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Refinado por: Nome da Publicação: Molecular Endocrinology remover assunto: Receptors, Calcitriol - Metabolism remover
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1
1 alpha,25-dihydroxyvitamin D3 transrepresses retinoic acid transcriptional activity via vitamin D receptor in myeloid cells
1 alpha,25-dihydroxyvitamin D3 transrepresses retinoic acid transcriptional activity via vitamin D receptor in myeloid cells
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1 alpha,25-dihydroxyvitamin D3 transrepresses retinoic acid transcriptional activity via vitamin D receptor in myeloid cells

Bastie, Jean-Noël ; Balitrand, Nicole ; Guidez, Fabien ; Guillemot, Isabelle ; Larghero, Jerome ; Calabresse, Cynthia ; Chomienne, Christine ; Delva, Laurent

Molecular endocrinology (Baltimore, Md.), 2004-11, Vol.18 (11), p.2685-2699 [Periódico revisado por pares]

United States

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2
1Alpha,25(OH)2D3-induced transrepression by vitamin D receptor through E-box-type elements in the human parathyroid hormone gene promoter
1Alpha,25(OH)2D3-induced transrepression by vitamin D receptor through E-box-type elements in the human parathyroid hormone gene promoter
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1Alpha,25(OH)2D3-induced transrepression by vitamin D receptor through E-box-type elements in the human parathyroid hormone gene promoter

Kim, Mi-sun ; Fujiki, Ryoji ; Murayama, Akiko ; Kitagawa, Hirochika ; Yamaoka, Kazuyoshi ; Yamamoto, Yoko ; Mihara, Masatomo ; Takeyama, Ken-ichi ; Kato, Shigeaki

Molecular endocrinology (Baltimore, Md.), 2007-02, Vol.21 (2), p.334-342 [Periódico revisado por pares]

United States

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3
A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation
A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation
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A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation

Whitfield, G K ; Hsieh, J C ; Nakajima, S ; MacDonald, P N ; Thompson, P D ; Jurutka, P W ; Haussler, C A ; Haussler, M R

Molecular endocrinology (Baltimore, Md.), 1995-09, Vol.9 (9), p.1166-1179 [Periódico revisado por pares]

United States

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4
A Novel Bile Acid-Activated Vitamin D Receptor Signaling in Human Hepatocytes
A Novel Bile Acid-Activated Vitamin D Receptor Signaling in Human Hepatocytes
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A Novel Bile Acid-Activated Vitamin D Receptor Signaling in Human Hepatocytes

Han, Shuxin ; Li, Tiangang ; Ellis, Ewa ; Strom, Stephen ; Chiang, John Y. L

Molecular endocrinology (Baltimore, Md.), 2010-06, Vol.24 (6), p.1151-1164 [Periódico revisado por pares]

United States: Endocrine Society

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5
Analysis of vitamin D analog-induced heterodimerization of vitamin D receptor with retinoid X receptor using the yeast two-hybrid system
Analysis of vitamin D analog-induced heterodimerization of vitamin D receptor with retinoid X receptor using the yeast two-hybrid system
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Analysis of vitamin D analog-induced heterodimerization of vitamin D receptor with retinoid X receptor using the yeast two-hybrid system

Zhao, X Y ; Eccleshall, T R ; Krishnan, A V ; Gross, C ; Feldman, D

Molecular endocrinology (Baltimore, Md.), 1997-03, Vol.11 (3), p.366-378 [Periódico revisado por pares]

United States

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6
Antagonist- and Inverse Agonist-Driven Interactions of the Vitamin D Receptor and the Constitutive Androstane Receptor with Corepressor Protein
Antagonist- and Inverse Agonist-Driven Interactions of the Vitamin D Receptor and the Constitutive Androstane Receptor with Corepressor Protein
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Antagonist- and Inverse Agonist-Driven Interactions of the Vitamin D Receptor and the Constitutive Androstane Receptor with Corepressor Protein

Lempiäinen, Harri ; Molnár, Ferdinand ; Macias Gonzalez, Manuel ; Peräkylä, Mikael ; Carlberg, Carsten

Molecular endocrinology (Baltimore, Md.), 2005-09, Vol.19 (9), p.2258-2272 [Periódico revisado por pares]

United States: Endocrine Society

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7
Calreticulin inhibits vitamin D's action on the PTH gene in vitro and may prevent vitamin D's effect in vivo in hypocalcemic rats
Calreticulin inhibits vitamin D's action on the PTH gene in vitro and may prevent vitamin D's effect in vivo in hypocalcemic rats
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Calreticulin inhibits vitamin D's action on the PTH gene in vitro and may prevent vitamin D's effect in vivo in hypocalcemic rats

Sela-Brown, A ; Russell, J ; Koszewski, N J ; Michalak, M ; Naveh-Many, T ; Silver, J

Molecular endocrinology (Baltimore, Md.), 1998-08, Vol.12 (8), p.1193-1200 [Periódico revisado por pares]

United States

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8
Distinct conformations of vitamin D receptor/retinoid X receptor-alpha heterodimers are specified by dinucleotide differences in the vitamin D-responsive elements of the osteocalcin and osteopontin genes
Distinct conformations of vitamin D receptor/retinoid X receptor-alpha heterodimers are specified by dinucleotide differences in the vitamin D-responsive elements of the osteocalcin and osteopontin genes
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Distinct conformations of vitamin D receptor/retinoid X receptor-alpha heterodimers are specified by dinucleotide differences in the vitamin D-responsive elements of the osteocalcin and osteopontin genes

Staal, A ; van Wijnen, A J ; Birkenhäger, J C ; Pols, H A ; Prahl, J ; DeLuca, H ; Gaub, M P ; Lian, J B ; Stein, G S ; van Leeuwen, J P ; Stein, J L

Molecular endocrinology (Baltimore, Md.), 1996-11, Vol.10 (11), p.1444-1456 [Periódico revisado por pares]

United States

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9
DNA sequences that act as high affinity targets for the vitamin D3 receptor in the absence of the retinoid X receptor
DNA sequences that act as high affinity targets for the vitamin D3 receptor in the absence of the retinoid X receptor
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DNA sequences that act as high affinity targets for the vitamin D3 receptor in the absence of the retinoid X receptor

FREEDMAN, L. P ; ARCE, V ; FERNANDEZ, R. P

Molecular endocrinology (Baltimore, Md.), 1994-03, Vol.8 (3), p.265-273 [Periódico revisado por pares]

Bethesda, MD: Endocrine Society

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10
Enhancement of VDR-mediated transcription by phosphorylation: correlation with increased interaction between the VDR and DRIP205, a subunit of the VDR-interacting protein coactivator complex
Enhancement of VDR-mediated transcription by phosphorylation: correlation with increased interaction between the VDR and DRIP205, a subunit of the VDR-interacting protein coactivator complex
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Enhancement of VDR-mediated transcription by phosphorylation: correlation with increased interaction between the VDR and DRIP205, a subunit of the VDR-interacting protein coactivator complex

Barletta, Frank ; Freedman, Leonard P ; Christakos, Sylvia

Molecular endocrinology (Baltimore, Md.), 2002-02, Vol.16 (2), p.301 [Periódico revisado por pares]

United States

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