The DOI matches its Crossref record; 299 of the 299 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredIn the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
2 retracted
Items 201–299 of 299
Physical Properties of a Dog Liver and Kidney Cytosol Protein That Binds Thyroid Hormone
Davis, P. J., Handwerger, B. S., & Glaser, F. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42241-2 · Cited by 76
Self-citationYing, H., Suzuki, H., Zhao, L., Willingham, M. C., Meltzer, P. S., & Cheng, S.-Y. (2003) · PubMed · Cited by 76
Self-citationFarwell, A. P., Lynch, R. M., Okulicz, W. C., Comi, A. M., & Leonard, J. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44786-7 · Cited by 74
Self-citationGalo, M. G., Uñates, L. E., & Farı́as, R. N. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68932-5 · Cited by 74
Liesi, P., Hager, G., Dodt, H., et al. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490400208 · Cited by 74
Lei, J., Mariash, C. N., Bhargava, M., et al. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00335.2007 · Cited by 72
Lei, J., Nowbar, S., Mariash, C. N., et al. (2003) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00376.2002 · Cited by 72
Hashimoto, K., Cohen, R., Yamada, M., Markan, K. R., Monden, T., Satoh, T., Mori, M., & Wondisford, F. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507877200 · Cited by 71
Thyroid Hormone Regulates the Extracellular Organization of Laminin on Astrocytes1
Farwell, A. P., & Dubord-Tomasetti, S. A. (1999) · Endocrinology · doi:10.1210/endo.140.11.7114 · Cited by 70
Ying, H. (2003) · Carcinogenesis · doi:10.1093/carcin/bgg111 · Cited by 70
Chen, Y., Chen, P., Chen, C., Sharp, Z. D., & Lee, W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4443 · Cited by 69
Nuclear receptors as drug targets in obesity, dyslipidemia and atherosclerosis.
Hansen, M. K., & Connolly, T. M. (2008) · PubMed · Cited by 67
Oligomeric binding of T3 receptor is required for maximal T3 response.
Williams, G. R., Harney, J. W., FORMAN, B. M., et al. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55040-7 · Cited by 66
Mylotte, K. M., Cody, V., Davis, P. J., et al. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.7974 · Cited by 66
Self-citationAcute Effects of Thyroid Hormone Analogs on Sodium Currents in Neonatal Rat Myocytes
Huang, C.-J., Geller, H. M., Green, W. L., & Craelius, W. (1999) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1998.0930 · Cited by 65
Rebbaa, A., Chu, F., Davis, F. B., Davis, P. J., & Mousa, S. A. (2008) · Angiogenesis · doi:10.1007/s10456-008-9110-8 · Cited by 64
Self-citationMarques, A. R., Espadinha, C., Frias, M. J., et al. (2004) · British Journal of Cancer · doi:10.1038/sj.bjc.6601989 · Cited by 64
Samuels, H. H., Tsai, J. S., & Casanova, J. (1974) · Science · doi:10.1126/science.184.4142.1188 · Cited by 64
Lin, H., Zhang, West, B. L., Tang, H.-Y., Passaretti, T. V., Davis, F. B., & Davis, P. J. (2003) · Biochemistry · doi:10.1021/bi0273967 · Cited by 62
Self-citationJones, I., Ng, L., Liu, H., & Forrest, D. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0037 · Cited by 62
Shih, A., Zhang, S., Cao, H. J., et al. (2003) · Endocrinology · doi:10.1210/en.2003-0742 · Cited by 60
Tagami, T., & Jameson, J. L. (1998) · Endocrinology · doi:10.1210/endo.139.2.5742 · Cited by 60
Tumor Suppressor p53 Is a Negative Regulator in Thyroid Hormone Receptor Signaling Pathways
Bhat, M. K., Yu, C.-L., Yap, N. L., Zhan, Q., Hayashi, Y., Seth, P. K., & Cheng, S.-Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.28989 · Cited by 58
Self-citationTsou, R., & Isik, F. F. (2001) · Molecular and Cellular Biochemistry · doi:10.1023/a:1011947301849 · Cited by 57
Araki, O., Ying, H., Furuya, F., Zhu, X., & Cheng, S.-Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508556102 · Cited by 57
Self-citationSiesser, W. B., Cheng, S.-Y., & McDonald, M. P. (2005) · Psychopharmacology · doi:10.1007/s00213-005-0024-5 · Cited by 57
Self-citationNovel forms of neuronal migration in the rat cerebellum
Hager, G., Dodt, H., Zieglgänsberger, W., & Liesi, P. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490400209 · Cited by 56
Zhang, X., Kaneshige, M., Kamiya, Y., Kaneshige, K., McPhie, P., & Cheng, S.-Y. (2002) · Molecular Endocrinology · doi:10.1210/me.2002-0080 · Cited by 55
Self-citationPotentiation by thyroid hormone of human IFN-gamma-induced HLA-DR expression.
Lin, H., Martino, L. J., Wilcox, B. D., Davis, F. B., Gordinier, J., & Davis, P. J. (1998) · PubMed · Cited by 53
Self-citationHeart mitochondrial DNA and enzyme changes during early human development
Marı́n-Garcı́a, J., Ananthakrishnan, R., & Goldenthal, M. J. (2000) · Molecular and Cellular Biochemistry · doi:10.1023/a:1007031919298 · Cited by 52
Sodium butyrate selectively alters thyroid hormone receptor gene expression in GH3 cells.
Lazar, M. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38188-2 · Cited by 52
Regulation of thyroid hormone receptor-mediated transcription by a cytosol protein.
Ashizawa, K., & Cheng, S.-Y. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.19.9277 · Cited by 51
Self-citationGriffith, A. J., Szymko, Y. M., Kaneshige, M., Quiñónez, R. E., Kaneshige, K., Heintz, K. A., Mastroianni, M., Kelley, M. W., & Cheng, S.-Y. (2002) · Journal of the Association for Research in Otolaryngology · doi:10.1007/s101620010092 · Cited by 50
Self-citationA Thyroid Hormone Analog Stimulates Angiogenesis in the Post-infarcted Rat Heart
Tomanek, R. J. (1998) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1998.0671 · Cited by 50
Segal, J., & Ingbar, S. H. (1981) · Journal of Clinical Investigation · doi:10.1172/jci110224 · Cited by 50
Segal, J., & Ingbar, S. H. (1989) · Endocrinology · doi:10.1210/endo-124-4-1949 · Cited by 49
Puymirat, J., Étongué-Mayer, P., & Dussault, J. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30651 · Cited by 48
Cao, H. J., Lin, H., Luidens, M. K., Davis, F. B., & Davis, P. J. (2009) · Endocrine Research · doi:10.1080/07435800902911810 · Cited by 48
Self-citationApriletti, J. W., Eberhardt, N. L., Latham, K. R., & Baxter, J. D. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43238-3 · Cited by 47
Stimulation in vitro of Rabbit Erythrocyte Cytosol Phospholipid-dependent Protein Kinase Activity
Lawrence, W. D., Schoenl, M., & Davis, P. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83655-9 · Cited by 45
Self-citationZhu, X., Park, K. S., Kaneshige, M., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2604-2618.2000 · Cited by 44
Mousa, S. S., Mousa, S. S., Davis, F. B., et al. (2009) · Clinical and Applied Thrombosis/Hemostasis · doi:10.1177/1076029609348315 · Cited by 44
Acute thyroid hormone promotes slow inactivation of sodium current in neonatal cardiac myocytes
Harris, D. R., Green, W. L., & Craelius, W. (1991) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(91)90081-8 · Cited by 43
Apriletti, J. W., Baxter, J. D., & Lavin, T. N. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)76556-9 · Cited by 42
Kamiya, Y., Zhang, X., Ying, H., Kato, Y., Willingham, M. C., Xu, J., O’Malley, B. W., & Cheng, S.-Y. (2003) · Endocrinology · doi:10.1210/en.2003-0239 · Cited by 42
Self-citationSensory Neuron Sodium Current Requires Nongenomic Actions of Thyroid Hormone During Development
Yonkers, M. A., & Ribera, A. B. (2008) · Journal of Neurophysiology · doi:10.1152/jn.90801.2008 · Cited by 42
Saelim, N., John, L. M., Wu, J., Park, J. S., Bai, Y., Camacho, P., & Lechleiter, J. D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200409011 · Cited by 41
Molecular components underlying nongenomic thyroid hormone signaling in embryonic zebrafish neurons
Yonkers, M. A., & Ribera, A. B. (2009) · Neural Development · doi:10.1186/1749-8104-4-20 · Cited by 41
Potentiation by Thyroid Hormone of Human IFN-γ-Induced HLA-DR Expression
Lin, H., Martino, L. J., Wilcox, B. D., Davis, F. B., Gordinier, J., & Davis, P. J. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.2.843 · Cited by 41
Self-citationEffects of thyroidectomy, T4, and DITPA replacement on brain blood vessel density in adult rats
Schlenker, E. H., Hora, M. J., Liu, Y., Redetzke, R. A., Morkin, E., & Gerdes, A. M. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00027.2008 · Cited by 39
Nuclear Receptor Corepressor Is a Novel Regulator of Phosphatidylinositol 3-Kinase Signaling
Furuya, F., Guigon, C. J., Zhao, L., Lu, C., Hanover, J. A., & Cheng, S.-Y. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00900-07 · Cited by 38
Self-citationParkison, C., Ashizawa, K., McPhie, P., et al. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91424-b · Cited by 37
Zinman, T., Shneyvays, V., Tribulová, N., et al. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20562 · Cited by 37
Thyroid Hormone Receptor Is a Negative Regulator in p53-Mediated Signaling Pathways
Barrera-Hernandez, G., Zhan, Q., Wong, R. S. L., et al. (1998) · DNA and Cell Biology · doi:10.1089/dna.1998.17.743 · Cited by 37
Thyroid Hormone Inhibits Fibronectin Synthesis by Cultured Human Skin Fibroblsts*
Murata, Y., CECCARELLI, P., Refetoff, S., Horwitz, A. L., & Matsui, N. (1987) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-64-2-334 · Cited by 35
Hashizume, K., Miyamoto, T., Ichikawa, K., et al. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83671-7 · Cited by 33
Stachelek, S. J., Kowalik, T. F., Farwell, A. P., & Leonard, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004221200 · Cited by 32
Self-citationMarino, F., Guasti, L., Cosentino, M., Piazza, D. D., Simoni, C., Piantanida, E., Cimpanelli, M., Klersy, C., Bartalena, L., Venco, A., et al. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.06.016 · Cited by 31
Angel, R. C., Botta, J. A., & Farı́as, R. N. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47279-7 · Cited by 30
Qi, J.-S., Desai-Yajnik, V., Yuan, Y., & Samuels, H. H. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.7195 · Cited by 30
Kobayashi, M., Hashizume, K., Suzuki, S., Ichikawa, K., & Takeda, T. (1991) · Endocrinology · doi:10.1210/endo-129-4-1701 · Cited by 29
Nemenoff, R. A., Weiser‐Evans, M. C. M., & Winn, R. A. (2008) · PPAR Research · doi:10.1155/2008/156875 · Cited by 28
Sherr, C. J. (2002) · Cell Cycle · doi:10.4161/cc.1.1.106 · Cited by 28
Bhargava, M., Lei, J., Mariash, C. N., & Ingbar, D. H. (2007) · Current Opinion in Endocrinology Diabetes and Obesity · doi:10.1097/med.0b013e3282f02ae8 · Cited by 28
Gustafson, K. S., Baloch, Z. W., Putt, M. E., et al. (2003) · American Journal of Clinical Pathology · doi:10.1309/2e6q-gjrg-getv-t8k9 · Cited by 28
Segal, J., & Ingbar, S. H. (1989) · Endocrinology · doi:10.1210/endo-124-5-2166 · Cited by 28
Safran, M., Farwell, A. P., Rokos, H., & Leonard, J. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85230-4 · Cited by 27
Self-citationReceptor Tyrosine Kinases as Therapeutic Targets in Malignant Glioma
Ren, H., Yang, B., & Rainov, N. G. (2007) · Reviews on Recent Clinical Trials · doi:10.2174/157488707780599384 · Cited by 27
Acute effects of thyroid hormone on sodium currents in neonatal myocytes
Craelius, W., Green, W. L., & Harris, D. R. (1990) · Bioscience Reports · doi:10.1007/bf01117247 · Cited by 27
Kim, C. S., Furuya, F., Ying, H., et al. (2006) · Endocrinology · doi:10.1210/en.2006-0923 · Cited by 27
Chakrabarti, N. (2000) · Neuropsychopharmacology · doi:10.1016/s0893-133x(99)00073-1 · Cited by 25
Kuzman, J. A., Tang, Y., Vogelsang, K. A., Said, S., Anderson, B. E., Morkin, E., & Gerdes, A. M. (2007) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y07-011 · Cited by 25
Effect of thyroid hormones on G proteins in synaptosomes of chick embryo.
Giguère, A., Fortier, S., Beaudry, C., Gallo‐Payet, N., & Bellabarba, D. (1996) · Endocrinology · doi:10.1210/endo.137.6.8641209 · Cited by 25
Breast cancer and thyroid therapy. Statement by the American Thyroid Association
Gorman, C. A. (1977) · JAMA · doi:10.1001/jama.237.14.1459 · Cited by 25
Kim, D. S., McCabe, C., Buchanan, M. A., et al. (2003) · Clinical Otolaryngology · doi:10.1046/j.1365-2273.2003.00732.x · Cited by 24
Duncan, K. G., Jumper, M. D., Ribeiro, R. C. J., et al. (1999) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s004170050224 · Cited by 24
Sarkar, P., Durga, N. D., Morris, J. J., & Martin, J. V. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.10.002 · Cited by 24
Andersson‐Lendahl, M., & Vennström, B. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01223-4 · Cited by 24
Segal, J., Hardiman, J., & Ingbar, S. H. (1989) · Biochemical Journal · doi:10.1042/bj2610749 · Cited by 24
Sarkar, P., & Ray, A. K. (1998) · Neuroreport · doi:10.1097/00001756-199804200-00035 · Cited by 23
Saelim, N., Holstein, D. M., Chocrón, E. S., Camacho, P., & Lechleiter, J. D. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0109-1 · Cited by 22
Zandieh‐Doulabi, B., Schiphorst, M. P.-T., Kalsbeek, A., Fliers, E., Bakker, O., & Wiersinga, W. M. (2003) · Endocrinology · doi:10.1210/en.2003-0791 · Cited by 21
Vandenbrouck, Y., Janvier, B., LORIETTE, C., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0126f.x · Cited by 20
Effects of Hyperthyroidism and Hypothyroidism on Human Red Blood Cell Ca2+-ATPase Activity*
Dube, M. P., Davis, F. B., Davis, P. J., et al. (1986) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-62-2-253 · Cited by 19
Self-citationPeroxisome Proliferator–Activated Receptor γ Expression in Follicular-Patterned Thyroid Lesions
Gustafson, K. S., LiVolsi, V. A., Furth, E. E., et al. (2003) · American Journal of Clinical Pathology · doi:10.1309/2e6qgjrggetvt8k9 · Cited by 19
Nieman, L. K., Fb, D., Pj, D., et al. (1983) · PubMed · Cited by 19
Wei, L., & Hu, X. (2004) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2003.12.010 · Cited by 18
Suzuki, H., & Cheng, S.-Y. (2003) · Molecular Endocrinology · doi:10.1210/me.2003-0114 · Cited by 18
Self-citationVandenbrouck, Y., Janvier, B., LORIETTE, C., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20678.x · Cited by 18
Hashizume, K., Suzuki, S., Ichikawa, K., et al. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91531-g · Cited by 16
The Role of PPARγ in Pulmonary Vascular Disease
Hart, C. M. (2008) · Journal of Investigative Medicine · doi:10.2310/jim.0b013e318165e921 · Cited by 16
Giguère, A., Lehoux, J., Gallo‐Payet, N., & Bellabarba, D. (1992) · Developmental Brain Research · doi:10.1016/0165-3806(92)90083-9 · Cited by 15
Galusca, B., Dumollard, J. M., Chambonnière, M. L., et al. (2004) · PubMed · Cited by 14
Vié-Luton, M.-P., Blanchet, P., Samson, M., et al. (1996) · Endocrinology · doi:10.1210/endo.137.11.8895318 · Cited by 13
Saturable binding of thyroid hormone to isolated rat hepatocytes
Blondeau, J. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)81384-9 · Cited by 12
Binding of (125I) triiodothyronine to human peripheral leukocytes and its internalization
Kostrouch, Z., Felt, V., Raška, I., Nedvidkova, J., & Holečková, E. (1987) · Cellular and Molecular Life Sciences · doi:10.1007/bf01956056 · Cited by 7
Stanley, F. M., Tsai, J. S., & Samuels, H. H. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67668-9 · Cited by 6
Chakrabarti, N., & Ray, A. K. (2002) · Neuroscience Research Communications · doi:10.1002/nrc.10052 · Cited by 5
Flagged first, then by citations
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
Cited by
Sorted by citations
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
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
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
“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
Mechanisms of thyroid hormone action
Brent, G. A. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60047 · Cited by 1,244
Metadata
- 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 › 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
