Thyroxine-thyroid hormone receptor interactions

Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,253 · see citing works

Molecular basis of agonism and antagonism in the oestrogen receptor

Brzozowski, A. M., Pike, A. C. W., Dauter, Z., Hubbard, R. E., Bonn, T., Engström, O., Öhman, L., Greene, G. L., Gustafsson, J.-Å., & Carlquist, M. (1997) · Nature · doi:10.1038/39645 · Cited by 3,355 · see citing works

The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen

Shiau, A. K., Barstad, D., Loria, P. M., Cheng, L., Kushner, P. J., Agard, D. A., & Greene, G. L. (1998) · Cell · doi:10.1016/s0092-8674(00)81717-1 · Cited by 2,726 · 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

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

Werner & Ingbar's the thyroid : a fundamental and clinical text

Werner, S. C., Ingbar, S. H., Braverman, L. E., & Utiger, R. D. (2012) · Lippincott-Raven eBooks · Cited by 1,016 · 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

The Human Nuclear Xenobiotic Receptor PXR: Structural Determinants of Directed Promiscuity

Watkins, R. E., Wisely, G. B., Moore, L. B., Collins, J. L., Lambert, M. H., Williams, S. P., Willson, T. M., Kliewer, S. A., & Redinbo, M. R. (2001) · Science · doi:10.1126/science.1060762 · Cited by 760 · see citing works

The Mechanism of Action of Thyroid Hormones

Zhang, J., & Lazar, M. A. (2000) · Annual Review of Physiology · doi:10.1146/annurev.physiol.62.1.439 · Cited by 718 · 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 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 · see citing works

Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): multiple motifs with different binding specificities

Ding, X. F., Anderson, C. M., Ma, H., Hong, H., Uht, R. M., Kushner, P. J., & Stallcup, M. R. (1998) · Molecular Endocrinology · doi:10.1210/mend.12.2.0065 · Cited by 434 · see citing works

Local activation and inactivation of thyroid hormones: the deiodinase family

Köhrle, J. (1999) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(99)00040-4 · Cited by 339 · see citing works

Nuclear-Receptor Ligands and Ligand-Binding Domains

Weatherman, R. V., Fletterick, R. J., & Scanlan, T. S. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.559 · Cited by 323 · see citing works

2.1 Å Crystal Structure of Human PXR in Complex with the St. John's Wort Compound Hyperforin,

Watkins, R. E., Maglich, J. M., Moore, L. B., Wisely, G. B., Noble, S. M., Davis-Searles, P. R., Lambert, M. H., Kliewer, S. A., & Redinbo, M. R. (2003) · Biochemistry · doi:10.1021/bi0268753 · Cited by 318 · see citing works

Coactivator Binding Promotes the Specific Interaction Between Ligand and the Pregnane X Receptor

Watkins, R. E., Davis-Searles, P. R., Lambert, M. H., & Redinbo, M. R. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00795-2 · Cited by 222 · see citing works

Contributions of Plasma Triiodothyronine and Local Thyroxine Monodeiodination to Triiodothyronine to Nuclear Triiodothyronine Receptor Saturation in Pituitary, Liver, and Kidney of Hypothyroid Rats

Silva, J. E., & Larsen, P. R. (1978) · Journal of Clinical Investigation · doi:10.1172/jci109041 · Cited by 209 · see citing works

Interpretation of binding curves obtained with high receptor concentrations: practical aid for computer analysis.

Swillens, S. (1995) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)08761-9 · Cited by 188 · see citing works

Hormone Selectivity in Thyroid Hormone Receptors

Wagner, R., Huber, B. R., Shiau, A. K., Kelly, A. E., Lima, S. T. D. C., Scanlan, T. S., Apriletti, J. W., Baxter, J. D., West, B. L., & Fletterick, R. J. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.3.0608 · Cited by 167 · see citing works

Ligand selectivity by seeking hydrophobicity in thyroid hormone receptor

Borngraeber, S., Budny, M. J., Chiellini, G., Lima, S. T. D. C., Togashi, M., Webb, P., Baxter, J. D., Scanlan, T. S., & Fletterick, R. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2136689100 · Cited by 161 · see citing works

Binding of 3,5,3′-Triiodothyronine (T3) and its Analogs to thein VitroTranslational Products of c-erbA Protooncogenes: Differences in the Affinity of the α- and β-Forms for the Acetic Acid Analog and Failure of the Human Testis and Kidney α-2 Products to Bind T3

Schueler, P. A., Schwartz, H. L., Strait, K. A., Mariash, C. N., & Oppenheimer, J. H. (1990) · Molecular Endocrinology · doi:10.1210/mend-4-2-227 · Cited by 144 · see citing works

Thyroid Receptor Ligands. 1. Agonist Ligands Selective for the Thyroid Receptor β1

Liu, Y., Li, Y.-L., Mellström, K., Mellin, C., Bladh, L.-G., Koehler, K., Garg, N. K., Collazo, A., Litten, C., Husman, B., et al. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm021080f · Cited by 143 · see citing works

Concentration of l-Thyroxine and l-Triiodothyronine Specifically Bound to Nuclear Receptors in Rat Liver and Kidney

Surks, M. I., & Oppenheimer, J. H. (1977) · Journal of Clinical Investigation · doi:10.1172/jci108807 · Cited by 124 · see citing works

Relationship of receptor affinity to the modulation of thyroid hormone nuclear receptor levels and growth hormone synthesis by L-triiodothyronine and iodothyronine analogues in cultured GH1 cells.

Samuels, H. H., Stanley, F. M., & Casanova, J. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109418 · Cited by 121 · see citing works

Rational Design and Synthesis of a Novel Thyroid Hormone Antagonist That Blocks Coactivator Recruitment

Nguyen, N.-H., Apriletti, J. W., Lima, S. T. D. C., Webb, P., Baxter, J. D., & Scanlan, T. S. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm0201013 · Cited by 105 · see citing works

Comparison of the mechanisms of nongenomic actions of thyroid hormone and steroid hormones

Davis, P. J., Tillmann, H. C., Davis, F. B., & Wehling, M. (2002) · Journal of Endocrinological Investigation · doi:10.1007/bf03344022 · Cited by 91 · see citing works

Mechanisms of thyroid hormone action: insights from X-ray crystallographic and functional studies.

Ribeiro, R. C., Apriletti, J. W., Wagner, R., West, B. L., Feng, W., Huber, R., Kushner, P. J., Nilsson, S. V., Scanlan, T. S., Fletterick, R. J., et al. (1998) · PubMed · Cited by 82 · see citing works

X-ray crystallographic and functional studies of thyroid hormone receptor

Ribeiro, R. C. J., Apriletti, J. W., Wagner, R., Feng, W., Kushner, P. J., Nilsson, S. V., Scanlan, T. S., West, B. L., Fletterick, R. J., & Baxter, J. D. (1998) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(98)00029-6 · Cited by 74 · see citing works

Synthesis and biological activity of novel thyroid hormone analogues: 5′-aryl substituted GC-1 derivatives

Chiellini, G., Nguyen, N.-H., Apriletti, J. W., Baxter, J. D., & Scanlan, T. S. (2002) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(01)00284-x · Cited by 74 · see citing works

Design of thyroid hormone receptor antagonists from first principles.

Webb, P., Nguyen, N., Chiellini, G., Yoshihara, H., Lima, S. C. C., Apriletti, J., Ribeiro, R. C., Marimuthu, A., West, B., Goede, P., et al. (2002) · Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(02)00270-4 · Cited by 64 · see citing works

Definition of the Surface in the Thyroid Hormone Receptor Ligand Binding Domain for Association as Homodimers and Heterodimers with Retinoid X Receptor

Ribeiro, R. C. J., Feng, W., Wagner, R., Costa, C. H. R. M., Pereira, A. C., Apriletti, J. W., Fletterick, R. J., & Baxter, J. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010195200 · Cited by 60 · see citing works

Structure-Based Design and Synthesis of a Thyroid Hormone Receptor (TR) Antagonist

Baxter, J. D., Goede, P., Apriletti, J. W., West, B. L., Feng, W., Mellström, K., Fletterick, R. J., Wagner, R. L., Kushner, P. J., Ribeiro, R. C. J., et al. (2002) · Endocrinology · doi:10.1210/endo.143.2.8617 · Cited by 52 · see citing works

Affinity chromatography of thyroid hormone receptors. Biospecific elution from support matrices, characterization of the partially purified receptor.

Apriletti, 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 · see citing works

Expression of the Rat α1 Thyroid Hormone Receptor Ligand Binding Domain in Escherichia coli and the Use of a Ligand-Induced Conformation Change as a Method for Its Purification to Homogeneity

Apriletti, J. W., Baxter, J. D., Lau, K. H., & West, B. L. (1995) · Protein Expression and Purification · doi:10.1006/prep.1995.1048 · Cited by 40 · see citing works

Heterodimerization and deoxyribonucleic acid-binding properties of a retinoid X receptor-related factor

Ribeiro, R. C., Apriletti, J. W., Yen, P. M., Chin, W. W., & Baxter, J. D. (1994) · Endocrinology · doi:10.1210/endo.135.5.7956930 · Cited by 25 · see citing works

Nuclear thyroid hormone receptors in cultured human fibroblasts: Improved method of isolation, partial characterization, and interaction with chromatin

Ichikawa, K., DeGroot, L. J., Refetoff, S., Horwitz, A. L., & Pollak, E. R. (1986) · Metabolism · doi:10.1016/0026-0495(86)90229-5 · Cited by 12 · see citing works

The Halogen Bond

Cavallo, G., Metrangolo, P., Milani, R., Pilati, T., Priimägi, A., Resnati, G., & Terraneo, G. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00484 · Cited by 4,063 · see citing works

Thyroid Hormones and Cardiovascular Function and Diseases

Razvi, S., Jabbar, A., Pingitore, A., Danzi, S., Biondi, B., Klein, I., Peeters, R., Zaman, A., & Iervasi, G. (2018) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2018.02.045 · Cited by 515 · see citing works

Thyroid hormone transporters—functions and clinical implications

Bernal, J., Guadaño‐Ferraz, A., & Morte, B. (2015) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.66 · Cited by 293 · see citing works

Chemistry and Biology in the Biosynthesis and Action of Thyroid Hormones

Mondal, S., Raja, K., Schweizer, U., & Mugesh, G. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601116 · Cited by 216 · see citing works

Thyroid Hormones, T3 and T4, in the Brain

Schroeder, A. C., & Privalsky, M. L. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00040 · Cited by 191 · see citing works

Structural Rearrangements in the Thyroid Hormone Receptor Hinge Domain and Their Putative Role in the Receptor Function

Nascimento, A. S., Dias, S. M. G., Nunes, F. M., Aparício, R., Ambrosio, A. L. B., Bleicher, L., Figueira, A. C. M., Santos, M. A. M., Neto, M. D. O., Fischer, H., et al. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.008 · Cited by 161 · see citing works

Halogen Bonding inside a Molecular Container

El‐Sheshtawy, H. S., Bassil, B. S., Assaf, K. I., Kortz, U., & Nau, W. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3102902 · Cited by 126 · see citing works

Cell and molecular biology of transthyretin and thyroid hormones

Richardson, S. J. (2007) · International Review of Cytology · doi:10.1016/s0074-7696(07)58003-4 · Cited by 116 · see citing works

Halogen bonding in ligand–receptor systems in the framework of classical force fields

Rendine, S., Pieraccini, S., Forni, A., & Sironi, M. (2011) · Physical Chemistry Chemical Physics · doi:10.1039/c1cp22436k · Cited by 87 · see citing works

Gaining ligand selectivity in thyroid hormone receptors via entropy

Martı́nez, L., Nascimento, A. S., Nunes, F. M., Phillips, K. J., Aparício, R., Dias, S. M. G., Figueira, A. C. M., Lin, J. Z., Nguyen, P. T., Apriletti, J. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911024106 · Cited by 84 · see citing works

Revealing a Mutant-Induced Receptor Allosteric Mechanism for the Thyroid Hormone Resistance

Yao, B., Wei, Y., Zhang, S., Tian, S., Xu, S., Wang, R., Zheng, W., & Li, Y. (2019) · iScience · doi:10.1016/j.isci.2019.10.002 · Cited by 83 · see citing works

Molecular Dynamics Simulations Reveal Multiple Pathways of Ligand Dissociation from Thyroid Hormone Receptors

Martı́nez, L., Sonoda, M. T., Webb, P., Baxter, J. D., Skaf, M. S., & Polikarpov, I. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.063818 · Cited by 77 · see citing works

Identification of a New Hormone-Binding Site on the Surface of Thyroid Hormone Receptor

Souza, P. C. T., Puhl, A. C., Martı́nez, L., Aparício, R., Nascimento, A. S., Figueira, A. C. M., Nguyen, P. T., Webb, P., Skaf, M. S., & Polikarpov, I. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1359 · Cited by 66 · see citing works

Evolutionary changes to transthyretin: evolution of transthyretin biosynthesis

Richardson, S. J. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07244.x · Cited by 64 · see citing works

Cell division and apoptosis in the adult neural stem cell niche are differentially affected in transthyretin null mice

Richardson, S. J., Lemkine, G. F., Alfama, G., Hassani, Z., & DEMENEIX, B. A. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.05.040 · Cited by 59 · see citing works

Thyroid Hormone Function in the Rat Testis

Gao, Y., Lee, W. M., & Cheng, C. Y. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00188 · Cited by 57 · see citing works

Novel thyroid hormone analogues, enzyme inhibitors and mimetics, and their action

Mondal, S., & Mugesh, G. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.04.006 · Cited by 57 · see citing works

Halogen Bonds in Ligand–Protein Systems: Molecular Orbital Theory for Drug Design

Margiotta, E., van der Lubbe, S. C. C., Santos, L. D. A., Paragi, G., Moro, S., Bickelhaupt, F. M., & Guerra, C. F. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00946 · Cited by 55 · see citing works

Biomolecular Halogen Bonds

Ho, P. S. (2014) · Topics in current chemistry · doi:10.1007/128_2014_551 · Cited by 55 · see citing works

A mathematical model of pituitary–thyroid interaction to provide an insight into the nature of the thyrotropin–thyroid hormone relationship

Leow, M. K.-S. (2007) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2007.05.016 · Cited by 53 · see citing works

Developmentally regulated thyroid hormone distributor proteins in marsupials, a reptile, and fish

Richardson, S. J., Monk, J. A., Shepherdley, C. A., Ebbesson, L. O. E., Sin, F. Y. T., Power, D. M., Frappell, P. B., Köhrle, J., & Renfree, M. B. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00793.2004 · Cited by 53 · see citing works

Thyroxine Affects Expression of KSPG-Related Genes, the Carbonic Anhydrase II Gene, and KS Sulfation in the Embryonic Chicken Cornea

Conrad, A. H., Zhang, Y., Walker, A. R., Olberding, L. A., Hanzlick, A., Zimmer, A. J., Morffi, R., & Conrad, G. W. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-0806 · Cited by 52 · see citing works

Conformational adaptation of nuclear receptor ligand binding domains to agonists: Potential for novel approaches to ligand design

Togashi, M., Borngraeber, S., Sandler, B., Fletterick, R. J., Webb, P., & Baxter, J. D. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2005.01.004 · Cited by 52 · see citing works

Effect of Different Levels of Supplemental Yeast on Body Weight, Thyroid Hormone Metabolism and Lipid Profile of Broiler Chickens

Aluwong, T., HASSAN, F., DZENDA, T., Kawu, M. U., & Ayo, J. O. (2012) · Journal of Veterinary Medical Science · doi:10.1292/jvms.12-0368 · Cited by 49 · see citing works

Perfluorooctane sulfonic acid exposure increases cadmium toxicity in early life stage of zebrafish, Danio rerio

Kim, S., Ji, K., Lee, S.-W., Lee, J., Kim, J., Kim, S., Kho, Y., & Choi, K. (2010) · Environmental Toxicology and Chemistry · doi:10.1002/etc.443 · Cited by 48 · see citing works

Role of Halogen Bonds in Thyroid Hormone Receptor Selectivity: Pharmacophore-Based 3D-QSSR Studies

Valadares, N. F., Salum, L. B., Polikarpov, I., Andricopulo, A. D., & Garratt, R. C. (2009) · Journal of Chemical Information and Modeling · doi:10.1021/ci900316e · Cited by 47 · see citing works

Detrimental consequences of micropolymers associated plasticizers on endocrinal disruption

Saha, U., Kumari, P., Ghosh, A., Sinha, A., Jena, S., Kirti, A., Gupta, A., Choudhury, A., Simnani, F. Z., Nandi, A., et al. (2024) · Materials Today Bio · doi:10.1016/j.mtbio.2024.101139 · Cited by 48 · see citing works

Hormonal and ion regulatory response in three freshwater fish species following waterborne copper exposure

Eyckmans, M., Tudorache, C., Darras, V., Blust, R., & Boeck, G. D. (2010) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2010.05.002 · Cited by 45 · see citing works

Insights from the Structure of Estrogen Receptor into the Evolution of Estrogens: Implications for Endocrine Disruption

Baker, M. E. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.03.008 · Cited by 43 · see citing works

Hypothyroidism and metabolic cardiovascular disease

Patrizio, A., Ferrari, S. M., Elia, G., Ragusa, F., Balestri, E., Botrini, C., Rugani, L., Mazzi, V., Antonelli, A., Fallahi, P., et al. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1408684 · Cited by 52 · see citing works

Evaluation of a panel of in vitro methods for assessing thyroid receptor β and transthyretin transporter disrupting activities

Collet, B., Simon, E., van der Linden, S., el Abdellaoui, N., Naderman, M., Man, H.-Y., Middelhof, I., van der Burg, B., Besselink, H. T., & Brouwer, A. (2019) · Reproductive Toxicology · doi:10.1016/j.reprotox.2019.05.011 · Cited by 42 · see citing works

Role of thyroid hormone-integrin αvβ3-signal and therapeutic strategies in colorectal cancers

Yang, Y.-C. S. H., Ko, P.-J., Pan, Y.-S., Lin, H., Whang‐Peng, J., Davis, P. J., & Wang, K. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00719-5 · Cited by 43 · see citing works

Thyroid Receptor Ligands. 6. A High Affinity “Direct Antagonist” Selective for the Thyroid Hormone Receptor

Koehler, K., Gordon, S. L., Brandt, P., Carlsson, B., Bäcksbro-Saeidi, A., Apelqvist, T., Agback, P., Grover, G. J., Nelson, W., Grynfarb, M., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060521i · Cited by 39 · see citing works

Structure of a Thyroid Hormone Receptor DNA-Binding Domain Homodimer Bound to an Inverted Palindrome DNA Response Element

Chen, Y., & Young, M. A. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0129 · Cited by 38 · see citing works

Evolution of thyroid hormone distributor proteins

McLean, T. R., Rank, M. M., Smooker, P. M., & Richardson, S. J. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.02.038 · Cited by 37 · see citing works

Quantification of Ligand-Regulated Nuclear Receptor Corepressor and Coactivator Binding, Key Interactions Determining Ligand Potency and Efficacy for the Thyroid Hormone Receptor

Jeyakumar, M., Webb, P., Baxter, J. D., Scanlan, T. S., & Katzenellenbogen, J. A. (2008) · Biochemistry · doi:10.1021/bi800393u · Cited by 35 · see citing works

The Role of Thyroid Hormone in Neuronal Protection

Liu, Y., & Brent, G. A. (2021) · Comprehensive physiology · doi:10.1002/cphy.c200019 · Cited by 44 · see citing works

3,5‐diiodothyronine (3,5‐T2) reduces blood glucose independently of insulin sensitization in obese mice

Teixeira, S. D. S., Filgueira, C. S., Sieglaff, D. H., Benod, C. C., Villagomez, R. A., Minze, L. J., Zhang, A., Webb, P., & Nunes, M. T. (2016) · Acta Physiologica · doi:10.1111/apha.12821 · Cited by 33 · see citing works

Principles of Biomolecular Recognition

Kahn, K., & Plaxco, K. W. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0919-0_1 · Cited by 33 · see citing works

Insight Into Molecular Determinants of T3 vs T4 Recognition From Mutations in Thyroid Hormone Receptor α and β

Wejaphikul, K., Groeneweg, S., Hilhorst‐Hofstee, Y., Chatterjee, K., Peeters, R. P., Meima, M. E., & Visser, W. E. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-02794 · Cited by 30 · see citing works

Environmental Co-Exposure to Potassium Perchlorate and Cd Caused Toxicity and Thyroid Endocrine Disruption in Zebrafish Embryos and Larvae (Danio rerio)

Paola, D. D., Natale, S., Iaria, C., Crupi, R., Cuzzocrea, S., Spanò, N., Gugliandolo, E., & Peritore, A. F. (2022) · Toxics · doi:10.3390/toxics10040198 · Cited by 30 · see citing works

The Ability of Thyroid Hormone Receptors to Sense T4 as an Agonist Depends on Receptor Isoform and on Cellular Cofactors

Schroeder, A. C., Jimenez, R., Young, B. M., & Privalsky, M. L. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1335 · Cited by 30 · see citing works

Extending Halogen-based Medicinal Chemistry to Proteins

Hage, K. E., Pandyarajan, V., Phillips, N. B., Smith, B. J., Menting, J. G. T., Whittaker, J., Lawrence, M. C., Meuwly, M., & Weiss, M. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.761015 · Cited by 28 · see citing works

Brain Gene Expression in Systemic Hypothyroidism and Mouse Models of MCT8 Deficiency: The Mct8-Oatp1c1-Dio2 Triad

Morte, B., Gil-Ibáñez, P., Heuer, H., & Bernal, J. (2020) · Thyroid · doi:10.1089/thy.2020.0649 · Cited by 28 · see citing works

The Affinity of Brominated Phenolic Compounds for Human and Zebrafish Thyroid Receptor β: Influence of Chemical Structure

Kollitz, E. M., Carbonnel, L. D., Stapleton, H. M., & Ferguson, P. L. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy028 · 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

µ-Crystallin: A thyroid hormone binding protein

Kinney, C. J., & Bloch, R. J. (2021) · Endocrine Regulations · doi:10.2478/enr-2021-0011 · Cited by 26 · see citing works

Hypothyroidism and Diabetes-Related Dementia: Focused on Neuronal Dysfunction, Insulin Resistance, and Dyslipidemia

Kim, H. K., & Song, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23062982 · Cited by 28 · see citing works

The ups and downs of the thyroxine pro-hormone hypothesis

Galton, V. A. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.01.029 · Cited by 25 · see citing works

Predictive Value of Free Triiodothyronine to Free Thyroxine Ratio in Euthyroid Patients With Myocardial Infarction With Nonobstructive Coronary Arteries

Gao, S., Ma, W., Huang, S., Lin, X., & Yu, M. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.708216 · Cited by 25 · see citing works

Biophysical Optimization of a Therapeutic Protein by Nonstandard Mutagenesis

Pandyarajan, V., Phillips, N. B., Cox, G. P., Yang, Y., Whittaker, J., Ismail‐Beigi, F., & Weiss, M. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.588277 · Cited by 24 · see citing works

Identification and Molecular Interaction Studies of Thyroid Hormone Receptor Disruptors among Household Dust Contaminants

Zhang, J., Li, Y., Gupta, A. A., Nam, K., & Andersson, P. L. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00171 · Cited by 24 · see citing works

X-ray-Structure-Based Identification of Compounds with Activity against Targets from Different Families and Generation of Templates for Multitarget Ligand Design

Gilberg, E., Stumpfe, D., & Bajorath, J. (2018) · ACS Omega · doi:10.1021/acsomega.7b01849 · Cited by 21 · see citing works

Remarkably Selective Recognition of Iodobenzene Derivatives by a Macrocyclic Bis‐PtII Metallohost

Trokowski, R., Akine, S., & Nabeshima, T. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201101650 · Cited by 21 · see citing works

Evolution of the thyroid hormone, retinoic acid, ecdysone and liver X receptors

Ollikainen, N., Chandsawangbhuwana, C., & Baker, M. E. (2006) · Integrative and Comparative Biology · doi:10.1093/icb/icl035 · Cited by 20 · see citing works

Chemie und Biologie der Schilddrüsenhormon‐Biosynthese und ‐Wirkung

Mondal, S., Raja, K., Schweizer, U., & Mugesh, G. (2016) · Angewandte Chemie · doi:10.1002/ange.201601116 · Cited by 19 · see citing works

Is the Intrinsic Genomic Activity of Thyroxine Relevant In Vivo ? Effects on Gene Expression in Primary Cerebrocortical and Neuroblastoma Cells

Gil-Ibáñez, P., Belinchón, M. M., Morte, B., Obregón, M.-J., & Bernal, J. (2017) · Thyroid · doi:10.1089/thy.2017.0024 · Cited by 19 · see citing works

Effects of Thyroxine (T4), 3,5,3′-triiodo-l-thyronine (T3) and their Metabolites on Osteoblast Differentiation

Cheng, S., Xing, W., Pourteymoor, S., & Mohan, S. (2016) · Calcified Tissue International · doi:10.1007/s00223-016-0159-x · Cited by 19 · see citing works

Structural aspects of thyroid hormone binding to proteins and competitive interactions with natural and synthetic compounds

Schweizer, U., Towell, H., Vit, A., Rodriguez-Ruiz, A., & Steegborn, C. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.01.026 · Cited by 18 · see citing works

The power of heteronemin in cancers

Wang, K., Chen, Y., Yang, Y. S. H., Huang, H., Lee, S., Shih, Y.-J., Li, Z., Whang‐Peng, J., Lin, H., & Davis, P. J. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-022-00816-z · Cited by 17 · see citing works

Thyromimetics and MASLD: Unveiling the Novel Molecules Beyond Resmetirom

Ezhilarasan, D. (2025) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.16874 · Cited by 17 · see citing works

Site-specific basicities regulate molecular recognition in receptor binding: in silico docking of thyroid hormones

Tóth, G., Baska, F., Schretner, A., Rácz, Á., & Noszál, B. (2013) · European Biophysics Journal · doi:10.1007/s00249-013-0921-1 · Cited by 17 · see citing works

Ligand induced interaction of thyroid hormone receptor beta with its coregulators

Valadares, N. F., Polikarpov, I., & Garratt, R. C. (2008) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.10.006 · Cited by 16 · see citing works

Alternative ligands for thyroid hormone receptors

Lazcano, I., Hernández‐Puga, G., Robles, J. P., & Orozco, A. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.05.007 · Cited by 17 · see citing works

Erratum: Thyroid hormone transporters—functions and clinical implications

Bernal, J., Guadaño‐Ferraz, A., & Morte, B. (2015) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.113 · Cited by 17 · see citing works

Focus on Autoimmune Myocarditis in Graves' Disease: A Case-Based Review

Wu, L., Wang, W., Leng, Q., Tang, N., Zhou, N., Wang, Y., & Wang, D. W. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.678645 · Cited by 16 · see citing works

Structural Insights Into Thyroid Hormone Receptors

Tambones, I., & le Maire, A. (2024) · Endocrinology · doi:10.1210/endocr/bqae154 · Cited by 15 · see citing works

On the Denaturation Mechanisms of the Ligand Binding Domain of Thyroid Hormone Receptors

Martı́nez, L., Souza, P. C. T., García, W., Batista, F. A. H., Portugal, R. V., Nascimento, A. S., Nakahira, M., Lima, L. M. T. R., Polikarpov, I., & Skaf, M. S. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp911554p · Cited by 14 · see citing works

Classical nuclear hormone receptor activity as a mediator of complex concentration response relationships for endocrine active compounds

Cookman, C. J., & Belcher, S. M. (2014) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2014.09.013 · Cited by 14 · see citing works

Insight into the mechanisms of neuroendocrine toxicity induced by 6:2FTCA via thyroid hormone disruption

Wu, L., Gu, J., Duan, X., Feng, G., Ye, H., Kong, L., Liu, W., Gao, R., Jiao, J., Chen, H., et al. (2023) · Chemosphere · doi:10.1016/j.chemosphere.2023.140031 · Cited by 13 · see citing works

Pathological Interactions Between Mutant Thyroid Hormone Receptors and Corepressors and Their Modulation by a Thyroid Hormone Analogue with Therapeutic Potential

Harrus, D., Déméné, H., Vasquez, E., Boulahtouf, A., Germain, P., Figueira, A. C. M., Privalsky, M. L., Bourguet, W., & le Maire, A. (2018) · Thyroid · doi:10.1089/thy.2017.0551 · Cited by 13 · see citing works

Halogen Bonding in the Molecular Recognition of Thyroid Hormones and Their Metabolites by Transport Proteins and Thyroid Hormone Receptors

Mondal, S., Giri, D., & Mugesh, G. (2019) · Journal of the Indian Institute of Science · doi:10.1007/s41745-019-00153-5 · Cited by 12 · see citing works

Thyroid Hormones

Liu, Y., Milanesi, A., & Brent, G. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813814-4.00021-3 · Cited by 12 · see citing works

Intergenerational thyroid hormone homeostasis imbalance in cerebellum of rats perinatally exposed to glyphosate‐based herbicide

Reis, L. T. C., de Souza, J. S., Herai, R. H., Cunha, E. D. B. B., Soares, J. R. P., El-Bachá, R. D. S., da Silva, V. D. A., Romano, M. A., Romano, R. M., Chiamolera, M. I., et al. (2021) · Environmental Toxicology · doi:10.1002/tox.23102 · Cited by 12 · see citing works

Tracing iodine

Metrangolo, P., & Resnati, G. (2011) · Nature Chemistry · doi:10.1038/nchem.998 · Cited by 12 · see citing works

Label-Free Quantitative Mass Spectrometry Reveals Novel Pathways Involved in LL-37 Expression

Cederlund, A., Nylén, F., Miraglia, E., Bergman, P., Gudmundsson, G. H., & Agerberth, B. (2013) · Journal of Innate Immunity · doi:10.1159/000355931 · Cited by 12 · see citing works

Covalent ligands of nuclear receptors

Rajan, S., & Yoon, H. S. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115869 · Cited by 11 · see citing works

The Role of Thyroid Hormone in Neuronal Protection

Liu, Y., & Brent, G. A. (2021) · Comprehensive physiology · doi:10.1002/j.2040-4603.2021.tb00174.x · Cited by 11 · see citing works

Resistance to thyroid hormone α, revelation of basic study to clinical consequences

Tang, Y., Yu, M., & Lian, X. (2016) · Journal of Pediatric Endocrinology and Metabolism · doi:10.1515/jpem-2015-0286 · Cited by 11 · see citing works

A Feedforward Loop within the Thyroid-Brown Fat Axis Facilitates Thermoregulation

Sun, L., Goh, H. J., Govindharajulu, P., Sun, L., Henry, C. J., & Leow, M. K. (2020) · Scientific Reports · doi:10.1038/s41598-020-66697-0 · Cited by 11 · see citing works

The thyroid hormone system disrupting potential of resorcinol in fish

Dingenen, I. V., Andersen, E., Volz, S. N., Christiansen, M., Novák, J., Haigis, A.-C., Stacy, E. H., Blackwell, B. R., Villeneuve, D. L., Vergauwen, L., et al. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116995 · Cited by 10 · see citing works

Marsupial models for understanding evolution of thyroid hormone distributor proteins

Richardson, S. J. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.04.002 · Cited by 10 · see citing works

SNP mutations occurring in thyroid hormone receptor influenced individual susceptibility to triiodothyronine: Molecular dynamics and site‐directed mutagenesis approaches

Liu, Y., Qu, K., Hai, Y., Li, X., Zhao, L., & Zhao, C. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26425 · Cited by 10 · see citing works

Identification of a Thyroid Hormone Binding Site in Hsp90 with Implications for Its Interaction with Thyroid Hormone Receptor Beta

Fan, L., Kishore, A., Jansen‐Olliges, L., Wang, D., Stahl, F., Psathaki, O. E., Harre, J., Warnecke, A., Weder, J., Preller, M., et al. (2022) · ACS Omega · doi:10.1021/acsomega.2c02331 · Cited by 9 · see citing works

Laboratory Testing in Thyroid Disorders

Grebe, S. K. G. (2019) · Springer eBooks · doi:10.1007/978-3-319-72102-6_10 · Cited by 9 · see citing works

Quantitation of Thyroid Hormone Binding to Anti-Thyroxine Antibody Fab Fragment by Native Mass Spectrometry

Thangaraj, S. K., Arola, H. O., Tullila, A., Nevanen, T. K., Rouvinen, J., & Jänis, J. (2019) · ACS Omega · doi:10.1021/acsomega.9b02659 · Cited by 9 · see citing works

Cryo-EM: A new dawn in thyroid biology

Coscia, F., & Taler‐Verčič, A. (2021) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2021.111309 · Cited by 9 · see citing works

Halogen Bonding in Haspin-Halogenated Tubercidin Complexes: Molecular Dynamics and Quantum Chemical Calculations

Zhou, Y., & Wong, M. W. (2022) · Molecules · doi:10.3390/molecules27030706 · Cited by 9 · see citing works

A Novel Transgenic Model to Study Thyroid Axis Activity in Early Life Stage Medaka

Pesce, E., Garde, M., Rigolet, M., Tindall, A. J., Lemkine, G. F., Baumann, L., Sachs, L. M., & Pasquier, D. D. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c05515 · Cited by 8 · see citing works

Development of yeast reporter assays for the enhanced detection of environmental ligands of thyroid hormone receptors α and β from Xenopus tropicalis

Matsui, S., Ito‐Harashima, S., Sugimoto, Y., Takada, E., Shiizaki, K., Kawanishi, M., & Yagi, T. (2016) · Toxicology in Vitro · doi:10.1016/j.tiv.2016.08.008 · Cited by 8 · see citing works

Design and synthesis of novel 3-hydroxy-cyclobut-3-ene-1,2-dione derivatives as thyroid hormone receptor β (TR-β) selective ligands

Raval, S., Raval, P., Bandyopadhyay, D., Soni, K., Yevale, D. B., Jogiya, D., Modi, H., Joharapurkar, A. A., Gandhi, N. S., Jain, M. R., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.06.038 · Cited by 8 · see citing works

Circulating thyroid hormones and clinical parameters of heart failure in men

Turić, I., Velat, I., Bušić, Ž., & Čulić, V. (2023) · Scientific Reports · doi:10.1038/s41598-023-47391-3 · Cited by 7 · see citing works

New emerging polybromobiphenyls in serum of general population and their disruption on thyroid hormone receptor β1

Bao, J., Jin, H., Wang, Y., Jin, J., & Chen, L. (2022) · Environment International · doi:10.1016/j.envint.2022.107390 · Cited by 7 · see citing works

Halogen bonds between ligands and proteins: Can we use them in validation?

de Vries, I., Tsiompanaki, G., Anastassis Perrakis, A., & Joosten, R. P. (2025) · Protein Science · doi:10.1002/pro.70321 · Cited by 6 · see citing works

Differential effects of TR ligands on hormone dissociation rates: Evidence for multiple ligand entry/exit pathways

Lima, S. T. D. C., Nguyen, N.-H., Togashi, M., Apriletti, J. W., Nguyen, P. T., Polikarpov, I., Scanlan, T. S., Baxter, J. D., & Webb, P. (2009) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2009.08.003 · Cited by 6 · see citing works

The oligomeric state of thyroid receptor regulates hormone binding kinetics

Lima, S. T. D. C., & Rodrigues, E. D. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0019 · Cited by 6 · see citing works

Heat conduction by thyroid hormone receptors

Lamichhane, T. R., & Lamichhane, H. P. (2018) · AIMS Biophysics · doi:10.3934/biophy.2018.4.245 · Cited by 6 · see citing works

Echo dephasing and heat capacity from constrained and unconstrained dynamics of triiodothyronine nuclear receptor protein

Lamichhane, T. R., Paudel, S., Yadav, B. K., & Lamichhane, H. P. (2019) · Journal of Biological Physics · doi:10.1007/s10867-018-9518-3 · Cited by 6 · see citing works

Thyroid Hormone Deiodination—Mechanisms and Small Molecule Enzyme Mimics

Giri, D., & Mugesh, G. (2025) · Biomolecules · doi:10.3390/biom15040529 · Cited by 5 · see citing works

Structural insight to human Retinoid X receptor alpha-Thyroid hormone receptor beta heterodimer by molecular modelling and MD-simulation studies: role of conserved water molecules

Mukherjee, S., Dasgupta, S., Panja, S. S., & Adhikari, U. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2147097 · Cited by 5 · see citing works

An Update on Human Thyroid Hormone Receptors in Health and Disease: Chemistry, Physiology and Pathophysiology

Banu, L. A. S., Sharmila, S., & Aruldhas, M. M. (2013) · Journal of Endocrinology & Reproduction · doi:10.18519/jer/2013/v17/75784

X-ray crystallographic and functional studies of thyroid hormone receptor

Ribeiro, R. C. J., Apriletti, J. W., Wagner, R., Feng, W., Kushner, P. J., Nilsson, S. V., Scanlan, T. S., West, B. L., Fletterick, R. J., & Baxter, J. D. (1998) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(98)00029-6 · Cited by 74 · see citing works

Insight Into Molecular Determinants of T3 vs T4 Recognition From Mutations in Thyroid Hormone Receptor α and β

Wejaphikul, K., Groeneweg, S., Hilhorst‐Hofstee, Y., Chatterjee, K., Peeters, R. P., Meima, M. E., & Visser, W. E. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-02794 · Cited by 30 · see citing works

Identification of a New Hormone-Binding Site on the Surface of Thyroid Hormone Receptor

Souza, P. C. T., Puhl, A. C., Martı́nez, L., Aparício, R., Nascimento, A. S., Figueira, A. C. M., Nguyen, P. T., Webb, P., Skaf, M. S., & Polikarpov, I. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1359 · Cited by 66 · see citing works

Thyroid Hormones and 3,5-Diiodothyropropionic Acid: New Keys for New Locks

Yen, P. M. (2006) · Endocrinology · doi:10.1210/en.2006-0074 · Cited by 10 · see citing works