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1

Cahnmann, Hans J., Edison Goncalves, Yoichiro Ito, Henry M. Fales, and Edward A. Sokoloski. "Synthesis and characterization of N-bromoacetyl-3,3′,5-triiodo-L-thyronine." Journal of Chromatography A 538, no. 1 (1991): 165–75. http://dx.doi.org/10.1016/s0021-9673(01)91634-6.

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2

Grymuła, K., E. Paczkowska, V. Dziedziejko, et al. "The influence of 3,3',5-triiodo-l-thyronine on human haematopoiesis." Cell Proliferation 40, no. 3 (2007): 302–15. http://dx.doi.org/10.1111/j.1365-2184.2007.00435.x.

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3

MARCHAND, JEAN, ANNIE GORCE, GABRIEL BADOUAILLE, JEAN-MARC BRAS, DOMINIQUE SIMON, and BERNARD PAU. "Production and Partial Characterization of Monoclonal Antibodies Against 3,3′,5-Triiodo-L-Thyronine." Hybridoma 6, no. 1 (1987): 97–101. http://dx.doi.org/10.1089/hyb.1987.6.97.

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4

Lai, Ching-San, W. Korytowski, Chien-Hau Niu, and Sheue-Yann Cheng. "Transverse motion of spin-labeled 3,3′,5-triiodo-L-thyronine in phospholipid bilayers." Biochemical and Biophysical Research Communications 131, no. 1 (1985): 408–12. http://dx.doi.org/10.1016/0006-291x(85)91817-0.

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5

Obata, Toru, Takaaki Fukuda, and Sheue-yann Cheng. "Antibodies against the human cellular 3,3′,5-triiodo-L-thyronine-binding protein (p58)." FEBS Letters 230, no. 1-2 (1988): 9–12. http://dx.doi.org/10.1016/0014-5793(88)80630-6.

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6

Vacek, Jan, Pavel Kosina, Eva Gabrielová, Martin Modrianský, and Jitka Ulrichová. "Ion-trap mass spectrometry for determination of 3,5,3′-triiodo-l-thyronine and 3,5,3′,5′-tetraiodo-l-thyronine in neonatal rat cardiomyocytes." Journal of Pharmaceutical and Biomedical Analysis 53, no. 3 (2010): 688–92. http://dx.doi.org/10.1016/j.jpba.2010.03.018.

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7

Köhrle, J., L. Schomburg, S. Drescher, E. Fekete, and K. Bauer. "Rapid stimulation of type I 5′-deiodinase in rat pituitaries by 3,3′,5-triiodo-l-thyronine." Molecular and Cellular Endocrinology 108, no. 1-2 (1995): 17–21. http://dx.doi.org/10.1016/0303-7207(95)92574-8.

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8

Aboul-Enein, Hassan Y., Stefan Raluca-Ioana, Simona Litescu, and Gabriel Lucian Radu. "BIOSENSOR FOR THE ENANTIOSELECTIVE ANALYSIS OF THE THYROID HORMONES (+)-3,3′,5-TRIIODO-L-THYRONINE (T3) AND (+)-3,3′,5,5′-TETRAIODO-L-THYRONINE (T4)." Journal of Immunoassay and Immunochemistry 23, no. 2 (2002): 181–90. http://dx.doi.org/10.1081/ias-120003660.

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9

Aboul-Enein, Hassan Y., Raluca-Ioana Stefan, Gabriel Lucian Radu, and George-Emil Baiulescu. "The Construction of an Amperometric Immunosensor for the Thyroid Hormone (+)-3,3′,5-Triiodo-L-Thyronine (L-T3)." Analytical Letters 32, no. 3 (1999): 447–55. http://dx.doi.org/10.1080/00032719908542832.

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10

Walker, Jennifer D., Fred A. Crawford, Rupak Mukherjee, Michael R. Zile, and Francis G. Spinale. "Direct effects of acute administration of 3, 5, 3′ triiodo-l-thyronine on myocyte function." Annals of Thoracic Surgery 58, no. 3 (1994): 851–56. http://dx.doi.org/10.1016/0003-4975(94)90766-8.

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11

Chatonnet, Fabrice, Frédéric Picou, Teddy Fauquier, and Frédéric Flamant. "Thyroid Hormone Action in Cerebellum and Cerebral Cortex Development." Journal of Thyroid Research 2011 (2011): 1–8. http://dx.doi.org/10.4061/2011/145762.

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Thyroid hormones (TH, including the prohormone thyroxine (T4) and its active deiodinated derivative 3,,5-triiodo-L-thyronine (T3)) are important regulators of vertebrates neurodevelopment. Specific transporters and deiodinases are required to ensure T3 access to the developing brain. T3 activates a number of differentiation processes in neuronal and glial cell types by binding to nuclear receptors, acting directly on transcription. Only few T3 target genes are currently known. Deeper investigations are urgently needed, considering that some chemicals present in food are believed to interfere w
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12

Stefan, Raluca‐Ioana, Jacobus Frederick van Staden, and Hassan Y. Aboul‐Enein. "Determination of (+)‐3,3′,5‐Triiodo‐L‐thyronine (L‐T3) from Serum Using a Sequential Injection Analysis/Immunosensor System." Journal of Immunoassay and Immunochemistry 25, no. 2 (2004): 183–89. http://dx.doi.org/10.1081/ias-120030527.

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13

Suzuki, Shunsuke, Kentaro Kasai, and Kiyoshi Yamauchi. "Characterization of little skate (Leucoraja erinacea) recombinant transthyretin: Zinc-dependent 3,3′,5-triiodo-l-thyronine binding." General and Comparative Endocrinology 217-218 (June 2015): 43–53. http://dx.doi.org/10.1016/j.ygcen.2015.04.006.

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14

Michienzi, Simona, Barbara Bucci, Cecilia Verga Falzacappa, et al. "3,3′,5-Triiodo-l-thyronine inhibits ductal pancreatic adenocarcinoma proliferation improving the cytotoxic effect of chemotherapy." Journal of Endocrinology 193, no. 2 (2007): 209–23. http://dx.doi.org/10.1677/joe.1.07065.

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The pancreatic adenocarcinoma is an aggressive and devastating disease, which is characterized by invasiveness, rapid progression, and profound resistance to actual treatments, including chemotherapy and radiotherapy. At the moment, surgical resection provides the best possibility for long-term survival, but is feasible only in the minority of patients, when advanced disease chemotherapy is considered, although the effects are modest. Several studies have shown that thyroid hormone, 3,3′,5-triiodo-l-thyronine (T3) is able to promote or inhibit cell proliferation in a cell type-dependent manner
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15

Sar, Pranati, Bandita Rath, Umakanta Subudhi, Gagan Bihari Nityananda Chainy, and Prakash Chandra Supakar. "Alterations in expression of senescence marker protein-30 gene by 3,3′,5-triiodo-l-thyronine (T3)." Molecular and Cellular Biochemistry 303, no. 1-2 (2007): 239–42. http://dx.doi.org/10.1007/s11010-007-9462-1.

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16

Van Erp, A. C., R. Rebolledo, J. Wiersema-Buist, H. G. D. Leuvenink, and P. Romanque. "Anti-apoptotic effects of 3,3’,5-triiodo-l-thyronine in the liver of brain-dead rats." Transplant Immunology 31, no. 4 (2014): 249–50. http://dx.doi.org/10.1016/j.trim.2014.11.189.

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17

Rebolledo, Rolando A., Anne C. Van Erp, Petra J. Ottens, Janneke Wiersema-Buist, Henri G. D. Leuvenink, and Pamela Romanque. "Anti-Apoptotic Effects of 3,3’,5-Triiodo-L-Thyronine in the Liver of Brain-Dead Rats." PLOS ONE 10, no. 10 (2015): e0138749. http://dx.doi.org/10.1371/journal.pone.0138749.

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18

ALDERSON, RALPH, IRA PASTAN, and SHEUE-YANN CHENG. "Characterization of the 3,3′,5-Triiodo-L-Thyronine Binding Site on Plasma Membranes from Human Placenta." Endocrinology 116, no. 6 (1985): 2621–30. http://dx.doi.org/10.1210/endo-116-6-2621.

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19

Monk, Julie A., Natalie A. Sims, Katarzyna M. Dziegielewska, Roy E. Weiss, Robert G. Ramsay, and Samantha J. Richardson. "Delayed development of specific thyroid hormone-regulated events in transthyretin null mice." American Journal of Physiology-Endocrinology and Metabolism 304, no. 1 (2013): E23—E31. http://dx.doi.org/10.1152/ajpendo.00216.2012.

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Thyroid hormones (THs) are vital for normal postnatal development. Extracellular TH distributor proteins create an intravascular reservoir of THs. Transthyretin (TTR) is a TH distributor protein in the circulatory system and is the only TH distributor protein synthesized in the central nervous system. We investigated the phenotype of TTR null mice during development. Total and free 3′,5′,3,5-tetraiodo-l-thyronine (T4) and free 3′,3,5-triiodo-l-thyronine (T3) in plasma were significantly reduced in 14-day-old (P14) TTR null mice. TTR null mice also displayed a delayed suckling-to-weaning transi
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20

Hasumura, S., S. Kitagawa, E. Lovelace, M. C. Willingham, I. Pastan, and S. Cheng. "Characterization of a membrane-associated 3,3',5-triiodo-L-thyronine binding protein by use of monoclonal antibodies." Biochemistry 25, no. 24 (1986): 7881–88. http://dx.doi.org/10.1021/bi00372a014.

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21

Togashi, Marie, Phuong Nguyen, Robert Fletterick, John D. Baxter, and Paul Webb. "Rearrangements in Thyroid Hormone Receptor Charge Clusters That StabilizeBound 3,5′,5-Triiodo-L-thyronine and Inhibit HomodimerFormation." Journal of Biological Chemistry 280, no. 27 (2005): 25665–73. http://dx.doi.org/10.1074/jbc.m501615200.

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22

Petersen, K. F., G. W. Cline, J. B. Blair, and G. I. Shulman. "Substrate cycling between pyruvate and oxaloacetate in awake normal and 3,3'-5-triiodo-L-thyronine-treated rats." American Journal of Physiology-Endocrinology and Metabolism 267, no. 2 (1994): E273—E277. http://dx.doi.org/10.1152/ajpendo.1994.267.2.e273.

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Substrate cycling between pyruvate and oxaloacetate was assessed in awake 24-h fasted normal and triiodothyronine (T3)-treated rats. After a 20- or 60-min infusion of [3-13C]alanine (99% enriched, 12 mg/min) the 13C enrichments of liver glucose and alanine carbons were analyzed by 13C and 1H nuclear magnetic resonance spectroscopy and gas chromatography-mass spectrometry. Substrate cycling from phosphoenolpyruvate to pyruvate [via pyruvate kinase (PK)] and from oxaloacetate to pyruvate [via malic enzyme (ME)] relative to the pyruvate carboxylase (PC) flux [i.e., (PK+ME)/PC] was assessed by the
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23

Bhat, M. K., C. Parkison, P. Mcphie, C. M. Liang та S. Y. Cheng. "Conformational Changes of Human β1 Thyroid Hormone Receptor Induced by Binding of 3,3′,5-Triiodo-L-thyronine". Biochemical and Biophysical Research Communications 195, № 1 (1993): 385–92. http://dx.doi.org/10.1006/bbrc.1993.2055.

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24

Cheng, Sheue-Yann. "Structural Similarities between the Plasma Membrane Binding Sites for L-Thyroxine and 3,3′,5-Triiodo-L- Thyronine in Cultured Cells." Journal of Receptor Research 5, no. 1 (1985): 1–26. http://dx.doi.org/10.3109/10799898509041868.

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25

Lei, Jianxun, Sogol Nowbar, Cary N. Mariash, and David H. Ingbar. "Thyroid hormone stimulates Na-K-ATPase activity and its plasma membrane insertion in rat alveolar epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 285, no. 3 (2003): L762—L772. http://dx.doi.org/10.1152/ajplung.00376.2002.

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Na-K-ATPase protein is critical for maintaining cellular ion gradients and volume and for transepithelial ion transport in kidney and lung. Thyroid hormone, 3,3′,5-triiodo-l-thyronine (T3), given for 2 days to adult rats, increases alveolar fluid resorption by 65%, but the mechanism is undefined. We tested the hypothesis that T3 stimulates Na-K-ATPase in adult rat alveolar epithelial cells (AEC), including primary rat alveolar type II (ATII) cells, and determined mechanisms of the T3 effect on the Na-KATPase enzyme using two adult rat AEC cell lines (MP48 and RLE-6TN). T3 at 10-8 and 10-5 M in
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26

R Powley, Charles, Jinlan Dong, Bethany R. Hannas, and Zhihua Amanda Shen. "Rapid, high-throughput method for the quantification of thyroid hormones in rat blood serum using isotope-dilution LC–MS/MS." Bioanalysis 12, no. 23 (2020): 1689–98. http://dx.doi.org/10.4155/bio-2020-0248.

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Aim: Numerous guideline studies required for regulatory toxicity testing now include the measurement of the thyroid hormones 3,3′,5-triiodo-L-thyronine (T3) and L-thyroxine (T4) in blood serum from rodents. A rapid, high-throughput method for the determination of the thyroid hormones T4 and T3 is reported. Materials & methods: Sample preparation is done using a 96-well microtiter plate format. Stable isotope analogs of both hormones are used as internal standards for study and quality control samples. Results & conclusion: The validated quantification levels are T3: 10 pg/ml and T4: 1
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27

Kitagawa, S., T. Obata, S. Hasumura, I. Pastan, and S. Y. Cheng. "A cellular 3,3',5-triiodo-L-thyronine binding protein from a human carcinoma cell line. Purification and characterization." Journal of Biological Chemistry 262, no. 8 (1987): 3903–8. http://dx.doi.org/10.1016/s0021-9258(18)61442-5.

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28

Oziol, L., P. Faure, N. Bertrand, and P. Chomard. "Inhibition of in vitro macrophage-induced low density lipoprotein oxidation by thyroid compounds." Journal of Endocrinology 177, no. 1 (2003): 137–46. http://dx.doi.org/10.1677/joe.0.1770137.

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Oxidized low density lipoproteins (LDL) are highly suspected of initiating the atherosclerosis process. Thyroid hormones and structural analogues have been reported to protect LDL from lipid peroxidation induced by Cu2+ or the free radical generator 2,2'-azobis-'2-amidinopropane' dihydrochloride in vitro. We have examined the effects of thyroid compounds on macrophage-induced LDL oxidation. Human monocyte-derived macrophages (differentiated U937 cells) were incubated for 24 h with LDL and different concentrations (0-20 microM) of 3,5,3'-triiodo-l -thyronine (T3), 3,5,3',5'-tetraiodo-L-thyronin
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29

Markova, Natalyia, Anton Chernopiatko, Careen A. Schroeter, et al. "Hippocampal Gene Expression of Deiodinases 2 and 3 and Effects of 3,5-Diiodo-L-Thyronine T2 in Mouse Depression Paradigms." BioMed Research International 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/565218.

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Central thyroid hormone signaling is important in brain function/dysfunction, including affective disorders and depression. In contrast to 3,3′,5-triiodo-L-thyronine (T3), the role of 3,5-diiodo-L-thyronine (T2), which until recently was considered an inactive metabolite of T3, has not been studied in these pathologies. However, both T3 and T2 stimulate mitochondrial respiration, a factor counteracting the pathogenesis of depressive disorder, but the cellular origins in the CNS, mechanisms, and kinetics of the cellular action for these two hormones are distinct and independent of each other. H
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30

Iwase, Katsumi, Brian C. W. Hummel, and Paul G. Walfish. "Cytosol components from human placenta and rat liver in iodothyronine 5- and 5′-deiodination." Biochemistry and Cell Biology 67, no. 1 (1989): 58–63. http://dx.doi.org/10.1139/o89-009.

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Using either human placental microsomal 5-deiodinase as enzyme (5-DI) and thyroxine as substrate or rat liver (RL) microsomal 5′-deiodinase (5′ DI) as enzyme and reverse [(3′- or 5′-)-125I]triiodo-L-thyronine ([125I]rT3) as substrate, activation of 5′-DI in the presence of NADPH was observed using either human placental or rat liver cytosolic components, but there was no activation of 5-DI. Both could be activated by DTT, with higher concentrations being required for 5-DI than for 5′-DI. Iopanoic acid, dicumarol, and sodium arsenite inhibited 5′-DI and 5-DI activated by DTT. In the presence of
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31

Halperin, Y., L. E. Shapiro, and M. I. Surks. "Down-regulation of type II L-thyroxine, 5'-monodeiodinase in cultured GC cells: different pathways of regulation by L-triiodothyronine and 3,3',5'-triiodo-L-thyronine." Endocrinology 135, no. 4 (1994): 1464–69. http://dx.doi.org/10.1210/endo.135.4.7925108.

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32

Eales, J. G., and K. R. Finnson. "Response of hepatic thyroxine 5′-deiodinase of rainbow trout,Oncorhynchus mykiss, to chronic ingestion of 3,5,3′-triiodo-L-thyronine." Journal of Experimental Zoology 257, no. 2 (1991): 230–35. http://dx.doi.org/10.1002/jez.1402570213.

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33

Degani, Gad, and Margie Lee Gallagher. "The influence of 3,3',5-triiodo-l-thyronine on growth survival and body composition of slow-growing development elvers (Anguilla rostrata L.)." Comparative Biochemistry and Physiology Part A: Physiology 84, no. 1 (1986): 7–11. http://dx.doi.org/10.1016/0300-9629(86)90034-4.

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34

Morin, P. P., T. J. Hara, and J. G. Eales. "Thyroid function and olfactory responses to L-alanine during induced smoltification in Atlantic salmon, Salmo salar." Canadian Journal of Fisheries and Aquatic Sciences 54, no. 3 (1997): 596–602. http://dx.doi.org/10.1139/f96-309.

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For 5 weeks starting in mid-February we examined developmental correlations between external smolt features, plasma thyroid hormone levels, and olfactory responses in Atlantic salmon transferred from 0.9 to 11°C and exposed to a 16 h light : 8 h dark (16L) or an 8 h light : 16 h dark (8L) photoperiod. In 16L fish, external smolt features developed to 80% of full state, plasma L-thyroxine (T4) surged at week 3, but there were no changes in plasma 3,5,3 prime -triiodo-L-thyronine, olfactory bulb electroencephalographic (EEG), or olfactory epithelium electro-olfactographic (EOG) activities in res
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35

Eales, J. G., P. P. Morin, P. Tsang, and T. J. Hara. "Thyroid Hormone Deiodination in Brain, Liver, Gill, Heart and Muscle of Atlantic Salmon (Salmo salar) during Photoperiodically-Induced Parr-Smolt Transformation. II. Outer- and Inner-Ring 3,5,3′-Triiodo-l-Thyronine and 3,3′,5′-Triiodo-l-Thyronine (Reverse T3) Deiodination." General and Comparative Endocrinology 90, no. 2 (1993): 157–67. http://dx.doi.org/10.1006/gcen.1993.1070.

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36

Schroeder, Amy, Robyn Jimenez, Briana Young, and Martin L. Privalsky. "The Ability of Thyroid Hormone Receptors to Sense T4 as an Agonist Depends on Receptor Isoform and on Cellular Cofactors." Molecular Endocrinology 28, no. 5 (2014): 745–57. http://dx.doi.org/10.1210/me.2013-1335.

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Abstract T4 (3,5,3′,5′-tetraiodo-l-thyronine) is classically viewed as a prohormone that must be converted to the T3 (3,5,3′-triiodo-l-thyronine) form for biological activity. We first determined that the ability of reporter genes to respond to T4 and to T3 differed for the different thyroid hormone receptor (TR) isoforms, with TRα1 generally more responsive to T4 than was TRβ1. The response to T4 vs T3 also differed dramatically in different cell types in a manner that could not be attributed to differences in deiodinase activity or in hormone affinity, leading us to examine the role of TR co
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37

Scapin, Sergio, Silvia Leoni, Silvana Spagnuolo, Anna Maria Fiore, and Sandra Incerpi. "Short-term effects of thyroid hormones on Na+-K+-ATPase activity of chick embryo hepatocytes during development: focus on signal transduction." American Journal of Physiology-Cell Physiology 296, no. 1 (2009): C4—C12. http://dx.doi.org/10.1152/ajpcell.90604.2007.

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Nongenomic effects of thyroid hormones on Na+-K+-ATPase activity were studied in chick embryo hepatocytes at two different developmental stages, 14 and 19 days of embryonal age, and the signal transduction pathways involved were characterized. Our data showed the following. 1) 3,5,3′-Triiodo-l-thyronine (T3) and 3,5-diiodo-l-thyronine (3,5-T2) rapidly induced a transient inhibitory effect on the Na+-K+-ATPase; the extent and duration depended on the developmental age of the cells. 2) 3,5-T2 behaved as a true hormone and fully mimicked the effect of T3. 3) Thyroxine had no effect at any of the
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38

Wang, Xue, S. O. Adeniran, Ziming Wang, et al. "3, 3′, 5-Triiodo-L-thyronine affects polarity proteins of bovine Sertoli cells via WT1/non-canonical Wnt signaling pathway." Theriogenology 148 (May 2020): 8–17. http://dx.doi.org/10.1016/j.theriogenology.2020.02.034.

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39

Cheng, S. Y., S. Hasumura, M. C. Willingham, and I. Pastan. "Purification and characterization of a membrane-associated 3,3',5-triiodo-L-thyronine binding protein from a human carcinoma cell line." Proceedings of the National Academy of Sciences 83, no. 4 (1986): 947–51. http://dx.doi.org/10.1073/pnas.83.4.947.

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40

Lin, Kwang-huei, Ya-wen Lin, Clifford Parkison та Sheue-yann Cheng. "Stimulation of proliferation by 3,3′,5-triiodo-l-thyronine in poorly differentiated human hepatocarcinoma cells overexpressing β1 thyroid hormone receptor". Cancer Letters 85, № 2 (1994): 189–94. http://dx.doi.org/10.1016/0304-3835(94)90274-7.

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41

Hasumura, Satoshi, Shuji Kitagawa, Ira Pastan, and Sheue-yann Cheng. "Solubilization and characterization of a membrane 3, 3′, 5-triiodo-L-thyronine binding protein from rat pituitary tumor GH3 cells." Biochemical and Biophysical Research Communications 133, no. 3 (1985): 837–43. http://dx.doi.org/10.1016/0006-291x(85)91210-0.

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42

Masmoudi, Taoufik, Richard Planells, Jacques Mounié, Yves Artur, Jacques Magdalou, and Hervé Goudonnet. "Opposite regulation of bilirubin and 4-nitrophenol UDP-glucuronosyltransferase mRNA levels by 3,3′,5 triiodo-l -thyronine in rat liver." FEBS Letters 379, no. 2 (1996): 181–85. http://dx.doi.org/10.1016/0014-5793(95)01507-8.

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43

Maclatchy, Deborah L., and J. G. Eales. "Short-term treatment with testosterone increases plasma 3,5,3′-triiodo-l-thyronine and hepatic l-thyroxine 5′-monodeiodinase levels in arctic charr, Salvelinus alpinus." General and Comparative Endocrinology 71, no. 1 (1988): 10–16. http://dx.doi.org/10.1016/0016-6480(88)90289-4.

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44

Okabe, Nobuo, Naoko Mano, and Satomi Tahira. "Binding characteristics of a major thyroid hormone metabolite, 3,3′5′-triiodo-L-thyronine, to bovine serum albumin as measured by fluorescence." Biochimica et Biophysica Acta (BBA) - General Subjects 990, no. 3 (1989): 303–5. http://dx.doi.org/10.1016/s0304-4165(89)80049-2.

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45

Cruz, Raymundo, Lucia Chávez-Gutiérrez, Patricia Joseph-Bravo, and Jean-Louis Charli. "3,3',5'-Triiodo-L-Thyronine Reduces Efficiency of mRNA Knockdown by Antisense Oligodeoxynucleotides: A Study with Pyroglutamyl Aminopeptidase II in Adenohypophysis." Oligonucleotides 14, no. 3 (2004): 176–90. http://dx.doi.org/10.1089/oli.2004.14.176.

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46

Ledda-Columbano, G. M., A. Perra, R. Piga, et al. "Cell proliferation induced by 3,3′,5-triiodo-L-thyronine is associated with a reduction in the number of preneoplastic hepatic lesions." Carcinogenesis 20, no. 12 (1999): 2299–304. http://dx.doi.org/10.1093/carcin/20.12.2299.

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Abe, Eiichi, Shiqeo Murai, Hiroko Saito, Yoshikatsu Masuda, and Tadanobu Itoh. "Effect of 3,3’,5-triiodo-L-thyronine on the deficits of working memory and brain neurotransmitters induced by AF64A in mice." Japanese Journal of Pharmacology 58 (1992): 310. http://dx.doi.org/10.1016/s0021-5198(19)49423-7.

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Fernández-Pernas, Pablo, Juan Fafián-Labora, Iván Lesende-Rodriguez, et al. "3, 3′, 5-triiodo-L-thyronine Increases In Vitro Chondrogenesis of Mesenchymal Stem Cells From Human Umbilical Cord Stroma Through SRC2." Journal of Cellular Biochemistry 117, no. 9 (2016): 2097–108. http://dx.doi.org/10.1002/jcb.25515.

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Cruz, Raymundo, Lucia Chávez-Gutiérrez, Patricia Joseph-Bravo, and Jean-Louis Charli. "3,3′,5′-Triiodo-L-Thyronine Reduces Efficiency of mRNA Knockdown by Antisense Oligodeoxynucleotides: A Study with Pyroglutamyl Aminopeptidase II in Adenohypophysis." Oligonucleotides 14, no. 3 (2004): 176–90. http://dx.doi.org/10.1089/1545457042258314.

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Sweeting, R. M., and J. G. Eales. "Thyroxine 5′-monodeiodinase activity in microsomes from isolated hepatocytes of rainbow trout: Effects of growth hormone and 3,5,3′-triiodo-l-thyronine." General and Comparative Endocrinology 88, no. 2 (1992): 169–77. http://dx.doi.org/10.1016/0016-6480(92)90248-i.

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