Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain

Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain

Item
http://www.wikidata.org/entity/Q28285548
Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencingSingle-chain estrogen receptors (ERs) reveal that the ERalpha/beta heterodimer emulates functions of the ERalpha dimer in genomic estrogen signaling pathwaysLigand-dependent formation of retinoid receptors, receptor-interacting protein 140 (RIP140), and histone deacetylase complex is mediated by a novel receptor-interacting motif of RIP140The molecular basis of the interaction between the proline-rich SH3-binding motif of PNRC and estrogen receptor alpha.Truncated estrogen receptor product-1 suppresses estrogen receptor transactivation by dimerization with estrogen receptors alpha and beta.DT56a stimulates creatine kinase specific activity in vascular tissues of rats.Estrogen receptor α/β-cofactor motif interactions; interplay of tyrosine 537/488 phosphorylation and LXXLL motifs.The nuclear receptor transcriptional coregulator RIP140.Estradiol repression of tumor necrosis factor-alpha transcription requires estrogen receptor activation function-2 and is enhanced by coactivators.Genomic modelling of the ESR1 Y537S mutation for evaluating function and new therapeutic approaches for metastatic breast cancer.Limiting effects of RIP140 in estrogen signaling: potential mediation of anti-estrogenic effects of retinoic acid.Negative feedback at the level of nuclear receptor coregulation. Self-limitation of retinoid signaling by RIP140.Aspartate 351 of estrogen receptor alpha is not crucial for the antagonist activity of antiestrogens.beta-estradiol stimulation of DNA synthesis requires different PKC isoforms in HepG2 and MCF7 cells.Specificity of thyroid hormone receptor subtype and steroid receptor coactivator-1 on thyroid hormone action.Synthetic retinoids dissociate coactivator binding from corepressor release.
P2860

Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain

Item
http://www.wikidata.org/entity/Q28285548
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Different classes of coactivat ...... receptor ligand binding domain
@ast
Different classes of coactivat ...... receptor ligand binding domain
@en
Different classes of coactivat ...... receptor ligand binding domain
@nl
type
label
Different classes of coactivat ...... receptor ligand binding domain
@ast
Different classes of coactivat ...... receptor ligand binding domain
@en
Different classes of coactivat ...... receptor ligand binding domain
@nl
prefLabel
Different classes of coactivat ...... receptor ligand binding domain
@ast
Different classes of coactivat ...... receptor ligand binding domain
@en
Different classes of coactivat ...... receptor ligand binding domain
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P921
P356
P1433
P1476
Different classes of coactivat ...... receptor ligand binding domain
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P921