ERR-10: a new repressor in transcriptional signaling activation of estrogen receptor-alpha (Q33292447)

25 July 2017

title

ERR-10: a new repressor in transcriptional signaling activation of estrogen receptor-alpha (English)

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Zeguo Zhao

2

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author name string

Qinghui Meng

1

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Ming Yan

3

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Lixin Zhou

4

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Jiyou Li

5

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Christina Kitt

6

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Gao Bin

7

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Saijun Fan

8

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language of work or name

English

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publication date

1 October 2004

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25 July 2017

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volume

576

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issue

1-2

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page(s)

190-200

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The steroid and thyroid hormone receptor superfamily

25 July 2017

cites work

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The nuclear receptor superfamily: the second decade

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The human estrogen receptor has two independent nonacidic transcriptional activation functions

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Transcription activation by estrogen and progesterone receptors

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Estrogen receptor interaction with co-activators and co-repressors

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Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta

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The multifaceted mechanisms of estradiol and estrogen receptor signaling.

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CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant

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Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator

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Temporally distinct and ligand-specific recruitment of nuclear receptor-interacting peptides and cofactors to subnuclear domains containing the estrogen receptor

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N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif

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Mediator and p300/CBP-steroid receptor coactivator complexes have distinct roles, but function synergistically, during estrogen receptor alpha-dependent transcription with chromatin templates

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Cloning and characterization of RAP250, a novel nuclear receptor coactivator

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Core LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors

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The modified human DNA repair enzyme O(6)-methylguanine-DNA methyltransferase is a negative regulator of estrogen receptor-mediated transcription upon alkylation DNA damage

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Structure-function evaluation of ER alpha and beta interplay with SRC family coactivators. ER selective ligands

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Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor

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The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro

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Role of direct interaction in BRCA1 inhibition of estrogen receptor activity

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Disruption of BRCA1 LXCXE motif alters BRCA1 functional activity and regulation of RB family but not RB protein binding

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Screening λgt Recombinant Clones by Hybridization to Single Plaques in Situ

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21 January 2018

Identifiers

DOI

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25 July 2017

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