A core viral protein binds host nucleosomes to sequester immune danger signals. - Test2 - elhamkhani - TriplyDB

A core viral protein binds host nucleosomes to sequester immune danger signals.

A core viral protein binds host nucleosomes to sequester immune danger signals.

http://www.wikidata.org/entity/Q30389993

about

The adenovirus major core protein VII is dispensable for virion assembly but is essential for lytic infection.Chromosome Conformation Capture for Research on Innate Antiviral Immunity.Adenovirus core protein VII down-regulates the DNA damage response on the host genome.Adenovirus sensing by the immune system.Time-resolved Global and Chromatin Proteomics during Herpes Simplex Virus Type 1 (HSV-1) Infection.Differential Salt Fractionation of Nuclei to Analyze Chromatin-associated Proteins from Cultured Mammalian Cells.Omega-3 polyunsaturated fatty acid supplementation attenuates microglial-induced inflammation by inhibiting the HMGB1/TLR4/NF-κB pathway following experimental traumatic brain injury.Epigenetic Regulation of Viral Biological Processes.HAdV protein V core protein is targeted by the host SUMOylation machinery to limit essential viral functions.Human adenovirus infection causes the cellular MKRN1 E3 ubiquitin ligase degradation involving the viral core protein pVII.Longitudinal profiling of the lung microbiome in the AERIS study demonstrates repeatability of bacterial and eosinophilic COPD exacerbations.Mimicry of cellular A kinase anchoring proteins is a conserved and critical function of E1A across various human adenovirus species.MERS-CoV and H5N1 influenza virus antagonize antigen presentation by altering the epigenetic landscape.The genome of a prasinoviruses-related freshwater virus reveals unusual diversity of phycodnaviruses.The 38K-Mediated Specific Dephosphorylation of the Viral Core Protein P6.9 Plays an Important Role in the Nucleocapsid Assembly of Autographa californica Multiple Nucleopolyhedrovirus.A Screen for Epstein-Barr Virus Proteins that Inhibit the DNA Damage Response Reveals a Novel Histone Binding Protein.Viral proteins as a potential driver of histone depletion in dinoflagellates.Hacking the Cell: Network Intrusion and Exploitation by Adenovirus E1A.labelling of adenovirus DNA identifies chromatin anchoring and biphasic genome replication Drawing on disorder: How viruses use histone mimicry to their advantage Modulation of airway hyperresponsiveness by rhinovirus exposure

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P2860

A core viral protein binds host nucleosomes to sequester immune danger signals.

http://www.wikidata.org/entity/Q30389993

description

2016 nî lūn-bûn

@nan

2016 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

name

A core viral protein binds host nucleosomes to sequester immune danger signals.

@ast

A core viral protein binds host nucleosomes to sequester immune danger signals.

@en

type

label

A core viral protein binds host nucleosomes to sequester immune danger signals.

@ast

A core viral protein binds host nucleosomes to sequester immune danger signals.

@en

prefLabel

A core viral protein binds host nucleosomes to sequester immune danger signals.

@ast

A core viral protein binds host nucleosomes to sequester immune danger signals.

@en

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A core viral protein binds host nucleosomes to sequester immune danger signals

@en

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Ben E Black

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

Benjamin A Garcia

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

Christin Herrmann

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

Daphne C Avgousti

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

Emigdio D Reyes

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

G Scott Worthen

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

Joana Petrescu

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

Katarzyna Kulej

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

Matthew D Weitzman

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

Neha J Pancholi

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

P2860

Novel role of PKR in inflammasome activation and HMGB1 release

Suppression of the antiviral response by an influenza histone mimic

The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres

Chromosomes. CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere.

Chromatin modifications and their function

Release of chromatin protein HMGB1 by necrotic cells triggers inflammation

Global quantification of mammalian gene expression control

High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells

P2888

P304

173-177

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

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scholarly article

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10.1038/NATURE18317

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P433

7610

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P478

535

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Nikolina Sekulic

Daniel Blumenthal

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2016-06-29T00:00:00Z

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27362237

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4950998

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