About: Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR

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About: Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	artículu científicu espublizáu en 1996 (ast) vědecký článek publikovaný v roce 1996 (cs) 1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в грудні 1996 (uk) 1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في ديسمبر 1996) (ar) vedecký článok (publikovaný 1996/12/01) (sk) wetenschappelijk artikel (gepubliceerd op 1996/12/01) (nl) article scientifique publié en 1996 (fr) scientific journal article (en) im Dezember 1996 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28586882-F8C16E7E-1DDC-41D0-B6C9-0FC7B8A55C6D
publication date	1996-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28586882-05C86073-C956-4B91-977D-1AFEE6A2AE80
language of work or name	English
author name string	wds:Q28586882-12919352-A087-463E-9E1C-B4F56CF55E9B wds:Q28586882-36175EE8-3DA1-496E-B1D3-23C303DD1CBF wds:Q28586882-48C42783-33D7-4FA6-A469-D28CFF8FD411 wds:Q28586882-D09C8CE8-9BC2-41B6-AFAE-7240B6746B69
OpenCitations bibliographic resource ID	wds:Q28586882-270063EA-C6BB-41F2-B528-02D9D486986C
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2918209
author name string	D. D. Moore M. J. Mahon W. Seol Y. K. Lee
OpenCitations bibliographic resource ID	2918209
rdfs:label	Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (en) Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (nl) Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (ast)
skos:prefLabel	Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (en) Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (nl) Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (ast)
name	Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (en) Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (nl) Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (ast)
title	wds:Q28586882-B95D6DBB-FFDD-41E9-9CF1-182EDB4EA613
title	Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR (en)
page(s)	wds:Q28586882-CE03FD71-F02F-4400-A7B5-7EBFE828D701
page(s)	1646–1655
instance of	wds:Q28586882-5BC121F9-9CE8-4056-9791-131800C02592
instance of	scholarly article
main subject	wds:Q28586882-A1AA088C-8355-4361-9E38-51B9A30275D3
main subject	Nuclear receptor corepressor 1
PubMed ID	wds:Q28586882-BE6BCFB0-504F-4676-A95C-995BA9EDFBCF
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8961273
PubMed ID	8961273
published in	wds:Q28586882-989CCCBB-0E13-4FB9-97C4-0C9D0015DDF6
published in	Molecular Endocrinology
issue	wds:Q28586882-7164B6AE-F499-4F65-A13C-EC6533CA7909
volume	wds:Q28586882-ADCBCE1F-E0D4-4C25-8E0E-4137B677F80C
issue	12
volume	10
DOI	wds:Q28586882-AD504C00-1927-454C-925D-381E79E523CB wds:Q28586882-DDF83D1B-3409-4079-B613-45F9E4A9BD03
DOI	http://dx.doi.org/10.1210/ME.10.12.1646 http://dx.doi.org/10.1210/MEND.10.12.8961273
DOI	10.1210/ME.10.12.1646 10.1210/MEND.10.12.8961273
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28586882
is cites work of	The corepressor N-CoR and its variants RIP13a and RIP13Delta1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70. The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression A chicken ovalbumin upstream promoter transcription factor I (COUP-TFI) complex represses expression of the gene encoding tumor necrosis factor alpha-induced protein 8 (TNFAIP8). A unique secondary-structure switch controls constitutive gene repression by retinoic acid receptor Transcriptional repression by nuclear hormone receptors Mechanistic principles in NR box-dependent interaction between nuclear hormone receptors and the coactivator TIF2 Nuclear receptor coactivators: multiple enzymes, multiple complexes, multiple functions. Nuclear receptor DAX-1 recruits nuclear receptor corepressor N-CoR to steroidogenic factor 1 Activation of the orphan receptor RIP14 by retinoids The histone acetylase PCAF is a nuclear receptor coactivator. Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia A histone deacetylase corepressor complex regulates the Notch signal transduction pathway Corepressors: custom tailoring and alterations while you wait The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II) Alternative mRNA splicing of SMRT creates functional diversity by generating corepressor isoforms with different affinities for different nuclear receptors The SMRT corepressor is regulated by a MEK-1 kinase pathway: inhibition of corepressor function is associated with SMRT phosphorylation and nuclear export Signaling by tyrosine kinases negatively regulates the interaction between transcription factors and SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) corepressor Transcriptional repression by COUP-TF II is dependent on the C-terminal domain and involves the N-CoR variant, RIP13delta1. The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia Differential recognition of liganded and unliganded thyroid hormone receptor by retinoid X receptor regulates transcriptional repression LRRK2 regulates synaptic vesicle endocytosis SMRT and N-CoR corepressors are regulated by distinct kinase signaling pathways Transgenic targeting of a dominant negative corepressor to liver blocks basal repression by thyroid hormone receptor and increases cell proliferation Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors Molecular determinants of nuclear receptor-corepressor interaction Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes Transcriptional repression by the SMRT-mSin3 corepressor: multiple interactions, multiple mechanisms, and a potential role for TFIIB. One- plus two-hybrid system, a novel yeast genetic selection for specific missense mutations disrupting protein/protein interactions Resistance to thyroid hormone (RTH) syndrome reveals novel determinants regulating interaction of T3 receptor with corepressor Isolation of a novel family of C(2)H(2) zinc finger proteins implicated in transcriptional repression mediated by chicken ovalbumin upstream promoter transcription factor (COUP-TF) orphan nuclear receptors Characterization of the repressor function of the nuclear orphan receptor retinoid receptor-related testis-associated receptor/germ cell nuclear factor Coactivators and corepressors as mediators of nuclear receptor function: an update Thyroid hormone response elements differentially modulate the interactions of thyroid hormone receptors with two receptor binding domains in the steroid receptor coactivator-1. Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein Transcriptional silencing is defined by isoform- and heterodimer-specific interactions between nuclear hormone receptors and corepressors Novel receptor interaction and repression domains in the orphan receptor SHP. A novel role for helix 12 of retinoid X receptor in regulating repression T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha

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