Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
We further observed that a heterodimer of TRbeta and retinoid 10 receptor alpha ( RXR alpha ) , either in solution or bound to a DR+4 TRE , recruited SRC 1 in a T 3 dependent manner . ^^^ |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
In this report , we demonstrate that RAR selective ligands have distinct quantitative activation properties which are reflected by their abilities to promote interaction of DNA bound human RXRalpha ( hRXRalpha ) hRARalpha heterodimers with the nuclear receptor coactivator ( NCoA ) SRC 1 in vitro . ^^^ |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
We show that in vitro the steroid receptor coactivator SRC 1 can be recruited by RXRalpha upon addition of its ligand , and to OR 1 upon addition of 22 ( R ) OH cholesterol , demonstrating that the latter can act as a direct ligand to OR 1 . ^^^ Additionally , heterodimerization is sufficient to recruit SRC 1 to OR1 / RXRalpha , indicating SRC 1 as a molecular mediator of dimerization induced activation . ^^^ In transfection experiments , coexpression of a nuclear receptor interacting fragment of SRC 1 abolishes constitutive activation by OR1 / RXRalpha , which can be restored by over expression of full length SRC 1 . ^^^ This constitutes evidence for an in vivo role of SRC 1 in dimerization induced activation by OR1 / RXRalpha . ^^^ Additionally , we show that the nuclear receptor interacting protein RIP 140 binds in vitro to OR 1 and RXRalpha with requirements distinct from those of SRC 1 , and that binding of the two cofactors is competitive . ^^^ |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
To determine whether this enhanced activity is mediated through modulation of the dimerization process or through interaction with coactivators , we performed quantitative protein protein interaction assays with in vitro translated vitamin D receptor ( ivtVDR ) and fusion proteins containing glutathione S transferase ( GST ) and either the ligand binding domain of retinoid 10 receptor ( RXRalpha ) , or the nuclear receptor interacting domain of the steroid receptor coactivator 1 ( SRC 1 ) , or the glucocorticoid receptor interacting protein 1 ( GRIP 1 ) . ^^^ We found that heterodimerization of the ligand binding domains of RXRalpha and VDR was primarily deltanoid dependent as was the interaction of VDR with the SRC 1 or with GRIP 1 . ^^^ |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
The decrease in expression of RXRalpha , beta , and gamma , PPARalpha and delta , and TRalpha and beta , and of the coactivators CBP / p300 , SRC 1 , SRC 3 , TRAP 220 , and PGC 1 and the genes they regulate , induced by LPS in the heart , could account for the decreased expression of key proteins required for fatty acid oxidation and thereby play an important role in cardiac contractility . ^^^ |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
The aim of the study was to test the hypothesis that expression of retinoid receptors ( RARalpha , RARbeta , RARgamma ) , rexinoid receptors ( RXRalpha , RXRbeta ) , thyroid hormone receptors ( TRalpha , TRbeta ) , estrogen receptors ( ERalpha , ERbeta ) , nuclear receptor coregulators ( N CoR , SRC 1 , SMRT ) , and in addition type 1 iodothyronine 5 ' deiodinase ( 5 ' DI ) , EGFR and erb B2 / neu would be different in mammary postlactating tissue in comparison with that of nonlactating mammary gland . ^^^ Using RT PCR , we have shown that expression of RARalpha , RXRalpha , TRalpha , ERalpha , ERbeta , N CoR , SRC 1 , SMRT and EGFR in rat was significantly increased in postlactating mammary gland when compared to that of nonlactating mammary tissue . ^^^ |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
Whereas DEX increased the amount of RXRalpha mRNA , it did not affect the expression of other possible factors such as steroid receptor coactivator 1 and the binding protein of cAMP response element binding protein . ^^^ |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15788 and P19793 |
Pubmed |
SVM Score :0.0 |
NA |
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