Activation of p53 by protein inhibitor of activated Stat1 (PIAS1) - Wikidata - awgldk - TriplyDB

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

http://www.wikidata.org/entity/Q28215308

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PIAS1 interacts with FLASH and enhances its co-activation of c-Myb Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription Modification with SUMO. A role in transcriptional regulation Transcription factor Sp3 is silenced through SUMO modification by PIAS1 PIAS-1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73 The novel PIAS-like protein hZimp10 is a transcriptional co-activator of the p53 tumor suppressor The genetics of the p53 pathway, apoptosis and cancer therapy.PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription Regulation of gene-activation pathways by PIAS proteins in the immune system PIAS1 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 development Protein inhibitor of activated STAT1 interacts with and up-regulates activities of the pro-proliferative transcription factor Krüppel-like factor 5.Differential regulation of the two transcriptional activation domains of the coiled-coil coactivator CoCoA by sumoylation.Negative regulation of NF-kappaB signaling by PIAS1.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 transcription Phosphorylation-dependent interaction of SATB1 and PIAS1 directs SUMO-regulated caspase cleavage of SATB1.Emerging roles of SUMO modification in arthritis.A single-nucleotide variation in a p53-binding site affects nutrient-sensitive human SIRT1 expression ZNF76, a novel transcriptional repressor targeting TATA-binding protein, is modulated by sumoylation.Sumoylation of the net inhibitory domain (NID) is stimulated by PIAS1 and has a negative effect on the transcriptional activity of Net.The novel PIAS-like protein hZimp10 enhances Smad transcriptional activity.Ubiquitin and ubiquitin-like modifications of the p53 family.Roles and regulation of stat family transcription factors in human breast cancer.PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus PML nuclear bodies and apoptosis.The Expression of miR-375 Is Associated with Carcinogenesis in Three Subtypes of Lung Cancer STAT1 modification improves therapeutic effects of interferons on lung cancer cells The SUMO ligase PIAS1 regulates UV-induced apoptosis by recruiting Daxx to SUMOylated foci.Coping with stress: multiple ways to activate p53.Ribozyme-mediated targeting of IkappaBgamma inhibits melanoma invasion and metastasis.Identification of a novel role of ZMIZ2 protein in regulating the activity of the Wnt/β-catenin signaling pathway.Egr1 promotes growth and survival of prostate cancer cells. Identification of novel Egr1 target genes.PIAS1-modulated Smad2/4 complex activation is involved in zinc-induced cancer cell apoptosis.PIASx acts as an Elk-1 coactivator by facilitating derepression.SOCS1, a novel interaction partner of p53 controlling oncogene-induced senescence.A crosstalk between hSiah2 and Pias E3-ligases modulates Pias-dependent activation.Modification of Drosophila p53 by SUMO modulates its transactivation and pro-apoptotic functions.Statin-mediated correction of STAT1 signaling and inducible nitric oxide synthase expression in cystic fibrosis epithelial cells.Increased K+ efflux and apoptosis induced by the potassium channel modulatory protein KChAP/PIAS3beta in prostate cancer cells.PIAS1 selectively inhibits interferon-inducible genes and is important in innate immunity.

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Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

http://www.wikidata.org/entity/Q28215308

description

2002 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մարտին հրատարակված գիտական հոդված

@hy

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

artículu científicu espublizáu en 2002

@ast

im März 2002 veröffentlichter wissenschaftlicher Artikel

@de

scientific article (publication date: 8 March 2002)

@en

vedecký článok (publikovaný 2002/03/08)

@sk

vědecký článek publikovaný v roce 2002

@cs

wetenschappelijk artikel (gepubliceerd op 2002/03/08)

@nl

наукова стаття, опублікована в березні 2002

@uk

name

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@ast

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@en

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@nl

type

label

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@ast

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@en

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@nl

prefLabel

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@ast

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@en

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@nl

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P2860

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P1433

Journal of Biological Chemistry

P1476

Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)

@en

P2093

C Wilson Xu

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

Juliana H Xu

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

Tamar Megidish

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

P2860

p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities

Distinct roles of the NH2- and COOH-terminal domains of the protein inhibitor of activated signal transducer and activator of transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1-Stat1 interaction

Inhibition of Stat1-mediated gene activation by PIAS1

A new human p53 homologue

Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2

Mdm2 promotes the rapid degradation of p53

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

SUMO-1 modification activates the transcriptional response of p53

A Drosophila PIAS homologue negatively regulates stat92E

Regulation of p53 stability by Mdm2

P304

8255-9

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scholarly article

P356

10.1074/JBC.C200001200

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P407

P433

10

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P478

277

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P577

2002-03-08T00:00:00Z

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11788578

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