The co-chaperone BAG3 regulates Herpes Simplex Virus replication. - Wikidata - wikimedia - TriplyDB

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

http://www.wikidata.org/entity/Q37016389

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A novel, non-apoptotic role for Scythe/BAT3: a functional switch between the pro- and anti-proliferative roles of p21 during the cell cycle Quantitative proteomics analysis reveals BAG3 as a potential target to suppress severe acute respiratory syndrome coronavirus replication Herpes simplex virus type 1 immediate-early protein ICP22 is required for VICE domain formation during productive viral infection.Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infection AtBAG7, an Arabidopsis Bcl-2-associated athanogene, resides in the endoplasmic reticulum and is involved in the unfolded protein response Chaperone-Mediated Autophagy Protein BAG3 Negatively Regulates Ebola and Marburg VP40-Mediated Egress.BAG3-dependent noncanonical autophagy induced by proteasome inhibition in HepG2 cells Components of nuclear domain 10 bodies regulate varicella-zoster virus replication Bcl2-associated athanogene 3 interactome analysis reveals a new role in modulating proteasome activity.Complementation of a herpes simplex virus ICP0 null mutant by varicella-zoster virus ORF61p BAG3: a multifaceted protein that regulates major cell pathways.Broad action of Hsp90 as a host chaperone required for viral replication.The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease.Autoregulation of co-chaperone BAG3 gene transcription.The RING finger domain of Varicella-Zoster virus ORF61p has E3 ubiquitin ligase activity that is essential for efficient autoubiquitination and dispersion of Sp100-containing nuclear bodies.Chaperone-assisted proteostasis is essential for mechanotransduction in mammalian cells.

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The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

http://www.wikidata.org/entity/Q37016389

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 16 December 2008

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

@en

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

@nl

type

label

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

@en

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

@nl

prefLabel

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

@en

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

@nl

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PNAS.0810656105

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

P1476

The co-chaperone BAG3 regulates Herpes Simplex Virus replication.

@en

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Christos A Kyratsous

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

Saul J Silverstein

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P2860

An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators

PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0

Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections

Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90

Herpes simplex virus 1 alpha regulatory protein ICP0 interacts with and stabilizes the cell cycle regulator cyclin D3

Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells

Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes

Varicella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP0

Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex

The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a

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20912-20917

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scholarly article

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10.1073/PNAS.0810656105

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52

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105

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2008-12-16T00:00:00Z

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23669129

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19088197

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molecular chaperones

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2603433

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