Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase. - Wikidata - awgldk - TriplyDB

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

http://www.wikidata.org/entity/Q35749504

about

The UBXN1 protein associates with autoubiquitinated forms of the BRCA1 tumor suppressor and inhibits its enzymatic function XX ovarian dysgenesis is caused by a PSMC3IP/HOP2 mutation that abolishes coactivation of estrogen-driven transcription An emerging model for BAP1's role in regulating cell cycle progression BRCA1 and estrogen/estrogen receptor in breast cancer: where they interact?A guide for functional analysis of BRCA1 variants of uncertain significance RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase Dysregulation of ubiquitin ligases in cancer BRCA1 and Oxidative Stress BRCA1 targets G2/M cell cycle proteins for ubiquitination and proteasomal degradation Substitution of aspartic acid with glutamic acid at position 67 of the BRCA1 RING domain retains ubiquitin ligase activity and zinc(II) binding with a reduced transition temperature.Decreased BRCA1 confers tamoxifen resistance in breast cancer cells by altering estrogen receptor-coregulator interactions.The UPS: a promising target for breast cancer treatment.BRCA1 regulates acetylation and ubiquitination of estrogen receptor-alpha.Liver X receptor ligands suppress ubiquitination and degradation of LXRalpha by displacing BARD1/BRCA1.Indole-3-carbinol triggers aryl hydrocarbon receptor-dependent estrogen receptor (ER)alpha protein degradation in breast cancer cells disrupting an ERalpha-GATA3 transcriptional cross-regulatory loop.Estrogen receptor coregulators and pioneer factors: the orchestrators of mammary gland cell fate and development.Role of the BCA2 ubiquitin E3 ligase in hormone responsive breast cancer.Apigenin manipulates the ubiquitin-proteasome system to rescue estrogen receptor-β from degradation and induce apoptosis in prostate cancer cells.Small-molecule "BRCA1-mimetics" are antagonists of estrogen receptor-α A Novel Pathway that Links Caveolin-1 Down-Regulation to BRCA1 Dysfunction in Serous Epithelial Ovarian Cancer Cells.Impact of BRCA mutations on female fertility and offspring sex ratio FOXK2 transcription factor suppresses ERα-positive breast cancer cell growth through down-regulating the stability of ERα via mechanism involving BRCA1/BARD1.A role for estrogen receptor phosphorylation in the resistance to tamoxifen.Ubiquitylation of nuclear receptors: new linkages and therapeutic implications.Ubc9 mediates nuclear localization and growth suppression of BRCA1 and BRCA1a proteins Phosphorylation by p38 mitogen-activated protein kinase promotes estrogen receptor α turnover and functional activity via the SCF(Skp2) proteasomal complex.AKT regulates BRCA1 stability in response to hormone signaling.Atypical ubiquitin ligase RNF31: the nuclear factor modulator in breast cancer progression.BRCA1 proteins regulate growth of ovarian cancer cells by tethering Ubc9 ERα phosphorylation at Y537 by Src triggers E6-AP-ERα binding, ERα ubiquitylation, promoter occupancy, and target gene expression.Cellular strategies for making monoubiquitin signals.A DNA repair BRCA1 estrogen receptor and targeted therapy in breast cancer.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?Derailed estrogen signaling and breast cancer: an authentic couple.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 BRCA1-hapoinsufficiency: Unraveling the molecular and cellular basis for tissue-specific cancer Kinetic analysis of interaction of BRCA1 tandem breast cancer c-terminal domains with phosphorylated peptides reveals two binding conformations RAP80 and RNF8, key players in the recruitment of repair proteins to DNA damage sites.

P2860

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P2860

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

http://www.wikidata.org/entity/Q35749504

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

@zh-cn

name

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

@ast

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

@en

type

label

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

@ast

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

@en

prefLabel

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

@ast

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

@en

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PNAS.0610887104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Estrogen receptor alpha is a putative substrate for the BRCA1 ubiquitin ligase.

@en

P2093

Catherine M Eakin

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

Gregory L Finney

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

Michael J Maccoss

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Rachel E Klevit

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P2860

Structural determinants of the BRCA1 : estrogen receptor interaction

Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains

Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Molecular basis of agonism and antagonism in the oestrogen receptor

Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains

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

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

Large-scale analysis of the yeast proteome by multidimensional protein identification technology

Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase

Role of direct interaction in BRCA1 inhibition of estrogen receptor activity

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5794-5799

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scholarly article

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10.1073/PNAS.0610887104

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14

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104

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2007-03-28T00:00:00Z

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1851571

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