., Seto, E., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00064-7 · Cited by 511
Nuclear Receptor Coregulators: Judges, Juries, and Executioners of Cellular Regulation
Lonard, D. M., & O’Malley, B. W. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.012 · Cited by 507
Review of the in Vivo Functions of the p160 Steroid Receptor Coactivator Family
Xu, J., & Li, Q. (2003) · Molecular Endocrinology · doi:10.1210/me.2003-0116 · Cited by 493
Tissue Differences in the Concentration of Triiodothyronine Nuclear Binding Sites in the Rat: Liver, Kidney, Pituitary, Heart, Brain, Spleen and Testis
Oppenheimer, J. H., Schwartz, H. L., & Surks, M. I. (1974) · Endocrinology · doi:10.1210/endo-95-3-897 · Cited by 468
The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion
Yuan, C., Ito, M., Fondell, J. D., Fu, Z.-Y., & Roeder, R. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.7939 · Cited by 454
Mice devoid of all known thyroid hormone receptors are viable but exhibit disorders of the pituitary-thyroid axis, growth, and bone maturationPreprint
Gothe, S., Wang, Z., Ng, L., Kindblom, J. M., Campos‐Barros, Á., Ohlsson, C., Vennström, B., & Forrest, D. (1999) · Genes & Development · doi:10.1101/gad.13.10.1329 · Cited by 445
Purification and functional characterization of the human N‐CoR complex: the roles of HDAC3, TBL1 and TBLR1
Yoon, H., Chan, D. W., Huang, Z., Li, J., Fondell, J. D., Qin, J., & Wong, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg120 · Cited by 444
Recessive resistance to thyroid hormone in mice lacking thyroid hormone receptor beta: evidence for tissue‐specific modulation of receptor function.
Forrest, D., Hanebuth, E., Smeyne, R. J., Everds, N. E., Stewart, C. L., Wehner, J. M., & Curran, T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00664.x · Cited by 440
Pituitary Tumor Transforming Gene (PTTG) Expression in Pituitary Adenomas
Zhang, X., Horwitz, G. A., Heaney, A. P., Nakashima, M., Prezant, T. R., Bronstein, M. D., & Melmed, S. K. (1999) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.84.2.5432 · Cited by 440
Linking cyclins to transcriptional control
Coqueret, O. (2002) · Gene · doi:10.1016/s0378-1119(02)01055-7 · Cited by 433
ETO, a Target of t(8;21) in Acute Leukemia, Interacts with the N-CoR and mSin3 Corepressors
Lutterbach, B. A., Westendorf, J. J., Linggi, B. E., Patten, A. K., Moniwa, M., Davie, J., Huynh, K. D., Bardwell, V. J., Lavinsky, R. M., Rosenfeld, M. G., et al. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7176 · Cited by 432
Interaction of thyroid-hormone receptor with a conserved transcriptional mediator
Lee, J. W., Ryan, F., Swaffield, J. C., Johnston, S. A., & Moore, D. D. (1995) · Nature · doi:10.1038/374091a0 · Cited by 425
Role of STATs as downstream signal transducers in Src family kinase-mediated tumorigenesis
Silva, C. M. (2004) · Oncogene · doi:10.1038/sj.onc.1208159 · Cited by 412
The basal proton conductance of mitochondria depends on adenine nucleotide translocase content
Brand, M. D., Pakay, J. L., Ocloo, A., Kokoszka, J., Wallace, D. C., Brookes, P. S., & Cornwall, E. J. (2005) · Biochemical Journal · doi:10.1042/bj20050890 · Cited by 410
The efficiency and plasticity of mitochondrial energy transduction.
Brand, M. D. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330897 · Cited by 406
A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free systemPreprint
Rachez, C., Suldan, Z., Ward, J. O., Chang, C.-P. B., Burakov, D., Erdjument‐Bromage, H., Tempst, P., & Freedman, L. P. (1998) · Genes & Development · doi:10.1101/gad.12.12.1787 · Cited by 402
Ribonucleic acid synthesis during the early action of thyroid hormones
Tata, J., & Widnell, C. C. (1966) · Biochemical Journal · doi:10.1042/bj0980604 · Cited by 398
Thyroid Hormone as a Determinant of Energy Expenditure and the Basal Metabolic Rate
Kim, B. W. (2008) · Thyroid · doi:10.1089/thy.2007.0266 · Cited by 396
Functions of gelsolin: motility, signaling, apoptosis, cancer
Kwiatkowski, D. J. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80012-x · Cited by 380
Rapid nongenomic actions of thyroid hormone
Hiroi, Y., Kim, H.-H., Ying, H., Furuya, F., Huang, Z., Simoncini, T., Noma, K., Ueki, K., Nguyen, N.-H., Scanlan, T. S., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601600103 · Cited by 380
Self-citation
Disoriented pathfinding by pioneer neurone growth cones deprived of filopodia by cytochalasin treatment
Bentley, D., & Toroian‐Raymond, A. (1986) · Nature · doi:10.1038/323712a0 · Cited by 378
Thyroid hormone receptor β is essential for development of auditory function
Forrest, D., Erway, L. C., Ng, L., Altschuler, R. A., & Curran, T. (1996) · Nature Genetics · doi:10.1038/ng0796-354 · Cited by 370
Mechanisms of nongenomic actions of thyroid hormone
Davis, P. J., Leonard, J. L., & Davis, F. B. (2007) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2007.09.003 · Cited by 364
Self-citation
Growth of neurites without filopodial or lamellipodial activity in the presence of cytochalasin B.
Marsh, L., & Letourneau, P. C. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.99.6.2041 · Cited by 350
The T3Rα gene encoding a thyroid hormone receptor is essential for post‐natal development and thyroid hormone production
Fraichard, A., Chassande, O., Plateroti, M., Roux, J. P., Trouillas, J., Dehay, C., Legrand, C., Gauthier, K. C., Kédinger, M., Malaval, L., et al. (1997) · The EMBO Journal · doi:10.1093/emboj/16.14.4412 · Cited by 349
Nuclear receptor coregulators: multiple modes of modification.
Hermanson, O., Glass, C., & Rosenfeld, M. (2002) · Trends in endocrinology and metabolism · doi:10.1016/s1043-2760(01)00527-6 · Cited by 341
Genipin inhibits UCP2-mediated proton leak and acutely reverses obesity- and high glucose-induced β cell dysfunction in isolated pancreatic islets
Zhang, C., Parton, L. E., Ye, C. P., Krauss, S., Shen, R., Lin, C.-T., Porco, J. A. J., & Lowell, B. B. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.010 · Cited by 337
Neuronal Cytomechanics: The Actin-Based Motility of Growth Cones
Smith, S. J. (1988) · Science · doi:10.1126/science.3055292 · Cited by 329
Overexpression of the rat sarcoplasmic reticulum Ca2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation.
He, H., Giordano, F. J., Hilal-Dandan, R., Choi, D. J., Rockman, H. A., McDonough, P. M., Bluhm, W. F., Meyer, M., Sayen, M. R., Swanson, E., et al. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119544 · Cited by 323
Thyroid hormone receptors: lessons from knockout and knock-in mutant mice
Flamant, F., & Samarut, J. (2003) · Trends in Endocrinology & Metabolism · doi:10.1016/s1043-2760(02)00043-7 · Cited by 314
DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein.
Fisher, R. P., Lisowsky, T., Parisi, M. A., & Clayton, D. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50739-6 · Cited by 312
Alternative splicing generates messages encoding rat c-erbA proteins that do not bind thyroid hormone.
Mitsuhashi, T., Tennyson, G. E., & Nikodem, V. M. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.16.5804 · Cited by 304
Defining the Roles of the Iodothyronine Deiodinases: Current Concepts and Challenges
Germain, D. L. S., Galton, V. A., & Hernández, A. (2009) · Endocrinology · doi:10.1210/en.2008-1588 · Cited by 303
Laminin‐immunoreactive glia distinguish regenerative adult CNS systems from non‐regenerative ones.
Liesi, P. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03963.x · Cited by 297
Syndromes of reduced sensitivity to thyroid hormone: genetic defects in hormone receptors, cell transporters and deiodination
Refetoff, S., & Dumitrescu, A. M. (2007) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2007.03.005 · Cited by 294
Cloning and Characterization of Two Novel Thyroid Hormone Receptor β Isoforms
Williams, G. R. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8329-8342.2000 · Cited by 290
Motility and cytoskeletal organization of migrating cerebellar granule neurons
Rivas, R., & Hatten, M. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-02-00981.1995 · Cited by 279
The SRC-3/AIB1 Coactivator Is Degraded in a Ubiquitin- and ATP-Independent Manner by the REGγ Proteasome
Li, X., Lonard, D. M., Jung, S. Y., Malovannaya, A., Feng, Q. F., Qin, J., Tsai, S. Y., Tsai, M., & O’Malley, B. W. (2006) · Cell · doi:10.1016/j.cell.2005.11.037 · Cited by 274
Extracellular Matrix 2: Role of extracellular matrix molecules and their receptors in the nervous system
Venstrom, K. A., & Reichardt, L. F. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.11.8370483 · Cited by 269
Generalized resistance to thyroid hormone associated with a mutation in the ligand-binding domain of the human thyroid hormone receptor beta.
Sakurai, A., Takeda, K., Ain, K., Ceccarelli, P., Nakai, A., Seino, S., Bell, G. I., Refetoff, S., & DeGroot, L. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.8977 · Cited by 268
Mice with a targeted mutation in the thyroid hormone β receptor gene exhibit impaired growth and resistance to thyroid hormone
Kaneshige, M., Kaneshige, K., Zhu, X.-G., Dace, A., Garrett, L. J., Carter, T. A., Kazlauskaite, R., Pankratz, D. G., Wynshaw-Boris, A. J., Refetoff, S., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.230285997 · Cited by 268
Self-citation
THE NUCLEAR HORMONE RECEPTOR GENE SUPERFAMILY
Ribeiro, R. C. J., Kushner, P. J., & Baxter, J. D. (1995) · Annual Review of Medicine · doi:10.1146/annurev.med.46.1.443 · Cited by 268
Resistance to Thyroid Hormone
Weiss, R. E., & Refetoff, S. (2000) · Reviews in Endocrine and Metabolic Disorders · doi:10.1023/a:1010072605757 · Cited by 257
l -Thyroxine vs. 3,5,3′-triiodo- l -thyronine and cell proliferation: activation of mitogen-activated protein kinase and phosphatidylinositol 3-kinase
Lin, H., Sun, M., Tang, H.-Y., Lin, C., Luidens, M. K., Mousa, S. A., Incerpi, S., Drusano, G. L., Davis, F. B., & Davis, P. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00305.2008 · Cited by 255
Self-citation
Cellular Action of Thyroid Hormone on the Heart
DILLMANN, W. H. (2002) · Thyroid · doi:10.1089/105072502760143809 · Cited by 252
Do neurons in the vertebrate CNS migrate on laminin?
Liesi, P. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03755.x · Cited by 245
Thyroid Hormone Induces Rapid Activation of Akt/Protein Kinase B-Mammalian Target of Rapamycin-p70S6KCascade through Phosphatidylinositol 3-Kinase in Human Fibroblasts
Cao, X., Kambe, F., Moeller, L. C., Refetoff, S., & Seo, H. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0093 · Cited by 241
An unliganded thyroid hormone receptor causes severe neurological dysfunction
Hashimoto, K., Curty, F. H., Borges, P. P., Lee, C. E., Abel, E. D., Elmquist, J. K., Cohen, R., & Wondisford, F. E. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051454698 · Cited by 239
Expression of pituitary-tumour transforming gene in colorectal tumours
Heaney, A. P., Singson, R., McCabe, C. J., Nelson, V., Nakashima, M., & Melmed, S. K. (2000) · The Lancet · doi:10.1016/s0140-6736(99)10238-1 · Cited by 229
Deletion of the thyroid hormone receptor α1 prevents the structural alterations of the cerebellum induced by hypothyroidism
Morte, B., Manzano, J., Scanlan, T. S., Vennström, B., & Bernal, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.062413299 · Cited by 227
Adhesion signaling: How β-catenin interacts with its partners
Gottardi, C. J., & Gumbiner, B. M. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00473-0 · Cited by 227
Proangiogenic Action of Thyroid Hormone Is Fibroblast Growth Factor–Dependent and Is Initiated at the Cell Surface
Davis, F. B., Mousa, S. A., O’Connor, L., Mohamed, S. N., Lin, H., Cao, H. J., & Davis, P. J. (2004) · Circulation Research · doi:10.1161/01.res.0000130784.90237.4a · Cited by 225
Self-citation
Thyroxine Promotes Association of Mitogen-activated Protein Kinase and Nuclear Thyroid Hormone Receptor (TR) and Causes Serine Phosphorylation of TR
Davis, P. J., Shih, A., Lin, H., Martino, L. J., & Davis, F. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002560200 · Cited by 220
Self-citation
Thyroid hormone and breast carcinoma
Cristofanilli, M., Yamamura, Y., Kau, S., Bevers, T. B., Strom, S. S., Patangan, M., Hsu, L., Krishnamurthy, S., Theriault, R. L., & Hortobágyi, G. N. (2005) · Cancer · doi:10.1002/cncr.20881 · Cited by 219
Is astrocyte laminin involved in axon guidance in the mammalian CNS?
Liesi, P., & Silver, J. (1988) · Developmental Biology · doi:10.1016/0012-1606(88)90366-1 · Cited by 218
Thyroid Hormone Resistance Syndrome Manifests as an Aberrant Interaction between Mutant T3 Receptors and Transcriptional Corepressors
Yoh, S. M., Chatterjee, K., & Privalsky, M. L. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.4.9914 · Cited by 218
A Variant Form of the Nuclear Triiodothyronine Receptor c-ErbAα1 Plays a Direct Role in Regulation of Mitochondrial RNA Synthesis
Casas, F., Rochard, P., Rodier, A., Cassar‐Malek, I., Marchal-Victorion, S., Wiesner, R. J., Cabello, G., & Wrutniak‐Cabello, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.7913 · Cited by 217
Thyroid Hormone Causes Mitogen-Activated Protein Kinase-Dependent Phosphorylation of the Nuclear Estrogen Receptor
Tang, H., Lin, H., Zhang, S., Davis, F. B., & Davis, P. J. (2004) · Endocrinology · doi:10.1210/en.2004-0308 · Cited by 216
Self-citation
The gelsolin family of actin regulatory proteins: modular structures, versatile functions
McGough, A. M., Staiger, C. J., Min, J., & Simonetti, K. D. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00932-3 · Cited by 211
Activation and inactivation of thyroid hormone by deiodinases: Local action with general consequences
Gereben, B., Zeöld, A., Dentice, M., Salvatore, D., & Bianco, A. C. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7396-0 · Cited by 207
Actin regulation in endocytosis
Smythe, E., & Ayscough, K. R. (2006) · Journal of Cell Science · doi:10.1242/jcs.03247 · Cited by 205
Mechanisms of glial-guided neuronal migration in vitro and in vivo
Hatten, M. E., & Mason, C. A. (1990) · Cellular and Molecular Life Sciences · doi:10.1007/bf01939383 · Cited by 202
Large-scale chemical dissection of mitochondrial function
Wagner, B. K., Kitami, T., Gilbert, T. J., Peck, D., Ramanathan, A., Schreiber, S. L., Golub, T. R., & Mootha, V. K. (2008) · Nature Biotechnology · doi:10.1038/nbt1387 · Cited by 202
A 43-kDa Protein Related to c-Erb A α1 Is Located in the Mitochondrial Matrix of Rat Liver
Wrutniak‐Cabello, C., Cassar‐Malek, I., Marchal, S., Rascle, A., Heusser, S., Keller, J., Fléchon, J. E., Dau�a, M., Samarut, J., Ghysdael, J., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.27.16347 · Cited by 200
Alien, a Highly Conserved Protein with Characteristics of a Corepressor for Members of the Nuclear Hormone Receptor Superfamily
Dressel, U., Thormeyer, D., Altincicek, B., Paululat, A., Eggert, M., Schneider, S., Tenbaum, S. P., Renkawitz, R., & Baniahmad, A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3383 · Cited by 200
The basal proton conductance of skeletal muscle mitochondria from transgenic mice overexpressing or lacking uncoupling protein-3
Cadenas, S., Echtay, K. S., Harper, J. A., Jekabsons, M. B., Buckingham, J. A., Grau, E., Abuin, A., Chapman, H., Clapham, J. C., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109736200 · Cited by 199
The mitochondrial uncoupling proteins.
Ledesma, A., de Lacoba, M. G., & Rial, E. (2002) · Genome biology · doi:10.1186/gb-2002-3-12-reviews3015 · Cited by 197
Thyroid Hormone Effects on Mitochondrial Energetics
Harper, M.-E., & Seifert, E. L. (2008) · Thyroid · doi:10.1089/thy.2007.0250 · Cited by 194
A targeted dominant negative mutation of the thyroid hormone α1 receptor causes increased mortality, infertility, and dwarfism in mice
Kaneshige, M., Suzuki, H., Kaneshige, K., Cheng, J., Wimbrow, H. H., Barlow, C., Willingham, M. C., & Cheng, S.-Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261565798 · Cited by 194
Self-citation
hpttg, a human homologue of rat pttg, is overexpressed in hematopoietic neoplasms. Evidence for a transcriptional activation function of hPTTG
Domínguez, Á., Ramos‐Morales, F., Romero, F., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1202140 · Cited by 191
Mice with a Mutation in the Thyroid Hormone Receptor β Gene Spontaneously Develop Thyroid Carcinoma: A Mouse Model of Thyroid Carcinogenesis
Suzuki, H., Willingham, M. C., & Cheng, S.-Y. (2002) · Thyroid · doi:10.1089/105072502320908295 · Cited by 191
Self-citation
Multiple Mechanisms for Regulation of the Transcriptional Activity of Thyroid Hormone Receptors
Cheng, S.-Y. (2000) · Reviews in Endocrine and Metabolic Disorders · doi:10.1023/a:1010052101214 · Cited by 190
Self-citation
Cardiac Myocytes Ca2+ and Na+ Regulation in Normal and Failing Hearts
Bers, D. M., & Despa, S. I. (2006) · Journal of Pharmacological Sciences · doi:10.1254/jphs.cpj06001x · Cited by 187
Sarcoplasmic reticulum Ca2+-ATPase modulates cardiac contraction and relaxation
Frank, K. F. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(02)00694-6 · Cited by 185
The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressorPreprint
Potter, G. B., Beaudoin, G. M. J., DeRenzo, C., Zarach, J. M., Chen, S. H., & Thompson, C. C. (2001) · Genes & Development · doi:10.1101/gad.916701 · Cited by 184
Retardation of post‐natal development caused by a negatively acting thyroid hormone receptor α1
Tinnikov, A. A., Nordström, K., Thorén, P., Kindblom, J. M., Malin, S., Rozell, B., Adams, M., Rajanayagam, O., Pettersson, S., Ohlsson, C., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf523 · Cited by 183
Acting via a Cell Surface Receptor, Thyroid Hormone Is a Growth Factor for Glioma Cells
Davis, F. B., Tang, H., Shih, A., Keating, T., Lansing, L., Hercbergs, A. A., Fenstermaker, R. A., Mousa, S. A., Mousa, S. A., Davis, P. J., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4365 · Cited by 181
Self-citation
Membrane receptors mediating thyroid hormone action
Davis, P. J., Davis, F. B., & Cody, V. (2005) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2005.09.007 · Cited by 178
Self-citation
Identification of Transcripts Initiated from an Internal Promoter in the c-erbAα Locus That Encode Inhibitors of Retinoic Acid Receptor-α and Triiodothyronine Receptor Activities
Chassande, O., Fraichard, A., Gauthier, K. C., Flamant, F., Legrand, C., Savatier, P., Laudet, V., & Samarut, J. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.9.9972 · Cited by 177
Solubilized nuclear "receptors" for thyroid hormones. Physical characteristics and binding properties, evidence for multiple forms.
Latham, K. R., Ring, J. C., & Baxter, J. D. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32861-2 · Cited by 174
Tight Linkage between the Syndrome of Generalized Thyroid Hormone Resistance and the Human c-erbAβ Gene
Usala, S. J., Bale, A. E., Gesundheit, N., Weinberger, C., Lash, R. W., Wondisford, F. E., McBride, O. W., & Weintraub, B. D. (1988) · Molecular Endocrinology · doi:10.1210/mend-2-12-1217 · Cited by 169
A Thyroid Hormone Receptor α Gene Mutation (P398H) Is Associated with Visceral Adiposity and Impaired Catecholamine-stimulated Lipolysis in Mice
Liu, Y., Schultz, J. J., & Brent, G. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306120200 · Cited by 165
Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
MATTIAZZI, A. R., Mundiña‐Weilenmann, C., GUOXIANG, C., Vittone, L., & Kranias, E. G. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.08.010 · Cited by 163
No Evidence for a Basal, Retinoic, or Superoxide-induced Uncoupling Activity of the Uncoupling Protein 2 Present in Spleen or Lung Mitochondria
Couplan, E., del Mar Gonzalez-Barroso, M., Alves-Guerra, M. C., Ricquier, D., Goubern, M., & Bouillaud, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202535200 · Cited by 161
Thyroxine-dependent modulation of actin polymerization in cultured astrocytes. A novel, extranuclear action of thyroid hormone.
Siegrist-Kaiser, C. A., Juge-Aubry, C. E., Tranter, M. P., Ekenbarger, D. M., & Leonard, J. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34121-3 · Cited by 157
Self-citation
Patterns of Liver Gene Expression Governed by TRβ
Flores‐Morales, A., Gullberg, H., Fernández‐Pérez, L., Ståhlberg, N., Lee, N. H., Vennström, B., & Norstedt, G. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.6.0846 · Cited by 154
The role of migration in central nervous system neuronal development
Hatten, M. E. (1993) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(93)90033-u · Cited by 153
Functional Interference between Thyroid Hormone Receptor α (TRα) and Natural Truncated TRΔα Isoforms in the Control of Intestine Development
Plateroti, M., Gauthier, K. C., Domon–Dell, C., Freund, J., Samarut, J., & Chassande, O. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.14.4761-4772.2001 · Cited by 151
Pathophysiological Importance of Thyroid Hormone Transporters
Heuer, H., & Visser, T. J. (2009) · Endocrinology · doi:10.1210/en.2008-1518 · Cited by 148
Activation of phosphatidylinositol 3-kinase signaling by a mutant thyroid hormone β receptor
Furuya, F., Hanover, J. A., & Cheng, S.-Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510849103 · Cited by 147
Self-citation
Nuclear Cytoplasmic Shuttling by Thyroid Hormone Receptors
Baumann, C. T., Maruvada, P., Hager, G. L., & Yen, P. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011112200 · Cited by 147
Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors
Dace, A., Zhao, L., Park, K. S., Furuno, T., Takamura, N., Nakanishi, M., West, B. L., Hanover, J. A., & Cheng, S.-Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160257997 · Cited by 145
Self-citation
Overexpressed Pituitary Tumor-Transforming Gene Causes Aneuploidy in Live Human Cells
Yu, R., Lu, W., Chen, J., McCabe, C. J., & Melmed, S. K. (2003) · Endocrinology · doi:10.1210/en.2003-0305 · Cited by 138
Propylthiouracil-induced chemical hypothyroidism with high-dose tamoxifen prolongs survival in recurrent high grade glioma: a phase I/II study.
Hercbergs, A. A., Goyal, L. K., Suh, J. H., Lee, S., Reddy, C. A., Cohen, B. H., Stevens, G. H. J., Reddy, S. K., Peereboom, D. M., Elson, P. J., et al. (2003) · PubMed · Cited by 135
Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex
Zamir, I., Dawson, J., Lavinsky, R. M., Glass, C. K., Rosenfeld, M. G., & Lazar, M. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14400 · Cited by 135
Human Type 3 Iodothyronine Selenodeiodinase Is Located in the Plasma Membrane and Undergoes Rapid Internalization to Endosomes
Baqui, M. M. A., Botero, D., Gereben, B., Curcio, C., Harney, J. W., Salvatore, D., Sorimachi, K., Larsen, P. R., & Bianco, A. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210266200 · Cited by 133
Thyroid hormone mediated changes in gene expression can be initiated by cytosolic action of the thyroid hormone receptor β through the phosphatidylinositol 3-kinase pathway
Moeller, L. C., Cao, X., Dumitrescu, A. M., Seo, H., & Refetoff, S. (2006) · Nuclear Receptor Signaling · doi:10.1621/nrs.04020 · Cited by 133
Cytosolic Action of Thyroid Hormone Leads to Induction of Hypoxia-Inducible Factor-1α and Glycolytic Genes
Moeller, L. C., Dumitrescu, A. M., & Refetoff, S. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0542 · Cited by 131
A Thyrotoxic Skeletal Phenotype of Advanced Bone Formation in Mice with Resistance to Thyroid Hormone
O’Shea, P. J., Harvey, C. B., Suzuki, H., Kaneshige, M., Kaneshige, K., Cheng, S.-Y., & Williams, G. R. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0296 · Cited by 131
Self-citation
Molecular aspects of thyroid hormone transporters, including MCT8, MCT10, and OATPs, and the effects of genetic variation in these transporters
van der Deure, W. M., Peeters, R. P., & Visser, T. J. (2010) · Journal of Molecular Endocrinology · doi:10.1677/jme-09-0042 · Cited by 130
Molecular basis of resistance to thyroid hormone
Yen, P. M. (2003) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(03)00114-0 · Cited by 129
Resveratrol is pro-apoptotic and thyroid hormone is anti-apoptotic in glioma cells: both actions are integrin and ERK mediated
Lin, H., Tang, H., Keating, T., Wu, Y.-H., Shih, A., Hammond, D., Sun, M., Hercbergs, A. A., Davis, F. B., & Davis, P. J. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm239 · Cited by 128
Self-citation
Hypermetabolism in mice caused by the central action of an unliganded thyroid hormone receptor α1
Sjögren, M., Alkemade, A., Mittag, J., Nordström, K., Katz, A., Rozell, B., Westerblad, H., Arner, A., & Vennström, B. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601882 · Cited by 128
Functionally Impaired TR Mutants Are Present in Thyroid Papillary Cancer
Puzianowska‐Kuźnicka, M., Krystyniak, A., Madej, A., Cheng, S.-Y., & Nauman, J. A. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.87.3.8296 · Cited by 127
Self-citation
Rapid Nongenomic Effects of 3,5,3′-Triiodo-l-Thyronine on the Intracellular pH of L-6 Myoblasts Are Mediated by Intracellular Calcium Mobilization and Kinase Pathways
D’Arezzo, S., Incerpi, S., Davis, F. B., Acconcia, F., Marino, M., Farı́as, R. N., & Davis, P. J. (2004) · Endocrinology · doi:10.1210/en.2004-0890 · Cited by 126
Self-citation
Unliganded Thyroid Hormone Receptor α Can Target TATA-Binding Protein for Transcriptional Repression
Fondell, J. D., Brunel, F., Hisatake, K., & Roeder, R. G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.1.281 · Cited by 126
[Use of immobilization for the study of glyceraldehyde 3-phosphate dehydrogenase. Immobilized dimers of the enzyme].
Muronets, V. I., Golovina, T. O., & Nagradova, N. K. (1982) · PubMed · Cited by 124
Regulation of retinoid and thyroid hormone action through homodimeric and heterodimeric receptors
Zhang, X.-K., & Kahl, M. (1993) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(93)90105-n · Cited by 123
Regulation of cerebellar neuronal migration and neurite outgrowth by thyroxine and 3,3′,5′-triiodothyronine
Farwell, A. P., Dubord-Tomasetti, S. A., Pietrzykowski, A. Z., Stachelek, S. J., & Leonard, J. L. (2005) · Developmental Brain Research · doi:10.1016/j.devbrainres.2004.07.016 · Cited by 123
Self-citation
Rapid signaling at the plasma membrane by a nuclear receptor for thyroid hormone
Storey, N. M., Gentile, S., Ullah, H., Russo, A., Muessel, M. J., Erxleben, C. F. J., & Armstrong, D. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600089103 · Cited by 123
Homozygosity for a Dominant Negative Thyroid Hormone Receptor Gene Responsible for Generalized Resistance to Thyroid Hormone*
Ono, S., Schwartz, I. D., Mueller, O. T., Root, A. W., Usala, S. J., & Bercu, B. B. (1991) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-73-5-990 · Cited by 123
Effects of ligand and thyroid hormone receptor isoforms on hepatic gene expression profiles of thyroid hormone receptor knockout mice
Yen, P. M., Feng, X., Flamant, F., Chen, Y., Walker, R. L., Weiss, R. E., Chassande, O., Samarut, J., Refetoff, S., & Meltzer, P. S. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor862 · Cited by 123
Thyroid Hormone Promotes Serine Phosphorylation of p53 by Mitogen-Activated Protein Kinase
Shih, A., Lin, H., Davis, F. B., & Davis, P. J. (2001) · Biochemistry · doi:10.1021/bi001978b · Cited by 122
Self-citation
Structural and Dynamic Basis of Phospholamban and Sarcolipin Inhibition of Ca2+-ATPase
Traaseth, N. J., Ha, K. N., Verardi, R., Shi, L., Buffy, J. J., Masterson, L. R., & Veglia, G. (2007) · Biochemistry · doi:10.1021/bi701668v · Cited by 122
Atypical Expression of Type 2 Iodothyronine Deiodinase in Thyrotrophs Explains the Thyroxine-Mediated Pituitary Thyrotropin Feedback Mechanism
Christoffolete, M. A., Ribeiro, R., Singru, P., Fekete, C., da Silva, W. S., Gordon, D. F., Huang, S. A., Crescenzi, A., Harney, J. W., Ridgway, E. C., et al. (2006) · Endocrinology · doi:10.1210/en.2005-1300 · Cited by 118
Hormone-induced Translocation of Thyroid Hormone Receptors in Living Cells Visualized Using a Receptor Green Fluorescent Protein Chimera
Zhu, X., Hanover, J. A., Hager, G. L., & Cheng, S.-Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.42.27058 · Cited by 117
Self-citation
Somatic Mutation of TRβ Can Cause a Defect in Negative Regulation of TSH in a TSH-Secreting Pituitary Tumor
Ando, S., Sarlis, N. J., Oldfield, E. H., & Yen, P. M. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.11.7984 · Cited by 115
Dual Site Phospholamban Phosphorylation and Its Physiological Relevance in the Heart
Hagemann, D. (2002) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(01)00145-1 · Cited by 108
Tetraiodothyroacetic acid, a small molecule integrin ligand, blocks angiogenesis induced by vascular endothelial growth factor and basic fibroblast growth factor
Mousa, S. A., Bergh, J. J., Dier, E., Rebbaa, A., O’Connor, L. J., Yalçın, M., Aljada, A., Dyskin, E., Davis, F. B., Lin, H.-Y., et al. (2007) · Angiogenesis · doi:10.1007/s10456-007-9088-7 · Cited by 108
Self-citation
Thyroid Hormone-Regulated Actin Polymerization in Brain
Leonard, J. L., & Farwell, A. P. (1997) · Thyroid · doi:10.1089/thy.1997.7.147 · Cited by 108
Self-citation
Gelsolin‐induced epithelial cell invasion is dependent on Ras–Rac signaling
Corte, V. D., Bruyneel, E., Boucherie, C., Mareel, M., Vandekerckhove, J. S., & Gettemans, J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf680 · Cited by 107
Expression of mutant thyroid hormone nuclear receptors is associated with human renal clear cell carcinoma
Kamiya, Y. (2002) · Carcinogenesis · doi:10.1093/carcin/23.1.25 · Cited by 105
An Unliganded Thyroid Hormone β Receptor Activates the Cyclin D1/Cyclin-Dependent Kinase/Retinoblastoma/E2F Pathway and Induces Pituitary Tumorigenesis
Furumoto, H., Ying, H., Chandramouli, G., Zhao, L., Walker, R. L., Meltzer, P. S., Willingham, M. C., & Cheng, S.-Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.124-135.2005 · Cited by 105
Self-citation
Aberrant Alternative Splicing of Thyroid Hormone Receptor in a TSH-Secreting Pituitary Tumor Is A Mechanism for Hormone Resistance
Ando, S., Sarlis, N. J., Krishnan, J., Feng, X., Refetoff, S., Zhang, M. Q., Oldfield, E. H., & Yen, P. M. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.9.0687 · Cited by 104
Analysis of the steady-state and initial rate of doxorubicin efflux from a series of multidrug resistant cells expressing different levels of P-glycoprotein
Roepe, P. D. (1992) · Biochemistry · doi:10.1021/bi00165a003 · Cited by 103
An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1,6-bisphosphate
Ashizawa, K., McPhie, P., Lin, K., & Cheng, S. Y. (1991) · Biochemistry · doi:10.1021/bi00243a010 · Cited by 101
Self-citation
Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase.
Kato, H., Fukuda, T., Parkison, C., McPhie, P., & Cheng, S.-Y. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.7861 · Cited by 99
Self-citation
Effects of Resin or Charcoal Treatment on Fetal Bovine Serum and Bovine Calf Serum
Cao, Z. T., West, C., Norton-Wenzel, C. S., Rej, R., Davis, F. B., Davis, P. J., & Rej, R. (2009) · Endocrine Research · doi:10.3109/07435800903204082 · Cited by 98
Self-citation
PPARγ insufficiency promotes follicular thyroid carcinogenesis via activation of the nuclear factor-κB signaling pathway
Kato, Y., Ying, H., Zhao, L., Furuya, F., Araki, O., Willingham, M. C., & Cheng, S.-Y. (2005) · Oncogene · doi:10.1038/sj.onc.1209299 · Cited by 97
Self-citation
A proteomic survey of rat cerebral cortical synaptosomes
Witzmann, F. A., Arnold, R. J., Bai, F., Hrncirova, P., Kimpel, M. W., Mechref, Y. S., McBride, W. J., Novotný, M. V., Pedrick, N. M., Ringham, H. N., et al. (2005) · PROTEOMICS · doi:10.1002/pmic.200401102 · Cited by 96
Thyroid hormone receptor mutations and disease: beyond thyroid hormone resistance
Cheng, S.-Y. (2005) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2005.03.008 · Cited by 95
Self-citation
TR surfaces and conformations required to bind nuclear receptor corepressor.
Marimuthu, A., Feng, W., Tagami, T., Nguyen, H. T., Jameson, J., Fletterick, R. J., Baxter, J. D., & West, B. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.2.0777 · Cited by 95
Thyroxine-dependent regulation of integrin-laminin interactions in astrocytes
Farwell, A. P., Tranter, M. P., & Leonard, J. L. (1995) · Endocrinology · doi:10.1210/endo.136.9.7649099 · Cited by 95
Self-citation
Nuclear receptor corepressors
Lazar, M. A. (2003) · Nuclear Receptor Signaling · doi:10.1621/nrs.01001 · Cited by 94
Role of calmodulin in thyroid hormone stimulation in vitro of human erythrocyte Ca2+-ATPase activity.
Davis, F. B., Davis, P. J., & Blas, S. D. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110803 · Cited by 92
Self-citation
Glucose and triiodothyronine both induce malic enzyme in the rat hepatocyte culture: evidence that triiodothyronine multiplies a primary glucose-generated signal.
Mariash, C. N., McSwigan, C. R., Towle, H. C., Schwartz, H. L., & Oppenheimer, J. H. (1981) · Journal of Clinical Investigation · doi:10.1172/jci110401 · Cited by 91
Cyclin D1 Is a Ligand-independent Co-repressor for Thyroid Hormone Receptors
Lin, H., Zhao, L., & Cheng, S.-Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203380200 · Cited by 90
Self-citation
Extracellular matrix and neuronal movement
Liesi, P. (1990) · Cellular and Molecular Life Sciences · doi:10.1007/bf01939382 · Cited by 90
Thyroidal regulation of rat renal and hepatic Na,K-ATPase gene expression.
GICK, G. G., Ismail‐Beigi, F., & Edelman, I. S. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37434-9 · Cited by 89
Dynamic Nongenomic Actions of Thyroid Hormone in the Developing Rat Brain
Farwell, A. P., Dubord, S., Pietrzykowski, A. Z., & Leonard, J. L. (2006) · Endocrinology · doi:10.1210/en.2005-1272 · Cited by 89
Self-citation
Genetic and physiological analysis of the role of uncoupling proteins in human energy homeostasis
Pecqueur, C., Couplan, E., Bouillaud, F., & Ricquier, D. (2000) · Journal of Molecular Medicine · doi:10.1007/s001090000150 · Cited by 88
Aberrant accumulation of PTTG1 induced by a mutated thyroid hormone β receptor inhibits mitotic progression
Ying, H., Furuya, F., Zhao, L., Araki, O., West, B. L., Hanover, J. A., Willingham, M. C., & Cheng, S.-Y. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28598 · Cited by 86
Self-citation
Stoichiometry of Mitochondrial Transcripts and Regulation of Gene Expression by Mitochondrial Transcription Factor A
Garstka, H. L., Fäcke, M., Escribano, J., et al. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1493 · Cited by 86
Stimulation by Triiodothyronine of the In Vitro Uptake of Sugars by Rat Thymocytes
Segal, J., & Ingbar, S. H. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109329 · Cited by 85
Impaired Adipogenesis Caused by a Mutated Thyroid Hormone α 1 Receptor
Ying, H., Araki, O., Furuya, F., Kato, Y., & Cheng, S.-Y. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02189-06 · Cited by 85
Self-citation
3,3′,5-Triiodo-l-thyronine Up-regulation of Na,K-ATPase Activity and Cell Surface Expression in Alveolar Epithelial Cells Is Src Kinase- and Phosphoinositide 3-Kinase-dependent
Lei, J., Mariash, C. N., & Ingbar, D. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405497200 · Cited by 84
Oncogene Activation in Pituitary Tumors
Yu, R., & Melmed, S. K. (2001) · Brain Pathology · doi:10.1111/j.1750-3639.2001.tb00403.x · Cited by 84
Translational implications of nongenomic actions of thyroid hormone initiated at its integrin receptor
Davis, P. J., Davis, F. B., Lin, H., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00480.2009 · Cited by 83
Self-citation
Thyroid Hormone Regulates the Expression of Laminin in the Developing Rat Cerebellum1
Farwell, A. P., & Dubord, S. (1999) · Endocrinology · doi:10.1210/endo.140.9.7007 · Cited by 83
Regulation of β-Catenin by a Novel Nongenomic Action of Thyroid Hormone β Receptor
Guigon, C. J., Zhao, L., Lu, C., Willingham, M. C., & Cheng, S.-Y. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02192-07 · Cited by 82
Self-citation
Modulation of the transcriptional activity of thyroid hormone receptors by the tumor suppressor p53.
Yap, N., Yu, C., & Cheng, S.-Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4273 · Cited by 82
Self-citation
Short-Term Effects of Thyroid Hormones on the Na/H Antiport in L-6 Myoblasts: High Molecular Specificity for 3,3′,5-Triiodo- l -Thyronine1
Incerpi, S., Luly, P., Vito, P. D., & Farı́as, R. N. (1999) · Endocrinology · doi:10.1210/endo.140.2.6535 · Cited by 81
Triiodothyronine Induces the Transcription of the Uncoupling Protein Gene and Stabilizes Its mRNA in Fetal Rat Brown Adipocyte Primary Cultures
Guerra, C. E., Roncero, C., Porrás, A., Fernández, M., & Benito, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.4.2076 · Cited by 81
Interactions Between Estrogen and Growth Factor Receptors in Human Breast Cancers and the Tumor-Associated Vasculature
Pietras, R. J. (2003) · The Breast Journal · doi:10.1046/j.1524-4741.2003.09510.x · Cited by 80
Stimulation by thyroid hormone analogues of red blood cell Ca2+-ATPase activity in vitro. Correlations between hormone structure and biological activity in a human cell system.
Davis, F. B., Cody, V., Davis, P. J., Borzynski, L. J., & Blas, S. D. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44185-8 · Cited by 79
Self-citation
Pituitary tumour transforming gene (PTTG) induces genetic instability in thyroid cells
Kim, D., Pemberton, H. N., Stratford, A. L., Buelaert, K., Watkinson, J. C., Lopes, V. R., Franklyn, J. A., & McCabe, C. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208659 · Cited by 79
Transforming Events in Thyroid Tumorigenesis and Their Association with Follicular Lesions
Heaney, A. P., Nelson, V., Fernando, M. A., et al. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.10.7886 · Cited by 78
Mitochondrial localization and activity of P-glycoprotein in doxorubicin-resistant K562 cells
Munteanu, E., Verdier, M., Grandjean‐Forestier, F., et al. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.01.006 · Cited by 76

Research works printed but not linked: 2

Yalcin, 2008, (Abstract 110), Thyroid, 18, S46
El Eter, 2007, Role of thyroid hormone analogs in angiogenesis and the development of collaterals in rabbit hind limb ischemia model, J Thromb Haemost, 5, 375

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Authors: Cheng, S.-Y., Leonard, J. L., & Davis, P. J.
Affiliations: National Institutes of Health (US)
University of Massachusetts Chan Medical School (US)
Albany Medical College (US)
ORCID: Cheng, Sheue-Yann
Leonard, Jack L.
Davis, Paul J.
Venue: Endocrine Reviews
Publisher: The Endocrine Society
Published: 2010-04-01
Volume: 31
Issue: 2
Pages: 139-170
ISSN: 0163-769X (ISSN-L)
1945-7189
DOI: 10.1210/er.2009-0007
PMC: PMC2852208
OpenAlex: W2021932599
Cited by: 1,384
References: 299
Citations by year: 2026: 39 · 2025: 78 · 2024: 68 · 2023: 95 · 2022: 104 · 2021: 90 · 2020: 101 · 2019: 91 · 2018: 70 · 2017: 100 · 2016: 93 · 2015: 82 · 2014: 120 · 2013: 91 · 2012: 62
FWCI: 11.44
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Endocrine Reviews (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Cancer Institute
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Cancer Diagnosis and Treatment
Keywords: thyroid hormones, thyroid hormone receptor, thyroid hormone receptor beta, TRα, transcriptional regulation, thyroid hormone response element, transcriptional coactivator, corepressors, thyroid hormone resistance, knockin mouse model, hypothyroidism, nongenomic thyroid hormone action, integrin αvβ3, ERK signaling, Na+/H+ exchanger, angiogenesis, glioma proliferation, tetraiodothyroacetic acid, levothyroxine
MeSH terms: Animals, Humans, Receptors, Thyroid Hormone, Thyroid Hormones, Thyroxine, Triiodothyronine

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Molecular Aspects of Thyroid Hormone Actions

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