Identification of DRIP205 as a coactivator for the Farnesoid X receptor. (Q40547550)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15187081%20AND%20SRC:MED&resulttype=core&format=json

29 December 2019

title

Identification of DRIP205 as a coactivator for the Farnesoid X receptor (English)

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29 December 2019

1

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29 December 2019

author name string

Leonard P Freedman

series ordinal

2

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29 December 2019

Michael J Garabedian

series ordinal

3

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29 December 2019

language of work or name

English

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publication date

8 June 2004

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Journal of Biological Chemistry

29 December 2019

published in

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29 December 2019

volume

279

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29 December 2019

issue

35

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29 December 2019

page(s)

36184-36191

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Regulation of bile acid biosynthesis

29 December 2019

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Identification of the DNA binding specificity and potential target genes for the farnesoid X-activated receptor

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Regulation of multidrug resistance-associated protein 2 (ABCC2) by the nuclear receptors pregnane X receptor, farnesoid X-activated receptor, and constitutive androstane receptor

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Bile acids induce the expression of the human peroxisome proliferator-activated receptor alpha gene via activation of the farnesoid X receptor

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The Human Apolipoprotein AV Gene Is Regulated by Peroxisome Proliferator-activated Receptor-α and Contains a Novel Farnesoid X-activated Receptor Response Element

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Human bile salt export pump promoter is transactivated by the farnesoid X receptor/bile acid receptor.

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Farnesoid X Receptor Activates Transcription of the Phospholipid Pump MDR3

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Farnesoid X Receptor Regulates Bile Acid-Amino Acid Conjugation

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Farnesoid X receptor agonists suppress hepatic apolipoprotein CIII expression

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Regulated expression of the apolipoprotein E/C-I/C-IV/C-II gene cluster in murine and human macrophages. A critical role for nuclear liver X receptors alpha and beta

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Correlation of farnesoid X receptor coactivator recruitment and cholesterol 7alpha-hydroxylase gene repression by bile acids

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Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex

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A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system

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Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors

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Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor

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The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion

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Coactivators for the Orphan Nuclear Receptor ROR

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Polyamines modulate the interaction between nuclear receptors and vitamin D receptor-interacting protein 205

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M405126200

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15187081%20AND%20SRC:MED&resulttype=core&format=json

29 December 2019

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