Molecular orbital studies of thyroid hormone analogs

1973 ◽  
Vol 95 (26) ◽  
pp. 8518-8525 ◽  
Author(s):  
Peter A. Kollman ◽  
Wallace J. Murray ◽  
Merrill E. Nuss ◽  
Eugene C. Jorgensen ◽  
Steve. Rothenberg
1974 ◽  
Vol 5 (11) ◽  
pp. no-no
Author(s):  
PETER A. KOLLMAN ◽  
WALLACE J. MURRAY ◽  
MERRILL E. NUSS ◽  
EUGENE C. JORGENSEN ◽  
STEVE ROTHENBERG

2018 ◽  
Vol 9 ◽  
Author(s):  
Paul J. Davis ◽  
Heng-Yuan Tang ◽  
Aleck Hercbergs ◽  
Hung-Yun Lin ◽  
Kelly A. Keating ◽  
...  

Endocrinology ◽  
2011 ◽  
Vol 152 (3) ◽  
pp. 1136-1142 ◽  
Author(s):  
Carmen Grijota-Martínez ◽  
Eric Samarut ◽  
Thomas S. Scanlan ◽  
Beatriz Morte ◽  
Juan Bernal

Thyroid hormone analogs with selective actions through specific thyroid hormone receptor (TR) subtypes are of great interest. They might offer the possibility of mimicking physiological actions of thyroid hormone with receptor subtype or tissue specificity with therapeutic aims. They are also pharmacological tools to dissect biochemical pathways mediated by specific receptor subtypes, in a complementary way to mouse genetic modifications. In this work, we studied the in vivo activity in developing rats of two thyroid hormone agonists, the TRβ-selective GC-24 and the TRα-selective CO23. Our principal goal was to check whether these compounds were active in the rat brain. Analog activity was assessed by measuring the expression of thyroid hormone target genes in liver, heart, and brain, after administration to hypothyroid rats. GC-24 was very selective for TRβ and lacked activity on the brain. On the other hand, CO23 was active in liver, heart, and brain on genes regulated by either TRα or TRβ. This compound, previously shown to be TRα-selective in tadpoles, displayed no selectivity in the rat in vivo.


2015 ◽  
pp. 353-362 ◽  
Author(s):  
Paul J. Davis ◽  
Thangirala Sudha ◽  
Hung-Yun Lin ◽  
Shaker A. Mousa

Endocrinology ◽  
1973 ◽  
Vol 92 (1) ◽  
pp. 243-250 ◽  
Author(s):  
STACY PSYCHOYOS ◽  
S. MA DANIEL ◽  
ANDREW J. CZERNIK ◽  
HELEN SCHLANGEL BOWERS ◽  
CHARLOTTE D. ATKINS ◽  
...  

2009 ◽  
Vol 297 (6) ◽  
pp. E1238-E1246 ◽  
Author(s):  
Paul J. Davis ◽  
Faith B. Davis ◽  
Hung-Yun Lin ◽  
Shaker A. Mousa ◽  
Min Zhou ◽  
...  

A thyroid hormone receptor on integrin αvβ3 that mediates cell surface-initiated nongenomic actions of thyroid hormone on tumor cell proliferation and on angiogenesis has been described. Transduction of the hormone signal into these recently recognized proliferative effects is by extracellular-regulated kinases 1/2 (ERK1/2). Other nongenomic actions of the hormone may be transduced by phosphatidylinositol 3-kinase (PI3K) and are initiated in cytoplasm or at the cell surface. PI3K-mediated effects are important to angiogenesis or other recently appreciated cell functions but apparently not to tumor cell division. For those actions of thyroid hormone [l-thyroxine (T4) and 3,3′-5-triiodo-l-thyronine (T3)] that begin at the integrin receptor, tetraiodothyroacetic acid (tetrac) is an inhibitor of and probe for the participation of the receptor in downstream intracellular events. In addition, tetrac has actions initiated at the integrin receptor that are unrelated to inhibition of the effects of T4 and T3 but do involve gene transcription in tumor cells. Discussed here are the implications of translating these nongenomic mechanisms of thyroid hormone analogs into clinical cancer cell biology, tumor-related angiogenesis, and modulation of angiogenesis that is not related to cancer.


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