The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation (Q33911291)

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English	The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

30 July 2017

The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

1 reference

based on heuristic

inferred from title

author name string

D M Lonard

1

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Z Nawaz

2

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

C L Smith

3

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

B W O'Malley

4

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

language of work or name

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publication date

1 June 2000

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

6

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

939-948

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Proteasome-mediated proteolysis of estrogen receptor: a novel component in autologous down-regulation

1 reference

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The proteasome: paradigm of a self-compartmentalizing protease

1 reference

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7 January 2021

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Molecular basis of agonism and antagonism in the oestrogen receptor

1 reference

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7 January 2021

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Degradation of nuclear oncoproteins by the ubiquitin system in vitro

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Structure and functions of the 20S and 26S proteasomes

1 reference

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7 January 2021

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Estrogen receptor synthesis and turnover in MCF-7 breast cancer cells measured by a density shift technique

1 reference

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7 January 2021

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WAF1, a potential mediator of p53 tumor suppression

1 reference

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Implication of proteasome in estrogen receptor degradation

1 reference

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Protein synthesis is not implicated in the ligand-dependent activation of the estrogen receptor in MCF-7 cells

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Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85

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Coactivator peptides have a differential stabilizing effect on the binding of estrogens and antiestrogens with the estrogen receptor

1 reference

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Nuclear receptor coactivators

1 reference

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Interaction of the Ubc9 human homologue with c-Jun and with the glucocorticoid receptor

1 reference

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Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A

1 reference

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A signature motif in transcriptional co-activators mediates binding to nuclear receptors

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AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors

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Estradiol-stimulated proteolytic cleavage of the estrogen receptor in mouse uterus

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Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors

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Estrogen-binding substances of target tissues

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Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway

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Androgen increases androgen receptor protein while decreasing receptor mRNA in LNCaP cells

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Nuclear protein CBP is a coactivator for the transcription factor CREB

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Cloning of a novel receptor expressed in rat prostate and ovary

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The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer

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Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome

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Interaction of thyroid-hormone receptor with a conserved transcriptional mediator

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RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2

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1,25-Dihydroxyvitamin D3 increases nuclear vitamin D3 receptors by blocking ubiquitin/proteasome-mediated degradation in human skin

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Multiple signal input and output domains of the 160-kilodalton nuclear receptor coactivator proteins

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Molecular determinants of the estrogen receptor-coactivator interface

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Cloning of cDNA sequences of hormone-regulated genes from the MCF-7 human breast cancer cell line

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Nuclear receptor coactivators: multiple enzymes, multiple complexes, multiple functions.

1 reference

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Characterization of the subunit nature of nuclear estrogen receptors by chemical cross-linking and dense amino acid labeling

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Characterization of the estrogen receptor and its dynamics in MCF-7 human breast cancer cells using a covalently attaching antiestrogen

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The nuclear receptor ligand-binding domain: structure and function

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ER beta: identification and characterization of a novel human estrogen receptor

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The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily

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Proteasome-dependent degradation of the human estrogen receptor

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Ubiquitination of the Rat Uterine Estrogen Receptor: Dependence on Estradiol

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Sequence and characterization of a coactivator for the steroid hormone receptor superfamily

1 reference

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The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B

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1 reference

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1 reference

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7 January 2021

based on heuristic

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The estrogen receptor in MCF-7 cells: evidence from dense amino acid labeling for rapid turnover and a dimeric model of activated nuclear receptor

1 reference

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The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen

1 reference

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1 reference

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Competition between thyroid hormone receptor-associated protein (TRAP) 220 and transcriptional intermediary factor (TIF) 2 for binding to nuclear receptors. Implications for the recruitment of TRAP and p160 coactivator complexes

1 reference

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Molecular mechanisms of action of steroid/thyroid receptor superfamily members

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1 reference

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10.1016/S1097-2765(00)80259-2

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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