Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins. - Wikidata - awgldk - TriplyDB

Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins.

Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins.

http://www.wikidata.org/entity/Q37721763

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The function, regulation and therapeutic implications of the tumor suppressor protein, PML Mapping the SUMOylated landscape PML nuclear bodies: regulation, function and therapeutic perspectives.Comparative ultrastructure of CRM1-Nucleolar bodies (CNoBs), Intranucleolar bodies (INBs) and hybrid PML/p62 bodies uncovers new facets of nuclear body dynamic and diversity Establishment of HSV1 latency in immunodeficient mice facilitates efficient in vivo reactivation.Sustained accumulation of prelamin A and depletion of lamin A/C both cause oxidative stress and mitochondrial dysfunction but induce different cell fates PML nuclear bodies: assembly and oxidative stress-sensitive sumoylation.PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence.ZNF32 protects against oxidative stress-induced apoptosis by modulating C1QBP transcription.SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies.Pathogenic Mutations in the Valosin-containing Protein/p97(VCP) N-domain Inhibit the SUMOylation of VCP and Lead to Impaired Stress Response.Promyelocytic Leukemia Protein (PML) Controls Listeria monocytogenes Infection.p53 as an Effector or Inhibitor of Therapy Response.Compositional Control of Phase-Separated Cellular Bodies.Protein quality control in the nucleus.HIF-1α SUMOylation affects the stability and transcriptional activity of HIF-1α in human lens epithelial cells.Herpesvirus Latency: On the Importance of Positioning Oneself.Arsenic trioxide and angiotensin II have inhibitory effects on HERG protein expression: Evidence for the role of PML SUMOylation.Interferon controls SUMO availability via the Lin28 and let-7 axis to impede virus replication.PML is a ROS sensor activating p53 upon oxidative stress.Respiratory syncytial virus induces NRF2 degradation through a promyelocytic leukemia protein - ring finger protein 4 dependent pathway.Ataxia telangiectasia and rad3 related (ATR)-promyelocytic leukemia protein (PML) pathway of the DNA damage response in the brain of rats administered arsenic trioxide.Subcellular Trafficking of the Papillomavirus Genome during Initial Infection: The Remarkable Abilities of Minor Capsid Protein L2.CENP-B protects centromere chromatin integrity by facilitating histone deposition via the H3.3-specific chaperone Daxx.Generation of specific inhibitors of SUMO-1- and SUMO-2/3-mediated protein-protein interactions using Affimer (Adhiron) technology.C-terminal motifs in promyelocytic leukemia protein isoforms critically regulate PML nuclear body formation.Bypassing Border Control: Nuclear Envelope Rupture in Disease.Localization and regulation of PML bodies in the adult mouse brain.PML: Regulation and multifaceted function beyond tumor suppression.Manipulating PML SUMOylation via Silencing UBC9 and RNF4 Regulates Cardiac Fibrosis.Detection of Protein SUMOylation In Situ by Proximity Ligation Assays.Retinoic acid and arsenic trioxide sensitize acute promyelocytic leukemia cells to ER stress.A CK2-RNF4 interplay coordinates non-canonical SUMOylation and degradation of nuclear receptor FXR.Multimodal Light Microscopy Approaches to Reveal Structural and Functional Properties of Promyelocytic Leukemia Nuclear Bodies.RING tetramerization is required for nuclear body biogenesis and PML sumoylation.Quantitative SUMO proteomics reveals the modulation of several PML nuclear body associated proteins and an anti-senescence function of UBC9.

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P2860

Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins.

http://www.wikidata.org/entity/Q37721763

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on March 2014

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Oxidative stress-induced assem ...... moylation of partner proteins.

@en

Oxidative stress-induced assem ...... moylation of partner proteins.

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type

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Oxidative stress-induced assem ...... moylation of partner proteins.

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Oxidative stress-induced assem ...... moylation of partner proteins.

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Oxidative stress-induced assem ...... moylation of partner proteins.

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Oxidative stress-induced assem ...... moylation of partner proteins.

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Journal of Cell Biology

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Oxidative stress-induced assem ...... moylation of partner proteins.

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P2093

Caroline Berthier

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Florence Jollivet

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Marion Jeanne

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Michiko Niwa-Kawakita

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Niclas Setterblad

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Omar Ferhi

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Orestis Faklaris

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Shirine Benhenda

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Umut Sahin

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Valérie Lallemand-Breitenbach

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P2860

SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation

PML nuclear bodies

Role of SUMO-1-modified PML in nuclear body formation

The DNA topoisomerase I binding protein topors as a novel cellular target for SUMO-1 modification: characterization of domains necessary for subcellular localization and sumolation

Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.

Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex.

The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA

The mechanisms of PML-nuclear body formation

Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation

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931-945

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scholarly article

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10.1083/JCB.201305148

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6

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204

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2014-03-01T00:00:00Z

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260874656

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24637324

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3998805

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