The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1.
about
NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomersSUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activitySIP, a novel ankyrin repeat containing protein, sequesters steroid receptor coactivators in the cytoplasmInhibition of androgen receptor activity by histone deacetylase 4 through receptor SUMOylationModification with SUMO. A role in transcriptional regulationSENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1RSUME enhances glucocorticoid receptor SUMOylation and transcriptional activityRole of desumoylation in the development of prostate cancerThe novel PIAS-like protein hZimp10 is a transcriptional co-activator of the p53 tumor suppressorSumoylation of MITF and its related family members TFE3 and TFEBA synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3PIAS1 activates the expression of smooth muscle cell differentiation marker genes by interacting with serum response factor and class I basic helix-loop-helix proteins.The PIAS-like protein Zimp10 is essential for embryonic viability and proper vascular developmentSUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells.Androgen receptor phosphorylation: biological context and functional consequences.Small ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signalingRegulation of the SUMO pathway sensitizes differentiating human endometrial stromal cells to progesterone.A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics.Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif.A novel role for protein inhibitor of activated STAT (PIAS) proteins in modulating the activity of Zimp7, a novel PIAS-like protein, in androgen receptor-mediated transcriptionThe DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification.Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) familyPDSM, a motif for phosphorylation-dependent SUMO modification.SUMOylation regulates the transcriptional repression activity of FOG-2 and its association with GATA-4.The novel PIAS-like protein hZimp10 enhances Smad transcriptional activity.Exploring the association between genetic variation in the SUMO isopeptidase gene USPL1 and breast cancer through integration of data from the population-based GENICA study and external genetic databases.The potential role of estrogen receptors and the SRC family as targets for the treatment of breast cancer.Estrogen receptor alpha and nuclear factor Y coordinately regulate the transcription of the SUMO-conjugating UBC9 gene in MCF-7 breast cancer cells.Sentrin/SUMO specific proteases as novel tissue-selective modulators of vitamin D receptor-mediated signalingHuman adipose-derived mesenchymal stem cells as a new model of spinal and bulbar muscular atrophy.Analysis of the SUMO2 Proteome during HSV-1 Infection.Role of transcriptional coregulator GRIP1 in the anti-inflammatory actions of glucocorticoids.Chromatin modification by SUMO-1 stimulates the promoters of translation machinery genes.Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.Modulation of hormonal signaling in the brain by steroid receptor coactivators.Steroid receptor coactivator-3 as a potential molecular target for cancer therapy.Nuclear receptor coactivators: structural and functional biochemistry.SUMOylation of the farnesoid X receptor (FXR) regulates the expression of FXR target genes.SUMO-mediated inhibition of glucocorticoid receptor synergistic activity depends on stable assembly at the promoter but not on DAXX.Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3.
P2860
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P2860
The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@ast
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@en
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@nl
type
label
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@ast
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@en
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@nl
prefLabel
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@ast
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@en
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@nl
P2093
P2860
P356
P1476
The nuclear receptor interacti ...... covalent attachment of SUMO-1.
@en
P2093
Jorma J Palvimo
Noora Kotaja
Olli A Jänne
Ulla Karvonen
P2860
P304
30283-30288
P356
10.1074/JBC.M204768200
P407
P577
2002-06-11T00:00:00Z