Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor. - Wikidata - wikimedia - TriplyDB

Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.

Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.

http://www.wikidata.org/entity/Q40493369

about

The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates CHIP: A new modulator of human malignant disorders Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase Regulation of the cytoplasmic quality control protein degradation pathway by BAG2 Systematic Proteomic Identification of the Heat Shock Proteins (Hsp) that Interact with Estrogen Receptor Alpha (ERα) and Biochemical Characterization of the ERα-Hsp70 Interaction GSK3β controls epithelial-mesenchymal transition and tumor metastasis by CHIP-mediated degradation of Slug Systematic mapping of posttranslational modifications in human estrogen receptor-alpha with emphasis on novel phosphorylation sites The UPS: a promising target for breast cancer treatment.Coordinated regulation of nuclear receptor CAR by CCRP/DNAJC7, HSP70 and the ubiquitin-proteasome system.Liver X receptor ligands suppress ubiquitination and degradation of LXRalpha by displacing BARD1/BRCA1.Estrogen inhibits transforming growth factor beta signaling by promoting Smad2/3 degradation Suppression of estrogen receptor transcriptional activity by connective tissue growth factor.Phosphorylation of estrogen receptor beta at serine 105 is associated with good prognosis in breast cancer.Proteasome functioning in breast cancer: connection with clinical-pathological factors A specific CpG site demethylation in the human interleukin 2 gene promoter is an epigenetic memory.Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.Molecular mechanisms of oestrogen and SERMs in endometrial carcinogenesis.A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseases Liganded and unliganded activation of estrogen receptor and hormone replacement therapies.C terminus of Hsc70-interacting protein (CHIP)-mediated degradation of hippocampal estrogen receptor-alpha and the critical period hypothesis of estrogen neuroprotection.Isoform-specific regulation of a steroid hormone nuclear receptor by an E3 ubiquitin ligase in Drosophila melanogaster Regulation of proto-oncogenic dbl by chaperone-controlled, ubiquitin-mediated degradation.Acquisition of estrogen independence induces TOB1-related mechanisms supporting breast cancer cell proliferation.Ubiquitin-interaction motifs of RAP80 are critical in its regulation of estrogen receptor alpha.Back to your heart: ubiquitin proteasome system-regulated signal transduction Post-translational modifications of nuclear receptors and human disease Reciprocal Regulation of ERα and ERβ Stability and Activity by Diptoindonesin G.MDC1 Enhances Estrogen Receptor-mediated Transactivation and Contributes to Breast Cancer Suppression.A novel prenylflavone restricts breast cancer cell growth through AhR-mediated destabilization of ERα protein Tumor suppressor function of RUNX3 in breast cancer CAR and PXR: the xenobiotic-sensing receptors.Previous Midlife Oestradiol Treatment Results in Long-Term Maintenance of Hippocampal Oestrogen Receptor α Levels in Ovariectomised Rats: Mechanisms and Implications for Memory.PES1 promotes breast cancer by differentially regulating ERα and ERβ.MKKS is a centrosome-shuttling protein degraded by disease-causing mutations via CHIP-mediated ubiquitination.Regulatory function of the P295-T311 motif of the estrogen receptor alpha - does proteasomal degradation of the receptor induce emergence of peptides implicated in estrogenic responses?Aptamer-Enabled Manipulation of the Hsp70 Chaperone System Suggests a Novel Strategy for Targeted Ubiquitination.Phosphorylation of activation function-1 regulates proteasome-dependent nuclear mobility and E6-associated protein ubiquitin ligase recruitment to the estrogen receptor beta Estrogen receptor-alpha hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome

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Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.

http://www.wikidata.org/entity/Q40493369

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

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name

Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.

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type

label

Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.

@en

prefLabel

Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.

@en

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SJ.EMBOJ.7600472

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The EMBO Journal

P1476

Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.

@en

P2093

Akiko Murayama

http://www.w3.org/2001/XMLSchema#string

Junn Yanagisawa

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Keiji Tanaka

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Ken Ichikawa

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Shigeaki Kato

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Tadashi Baba

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Tomoki Chiba

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Yoh-ichi Kawabe

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Yukiyo Tateishi

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P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity

Interaction of thyroid-hormone receptor with a conserved transcriptional mediator

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

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

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

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

The nuclear receptor superfamily: the second decade

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

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4813-4823

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10.1038/SJ.EMBOJ.7600472

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15538384

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ubiquitin-proteasome system

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535086

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