Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues (Q24292691)

vitamin D receptor binding

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Vitamin D (1,25-dihydroxyvitamin D3) receptor

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Glutamate receptor interacting protein 1

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5

John A Eisman

John A

Eisman

1 reference

26 October 2023

Janelle B Barry

1

Janelle B

Barry

1 reference

26 October 2023

Gary M Leong

2

Gary M

Leong

1 reference

26 October 2023

W Bret Church

3

W Bret

Church

1 reference

26 October 2023

Laura L Issa

4

Laura L

Issa

1 reference

26 October 2023

Edith M Gardiner

6

Edith M

Journal of Biological Chemistry

Gardiner

1 reference

26 October 2023

language of work or name

English

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publication date

7 March 2003

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published in

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volume

278

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page(s)

8224-8

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issue

10

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The interaction of the vitamin D receptor with nuclear receptor corepressors and coactivators

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Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription

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The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42

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Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription

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Retinoid X receptor and peroxisome proliferator-activated receptor activate an estrogen responsive gene independent of the estrogen receptor.

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Vitamin D receptor contains multiple dimerization interfaces that are functionally different

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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

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The polymorphic N terminus in human vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB.

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Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone

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Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Interaction between the retinoid X receptor and transcription factor IIB is ligand-dependent in vivo

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