Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids (Q24306343)

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12 November 2019

title

Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids (English)

1 reference

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Hepatocyte nuclear factor 4 alpha

12 November 2019

main subject

fatty acid

0 references

1 reference

protein homodimerization activity

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Shawn Williams

12

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12 November 2019

author name string

G Bruce Wisely

1

1 reference

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12 November 2019

Ann B Miller

2

1 reference

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12 November 2019

Roderick G Davis

3

1 reference

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12 November 2019

Alan D Thornquest

4

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12 November 2019

Robert Johnson

5

1 reference

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12 November 2019

Tim Spitzer

6

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12 November 2019

Andrea Sefler

7

1 reference

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12 November 2019

Barry Shearer

8

1 reference

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12 November 2019

John T Moore

9

1 reference

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12 November 2019

Aaron B Miller

10

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12 November 2019

Timothy M Willson

11

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12 November 2019

language of work or name

English

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publication date

1 September 2002

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12 November 2019

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12 November 2019

volume

10

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12 November 2019

page(s)

1225-1234

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12 November 2019

issue

9

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Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily

12 November 2019

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Genotype/phenotype relationships in HNF-4alpha/MODY1: haploinsufficiency is associated with reduced apolipoprotein (AII), apolipoprotein (CIII), lipoprotein(a), and triglyceride levels

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Antagonism between apolipoprotein AI regulatory protein 1, Ear3/COUP-TF, and hepatocyte nuclear factor 4 modulates apolipoprotein CIII gene expression in liver and intestinal cells

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HNF-4 increases activity of the rat Apo A1 gene

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The maturity-onset diabetes of the young (MODY1) transcription factor HNF4alpha regulates expression of genes required for glucose transport and metabolism

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SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4.

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Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1

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7 January 2021

Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4α

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Analysis of protein dimerization and ligand binding of orphan receptor HNF4alpha

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Natural ligands of nuclear receptors have conserved volumes

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Atomic structure of progesterone complexed with its receptor

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Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations

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

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Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors

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7 January 2021

Exclusive homodimerization of the orphan receptor hepatocyte nuclear factor 4 defines a new subclass of nuclear receptors

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7 January 2021

The DNA binding domain of hepatocyte nuclear factor 4 mediates cooperative, specific binding to DNA and heterodimerization with the retinoid X receptor alpha

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7 January 2021

Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

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Molecular basis of agonism and antagonism in the oestrogen receptor

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Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma

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Crystal structure of the ligand-binding domain of the ultraspiracle protein USP, the ortholog of retinoid X receptors in insects

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7 January 2021

The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation

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Molecular recognition of fatty acids by peroxisome proliferator-activated receptors

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X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation.

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7 January 2021

Origins and evolutionary diversification of the nuclear receptor superfamily

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7 January 2021

Naturally occurring mutations in the human HNF4alpha gene impair the function of the transcription factor to a varying degree

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

3575249

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12220494%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

3575249

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

3575249