Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain.
about
Mammalian MST2 kinase and human Salvador activate and reduce estrogen receptor alpha in the absence of ligandSPBP is a phosphoserine-specific repressor of estrogen receptor alpha.Phosphorylation of estrogen receptor alpha serine 167 is predictive of response to endocrine therapy and increases postrelapse survival in metastatic breast cancer.The cell-specific activity of the estrogen receptor alpha may be fine-tuned by phosphorylation-induced structural gymnastics.Extracellular signal-regulated kinase 7, a regulator of hormone-dependent estrogen receptor destruction.Characterization of mouse Rsk4 as an inhibitor of fibroblast growth factor-RAS-extracellular signal-regulated kinase signalingc-Abl regulates estrogen receptor alpha transcription activity through its stabilization by phosphorylation.Development of a RSK Inhibitor as a Novel Therapy for Triple-Negative Breast Cancer.RSK2 Binding Models Delineate Key Features for ActivityRSK in tumorigenesis: connections to steroid signaling.Codependent functions of RSK2 and the apoptosis-promoting factor TIA-1 in stress granule assembly and cell survivalActivation of p90 ribosomal S6 kinase by ORF45 of Kaposi's sarcoma-associated herpesvirus and its role in viral lytic replicationIdentification of four novel phosphorylation sites in estrogen receptor alpha: impact on receptor-dependent gene expression and phosphorylation by protein kinase CK2.CDC2 mediates progestin initiated endometrial stromal cell proliferation: a PR signaling to gene expression independently of its binding to chromatin.A fully dissociated compound of plant origin for inflammatory gene repressionExploiting MEK inhibitor-mediated activation of ERα for therapeutic intervention in ER-positive ovarian carcinoma.Liganded and unliganded activation of estrogen receptor and hormone replacement therapies.DGCR14 induces Il17a gene expression through the RORγ/BAZ1B/RSKS2 complex.Ubiquitylation of nuclear receptors: new linkages and therapeutic implications.Kinases and protein phosphorylation as regulators of steroid hormone actionPPARgamma and MEK Interactions in CancerA Rising Cancer Prevention Target of RSK2 in Human Skin Cancer.Anti-invasive and antimetastatic activities of ribosomal protein S6 kinase 4 in breast cancer cellsSteroid receptor phosphorylation: Assigning function to site-specific phosphorylation.RSK2 signals through stathmin to promote microtubule dynamics and tumor metastasismTOR inhibition in breast cancer: unraveling the complex mechanisms of mTOR signal transduction and its clinical implications in therapy.Ribosomal S6 kinase (RSK) modulators: a patent review.Nur77 is phosphorylated in cells by RSK in response to mitogenic stimulation.Comparative analysis of nuclear estrogen receptor alpha and beta interactomes in breast cancer cells.A novel serine phosphorylation site detected in the N-terminal domain of estrogen receptor isolated from human breast cancer cells.ERpS294 is a biomarker of ligand or mutational ERα activation and a breast cancer target for CDK2 inhibition.The promise and challenges of targeting RSK for the treatment of cancer.
P2860
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P2860
Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Rsk2 allosterically activates ...... to the hormone-binding domain
@nl
Rsk2 allosterically activates ...... to the hormone-binding domain.
@ast
Rsk2 allosterically activates ...... to the hormone-binding domain.
@en
Rsk2 allosterically activates ...... to the hormone-binding domain.
@en-gb
type
label
Rsk2 allosterically activates ...... to the hormone-binding domain
@nl
Rsk2 allosterically activates ...... to the hormone-binding domain.
@ast
Rsk2 allosterically activates ...... to the hormone-binding domain.
@en
Rsk2 allosterically activates ...... to the hormone-binding domain.
@en-gb
prefLabel
Rsk2 allosterically activates ...... to the hormone-binding domain
@nl
Rsk2 allosterically activates ...... to the hormone-binding domain.
@ast
Rsk2 allosterically activates ...... to the hormone-binding domain.
@en
Rsk2 allosterically activates ...... to the hormone-binding domain.
@en-gb
P2093
P2860
P356
P1433
P1476
Rsk2 allosterically activates ...... to the hormone-binding domain.
@en
P2093
Lannigan DA
Poteet-Smith CE
P2860
P304
P356
10.1093/EMBOJ/20.13.3484
P407
P577
2001-07-01T00:00:00Z