Molecular Aspects of Thyroid Hormone Actions
Open accessAbstract
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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TH, in the form of T3, classically acts by binding to cytosolic TH receptors (TRα1, TRβ1, and TRβ2) that bind to TH response elements on DNA and regulate expression of TH target genes.
“TH, in the form of T3, has classically been considered to act by binding to cytosolic TH receptors (TR) (TRα1, TRβ1, and TRβ2) that bind to TH response elements on the DNA and regulate expression of TH target genes (canonical TH/TR action) (26,27).”
From Evidence-Based Use of Levothyroxine/Liothyronine Combinations in Treating Hypothyroidism: A Consensus Document (2021) · cites this paper as [27]
The Abstract describes T3-binding TR isoforms, their interaction with thyroid hormone response elements, and regulation of target-gene transcription. But the protein-trafficking section says the canonical view placed these receptors in the nucleus; it treats their presence in the cytoplasm as a surprising finding, not the location of canonical DNA-mediated action. The claim's description of the receptors as cytosolic is therefore not supported. (LLM, conf=0.90)
Experimental — accuracy not yet measuredBoth T3 and T4 following conversion into T3 bind to specific intracellular TR receptors exerting a repressive action on various genes, including TSHβ and to a lesser degree α-subunit.
“Both T3 and T4 following its conversion into T3 bind to specific intracellular TR receptors exerting a repressive action on various genes, including TSHβ and, to a lesser degree, α-subunit (47–52).”
From Homeostatic control of the thyroid-pituitary axis: perspectives for diagnosis and treatment (2015) · cites this paper as [48]
TH, in the form of T3, has classically been considered to act by binding to cytosolic TH receptors (TRα1, TRβ1, and TRβ2) that bind to TH response elements on DNA and regulate expression of TH target genes.
“TH, in the form of T3, has classically been considered to act by binding to cytosolic TH receptors (TR) (TRα1, TRβ1, and TRβ2) that bind to TH response elements on the DNA and regulate expression of TH target genes (canonical TH/TR action) [26, 27].”
From Evidence-Based Use of Levothyroxine/Liothyronine Combinations in Treating Hypothyroidism: A Consensus Document (2021) · cites this paper as [27]
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2 retracted
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 · see citing works
Self-citationRetractedThe 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 · see citing works
RetractedIntegrins: Versatility, modulation, and signaling in cell adhesion
Hynes, R. O. (1992) · Cell · doi:10.1016/0092-8674(92)90115-s · Cited by 9,857 · see citing works
The Steroid and Thyroid Hormone Receptor Superfamily
Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,442 · see citing works
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 · see citing works
The Molecular Biology of Axon Guidance
Tessier‐Lavigne, M., & Goodman, C. S. (1996) · Science · doi:10.1126/science.274.5290.1123 · Cited by 3,295 · see citing works
Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily
Oñate, S., Tsai, S., Tsai, M.-J., & O'Malley, B. (1995) · Science · doi:10.1126/science.270.5240.1354 · Cited by 2,507 · see citing works
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 · see citing works
EGFR Antagonists in Cancer Treatment
Ciardiello, F., & Tortora, G. (2008) · New England Journal of Medicine · doi:10.1056/nejmra0707704 · Cited by 2,063 · see citing works
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 2,035 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 1,905 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Ruoslahti, E. I. (1991) · Journal of Clinical Investigation · doi:10.1172/jci114957 · Cited by 1,391 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Forscher, P., & Smith, S. J. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.4.1505 · Cited by 854 · see citing works
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 · see citing works
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 · see citing works
Thyroid Hormone Action in the Heart
Kahaly, G. J., & DILLMANN, W. H. (2005) · Endocrine Reviews · doi:10.1210/er.2003-0033 · Cited by 710 · see citing works
Axon Guidance and the Patterning of Neuronal Projections in Vertebrates
Dodd, J., & Jessell, T. M. (1988) · Science · doi:10.1126/science.3055291 · Cited by 705 · see citing works
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 693 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 567 · see citing works
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 · see citing works
Self-citationHe, 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 · see citing works
Combinatorial roles of the nuclear receptor corepressor in transcription and development.
Jepsen, K., Hermanson, O., Onami, T. M., Gleiberman, A., Lunyak, V., Mcevilly, R., Kurokawa, R., Kumar, V., Liu, F. C., Seto, E., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00064-7 · Cited by 545 · see citing works
Bradley, D. J., Towle, H. C., & Young, W. S. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-06-02288.1992 · Cited by 530 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 489 · see citing works
Oppenheimer, J. H., Schwartz, H. L., & Surks, M. I. (1974) · Endocrinology · doi:10.1210/endo-95-3-897 · Cited by 468 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 431 · see citing works
Linking cyclins to transcriptional control
Coqueret, O. (2002) · Gene · doi:10.1016/s0378-1119(02)01055-7 · Cited by 428 · see citing works
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 · see citing works
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 · see citing works
The efficiency and plasticity of mitochondrial energy transduction.
Brand, M. D. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330897 · Cited by 406 · see citing works
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 · see citing works
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 400 · see citing works
Ribonucleic acid synthesis during the early action of thyroid hormones
Tata, J., & Widnell, C. C. (1966) · Biochemical Journal · doi:10.1042/bj0980604 · Cited by 400 · see citing works
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 383 · see citing works
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 · see citing works
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 · see citing works
Self-citationBentley, D., & Toroian‐Raymond, A. (1986) · Nature · doi:10.1038/323712a0 · Cited by 378 · see citing works
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 · see citing works
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 · see citing works
Self-citationGrowth 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 · see citing works
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 · see citing works
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 · see citing works
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 332 · see citing works
Neuronal Cytomechanics: The Actin-Based Motility of Growth Cones
Smith, S. J. (1988) · Science · doi:10.1126/science.3055292 · Cited by 329 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 295 · see citing works
Refetoff, S., & Dumitrescu, A. M. (2007) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2007.03.005 · Cited by 294 · see citing works
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 286 · see citing works
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 · see citing works
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 · see citing works
Venstrom, K. A., & Reichardt, L. F. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.11.8370483 · Cited by 269 · see citing works
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 · see citing works
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 · see citing works
Self-citationTHE 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 263 · see citing works
Weiss, R. E., & Refetoff, S. (2000) · Reviews in Endocrine and Metabolic Disorders · doi:10.1023/a:1010072605757 · Cited by 257 · see citing works
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 · see citing works
Self-citationCellular Action of Thyroid Hormone on the Heart
DILLMANN, W. H. (2002) · Thyroid · doi:10.1089/105072502760143809 · Cited by 252 · see citing works
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 · see citing works
Cao, X., Kambe, F., Moeller, L. C., Refetoff, S., & Seo, H. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0093 · Cited by 241 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationActin regulation in endocytosis
Smythe, E., & Ayscough, K. (2006) · Journal of Cell Science · doi:10.1242/jcs.03247 · Cited by 223 · see citing works
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 · see citing works
Self-citationThyroid 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 · see citing works
Yoh, S. M., Chatterjee, K., & Privalsky, M. L. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.4.9914 · Cited by 219 · see citing works
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 · see citing works
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 · see citing works
Tang, H., Lin, H., Zhang, S., Davis, F. B., & Davis, P. J. (2004) · Endocrinology · doi:10.1210/en.2004-0308 · Cited by 216 · see citing works
Self-citationThe 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 · see citing works
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 · see citing works
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 205 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Thyroid Hormone Effects on Mitochondrial Energetics
Harper, M.-E., & Seifert, E. L. (2008) · Thyroid · doi:10.1089/thy.2007.0250 · Cited by 194 · see citing works
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 · see citing works
Self-citationThe mitochondrial uncoupling proteins.
Ledesma, A., de Lacoba, M. G., & Rial, E. (2002) · Genome biology · doi:10.1186/gb-2002-3-12-reviews3015 · Cited by 193 · see citing works
Domínguez, Á., Ramos‐Morales, F., Romero, F., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1202140 · Cited by 191 · see citing works
Suzuki, H., Willingham, M. C., & Cheng, S.-Y. (2002) · Thyroid · doi:10.1089/105072502320908295 · Cited by 191 · see citing works
Self-citationMultiple 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 · see citing works
Self-citationCardiac 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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationActing via a Cell Surface Receptor, Thyroid Hormone Is a Growth Factor for Glioma Cells
Davis, F. B., Tang, H., Shih, A., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4365 · Cited by 177 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Liu, Y., Schultz, J. J., & Brent, G. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306120200 · Cited by 165 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationPatterns 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 · see citing works
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 · see citing works
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 · see citing works
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 148 · see citing works
Pathophysiological Importance of Thyroid Hormone Transporters
Heuer, H., & Visser, T. J. (2009) · Endocrinology · doi:10.1210/en.2008-1518 · Cited by 148 · see citing works
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 · see citing works
Self-citationHormone 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 · see citing works
Self-citationOverexpressed Pituitary Tumor-Transforming Gene Causes Aneuploidy in Live Human Cells
Yu, R., Lu, W., Chen, J., et al. (2003) · Endocrinology · doi:10.1210/en.2003-0305 · Cited by 136 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Moeller, L. C., Cao, X., Dumitrescu, A. M., Seo, H., & Refetoff, S. (2006) · Nuclear Receptor Signaling · doi:10.1621/nrs.04020 · Cited by 133 · see citing works
Moeller, L. C., Dumitrescu, A. M., & Refetoff, S. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0542 · Cited by 131 · see citing works
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 · see citing works
Self-citationvan der Deure, W. M., Peeters, R. P., & Visser, T. J. (2010) · Journal of Molecular Endocrinology · doi:10.1677/jme-09-0042 · Cited by 130 · see citing works
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 · see citing works
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 · see citing works
Self-citationHypermetabolism 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 · see citing works
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 · see citing works
Self-citationD’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 · see citing works
Self-citationUnliganded 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 · see citing works
Muronets, V. I., Golovina, T. O., & Nagradova, N. K. (1982) · PubMed · Cited by 124 · see citing works
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 · see citing works
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 · see citing works
Self-citationRapid 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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationStructural 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 · see citing works
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 · see citing works
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 · see citing works
Self-citationAndo, 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 · see citing works
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 · see citing works
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 · see citing works
Self-citationThyroid Hormone-Regulated Actin Polymerization in Brain
Leonard, J. L., & Farwell, A. P. (1997) · Thyroid · doi:10.1089/thy.1997.7.147 · Cited by 108 · see citing works
Self-citationGelsolin‐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 · see citing works
Kamiya, Y. (2002) · Carcinogenesis · doi:10.1093/carcin/23.1.25 · Cited by 105 · see citing works
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 · see citing works
Self-citationAndo, 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 105 · see citing works
Roepe, P. D. (1992) · Biochemistry · doi:10.1021/bi00165a003 · Cited by 103 · see citing works
Ashizawa, K., McPhie, P., Lin, K., & Cheng, S. Y. (1991) · Biochemistry · doi:10.1021/bi00243a010 · Cited by 101 · see citing works
Self-citationCytosolic 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 · see citing works
Self-citationEffects 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 · see citing works
Self-citationKato, 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 · see citing works
Self-citationA 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 · see citing works
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 · see citing works
Self-citationTR 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 · see citing works
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 · see citing works
Self-citationLazar, M. A. (2003) · Nuclear Receptor Signaling · doi:10.1621/nrs.01001 · Cited by 94 · see citing works
Davis, F. B., Davis, P. J., & Blas, S. D. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110803 · Cited by 92 · see citing works
Self-citationMariash, 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 · see citing works
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 · see citing works
Self-citationExtracellular matrix and neuronal movement
Liesi, P. (1990) · Cellular and Molecular Life Sciences · doi:10.1007/bf01939382 · Cited by 90 · see citing works
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 · see citing works
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 · see citing works
Self-citationYing, 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 · see citing works
Self-citationGarstka, H. L., Fäcke, M., Escribano, J., et al. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1493 · Cited by 86 · see citing works
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 86 · see citing works
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 85 · see citing works
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 · see citing works
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 · see citing works
Self-citationThyroid 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 · see citing works
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 83 · see citing works
Self-citationRegulation 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 · see citing works
Self-citationModulation 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 · see citing works
Self-citationLei, J., Mariash, C. N., & Ingbar, D. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405497200 · Cited by 82 · see citing works
Incerpi, S., Luly, P., Vito, P. D., & Farı́as, R. N. (1999) · Endocrinology · doi:10.1210/endo.140.2.6535 · Cited by 81 · see citing works
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 · see citing works
Pietras, R. J. (2003) · The Breast Journal · doi:10.1046/j.1524-4741.2003.09510.x · Cited by 80 · see citing works
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 · see citing works
Self-citationPituitary 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 · see citing works
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 · see citing works
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 · see citing works
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Hormones and endocrine-disrupting chemicals: low-dose effects and nonmonotonic dose responses
Vandenberg, L. N., Colborn, T., Hayes, T. B., Heindel, J. J., Jacobs, D. R., Lee, D.-H., Shioda, T., Soto, A. M., vom Saal, F. S., Welshons, W. V., et al. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1050 · Cited by 3,209 · see citing works
Thyroid Hormone Regulation of Metabolism
Mullur, R., Liu, Y.-Y., & Brent, G. A. (2014) · Physiological Reviews · doi:10.1152/physrev.00030.2013 · Cited by 2,421 · see citing works
Jonklaas, J., Bianco, A. C., Bauer, A. J., Burman, K. D., Cappola, A. R., Celi, F. S., Cooper, D. S., Kim, B. W., Peeters, R. P., Rosenthal, M. S., et al. (2014) · Thyroid® · doi:10.1089/thy.2014.0028 · Cited by 1,928 · see citing works
“While the traditional view has been that T3 is important as the main iodothyronine with significant binding to nuclear TRs at physiological concentrations, and T4 is important as a precursor of T3 (466), the use of desiccated thyroid extracts for therapy of hypothyroidism is based on the hypothesis that other molecule…”
Willner, P. (2005) · Neuropsychobiology · doi:10.1159/000087097 · Cited by 1,605 · see citing works
Thyroid hormones and cardiovascular disease
Jabbar, A., Pingitore, A., Pearce, S. H. S., Zaman, A., Iervasi, G., & Razvi, S. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2016.174 · Cited by 729 · see citing works
Role of Thyroid Hormones in Skeletal Development and Bone Maintenance
Bassett, J. H. D., & Williams, G. R. (2016) · Endocrine Reviews · doi:10.1210/er.2015-1106 · Cited by 540 · see citing works
Thyroid hormone receptors and resistance to thyroid hormone disorders
Ortiga-Carvalho, T. M., Sidhaye, A. R., & Wondisford, F. E. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2014.143 · Cited by 383 · see citing works
Thyroid Hormones as Modulators of Immune Activities at the Cellular Level
De Vito, P., Incerpi, S., Pedersen, J. Z., Luly, P., Davis, F. B., & Davis, P. J. (2011) · Thyroid · doi:10.1089/thy.2010.0429 · Cited by 347 · see citing works
Self-citationBeyond Low Plasma T3: Local Thyroid Hormone Metabolism during Inflammation and Infection
Boelen, A., Kwakkel, J., & Fliers, E. (2011) · Endocrine Reviews · doi:10.1210/er.2011-0007 · Cited by 287 · see citing works
Treatment with thyroid hormone
Biondi, B., & Wartofsky, L. (2014) · Endocrine Reviews · doi:10.1210/er.2013-1083 · Cited by 259 · see citing works
Santini, F., Marzullo, P., Rotondi, M., Ceccarini, G., Pagano, L., Ippolito, S., Chiovato, L., & Biondi, B. (2014) · European Journal of Endocrinology · doi:10.1530/eje-14-0067 · Cited by 240 · see citing works
Thyroid Hormone Diseases and Osteoporosis
Delitala, A. P., Scuteri, A., & Doria, C. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9041034 · Cited by 220 · see citing works
Thyroid hormone, thyroid hormone receptors, and cancer: a clinical perspective
Moeller, L. C., & Führer, D. (2013) · Endocrine-Related Cancer · doi:10.1530/erc-12-0219 · Cited by 184 · see citing works
Transthyretin: A multifaceted protein
Vieira, M., & Saraiva, M. J. (2014) · BioMolecular Concepts · doi:10.1515/bmc-2013-0038 · Cited by 185 · see citing works
Jonklaas, J., Bianco, A. C., Cappola, A. R., Celi, F. S., Fliers, E., Heuer, H., McAninch, E. A., Moeller, L. C., Nygaard, B., Sawka, A. M., et al. (2021) · Thyroid® · doi:10.1089/thy.2020.0720 · Cited by 172 · see citing works
Thyroid Hormone Signaling Pathways: Time for a More Precise Nomenclature
Flamant, F., Cheng, S.-Y., Hollenberg, A. N., Moeller, L. C., Samarut, J., Wondisford, F. E., Yen, P. M., & Refetoff, S. (2017) · Endocrinology · doi:10.1210/en.2017-00250 · Cited by 165 · see citing works
Self-citationTSH and thyrotropic agonists: key actors in thyroid homeostasis
Dietrich, J. W., Landgrafe, G., & Fotiadou, E. H. (2012) · Journal of Thyroid Research · doi:10.1155/2012/351864 · Cited by 146 · see citing works
Homeostatic control of the thyroid-pituitary axis: perspectives for diagnosis and treatment
Hoermann, R., Midgley, J. E. M., Larisch, R., & Dietrich, J. W. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00177 · Cited by 143 · see citing works
The skeletal consequences of thyrotoxicosis
Nicholls, J. J., Brassill, M. J., Williams, G. R., & Bassett, J. H. D. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0059 · Cited by 138 · see citing works
MECHANISMS IN ENDOCRINOLOGY: Beyond the fixed setpoint of the hypothalamus–pituitary–thyroid axis
Fliers, E., Kalsbeek, A., & Boelen, A. (2014) · European Journal of Endocrinology · doi:10.1530/eje-14-0285 · Cited by 124 · see citing works
The Deiodinase Trio and Thyroid Hormone Signaling
Bianco, A. C., & da Conceição, R. R. (2018) · Methods in Molecular Biology · doi:10.1007/978-1-4939-7902-8_8 · Cited by 96 · see citing works
Hoermann, R., Midgley, J. E. M., Giacobino, A., Eckl, W. A., Wahl, H. G., Dietrich, J. W., & Larisch, R. (2014) · Clinical Endocrinology · doi:10.1111/cen.12527 · Cited by 82 · see citing works
Parent, A.-S., Naveau, E., Gerard, A., Bourguignon, J.-P., & Westbrook, G. L. (2011) · Journal of Toxicology and Environmental Health, Part B · doi:10.1080/10937404.2011.578556 · Cited by 82 · see citing works
Jonklaas, J., Bianco, A. C., Cappola, A. R., Celi, F. S., Fliers, E., Heuer, H., McAninch, E. A., Moeller, L. C., Nygaard, B., Sawka, A. M., et al. (2021) · European Thyroid Journal · doi:10.1159/000512970 · Cited by 78 · see citing works
Léger, J. (2015) · European Journal of Endocrinology · doi:10.1530/eje-14-0777 · Cited by 72 · see citing works
Singh, B. K., & Yen, P. M. (2017) · Clinical Diabetes and Endocrinology · doi:10.1186/s40842-017-0046-z · Cited by 72 · see citing works
Type 3 deiodinase and consumptive hypothyroidism: a common mechanism for a rare disease
Luongo, C., Trivisano, L., Alfano, F., & Salvatore, D. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00115 · Cited by 67 · see citing works
Dayan, C., & Panicker, V. (2018) · Thyroid Research · doi:10.1186/s13044-018-0045-x · Cited by 62 · see citing works
Regulation of Intracellular Triiodothyronine Is Essential for Optimal Macrophage Function
van der Spek, A. H., Surovtseva, O. V., Jim, K. K., van Oudenaren, A., Brouwer, M. C., Vandenbroucke-Grauls, C. M. J. E., Leenen, P. J. M., van de Beek, D., Hernandez, A., Fliers, E., et al. (2018) · Endocrinology · doi:10.1210/en.2018-00053 · Cited by 62 · see citing works
Chiamolera, M. I., Sidhaye, A. R., Matsumoto, S., He, Q., Hashimoto, K., Ortiga-Carvalho, T. M., & Wondisford, F. E. (2012) · Molecular Endocrinology · doi:10.1210/me.2011-1290 · Cited by 62 · see citing works
Kalló, I., Mohácsik, P., Vida, B., Zeöld, A., Bardóczi, Z., Zavacki, A. M., Farkas, E., Kádár, A., Hrabovszky, E., Arrojo e Drigo, R., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037860 · Cited by 52 · see citing works
Cardioprotection and thyroid hormones
Pingitore, A., Nicolini, G., Kusmic, C., Iervasi, G., Grigolini, P., & Forini, F. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9545-8 · Cited by 51 · see citing works
Relational Stability in the Expression of Normality, Variation, and Control of Thyroid Function
Hoermann, R., Midgley, J. E. M., Larisch, R., & Dietrich, J. W. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2016.00142 · Cited by 48 · see citing works
Bassett, J. H. D., Boyde, A., Zikmund, T., Evans, H., Croucher, P. I., Zhu, X., Park, J. W., Cheng, S.-Y., & Williams, G. R. (2014) · Endocrinology · doi:10.1210/en.2013-2156 · Cited by 50 · see citing works
Self-citationAbdel-Moneim, A., Gaber, A. M., Gouda, S., Osama, A., Othman, S. I., & Allam, G. (2020) · Hormones · doi:10.1007/s42000-020-00208-8 · Cited by 45 · see citing works
Billon, C., Canaple, L., Fleury, S., Deloire, A., Beylot, M., Dombrowicz, D., del Carmine, P., Samarut, J., & Gauthier, K. (2014) · Endocrinology · doi:10.1210/en.2014-1098 · Cited by 45 · see citing works
Impact of Endocrine Disruptors on the Thyroid Hormone System
Gutleb, A. C., Cambier, S., & Serchi, T. (2016) · Hormone Research in Paediatrics · doi:10.1159/000443501 · Cited by 40 · see citing works
Effects of Short-Term Fasting and Different Overfeeding Diets on Thyroid Hormones in Healthy Humans
Basolo, A., Begaye, B., Hollstein, T., Vinales, K. L., Walter, M., Santini, F., Krakoff, J., & Piaggi, P. (2019) · Thyroid® · doi:10.1089/thy.2019.0237 · Cited by 37 · see citing works
The thyroid axis is regulated by NCoR1 via its actions in the pituitary
Costa-e-Sousa, R. H., Astapova, I., Ye, F., Wondisford, F. E., & Hollenberg, A. N. (2012) · Endocrinology · doi:10.1210/en.2012-1504 · Cited by 38 · see citing works
Low thyroid hormone levels improve survival in murine model for ocular melanoma
Fabian, I. D., Rosner, M., Fabian, I., Vishnevskia-Dai, V., Zloto, O., Maman, E. S., Cohen, K., Ellis, M., Lin, H.-Y., Hercbergs, A., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3566 · Cited by 36 · see citing works
Self-citationMidgley, J. E. M., Hoermann, R., Larisch, R., & Dietrich, J. W. (2013) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2012-201213 · Cited by 35 · see citing works
Lee, S., Young, B. M., Wan, W., Chan, I. H., & Privalsky, M. L. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0448 · Cited by 34 · see citing works
van der Spek, A. H., Jim, K. K., Karaczyn, A., van Beeren, H. C., Ackermans, M. T., Darras, V. M., Vandenbroucke-Grauls, C. M. J. E., Hernandez, A., Brouwer, M. C., Fliers, E., et al. (2018) · Endocrinology · doi:10.1210/en.2017-00666 · Cited by 33 · see citing works
Azar-Kolakez, A., Ecosse, E., Dos Santos, S., & Léger, J. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-2731 · Cited by 27 · see citing works
Thyroid hormone resistance: mechanisms and therapeutic development
Yao, B., Yang, C., Pan, C., & Li, Y. (2022) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2022.111679 · Cited by 26 · see citing works
Cytosolic T3-binding protein modulates dynamic alteration of T3-mediated gene expression in cells
Takeshige, K., Sekido, T., Kitahara, J.-I., Ohkubo, Y., Hiwatashi, D., Ishii, H., Nishio, S.-I., Takeda, T., Komatsu, M., & Suzuki, S. (2014) · Endocrine Journal · doi:10.1507/endocrj.ej13-0418 · Cited by 15 · see citing works
Growth Outcomes and Final Height in Children with Acquired Hypothyroidism: A Systematic Review
Cammisa, I., Rigante, D., & Cipolla, C. (2024) · Children · doi:10.3390/children11121510 · Cited by 10 · see citing works
Role of Thyroid Hormone Receptor-α1 in Endochondral Ossification
Williams, G. R. (2014) · Endocrinology · doi:10.1210/en.2014-1527 · Cited by 8 · see citing works
- 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)
- 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
- 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 › Genetics › 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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