The adenovirus E1b55K/E4orf6 complex induces degradation of the Bloom helicase during infection. - Wikidata - wikimedia - TriplyDB

The adenovirus E1b55K/E4orf6 complex induces degradation of the Bloom helicase during infection.

The adenovirus E1b55K/E4orf6 complex induces degradation of the Bloom helicase during infection.

http://www.wikidata.org/entity/Q42583162

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Ubiquitin-dependent recruitment of the Bloom syndrome helicase upon replication stress is required to suppress homologous recombination Viral Mimicry to Usurp Ubiquitin and SUMO Host Pathways The DNA damage response induced by infection with human cytomegalovirus and other viruses Adenovirus Early Proteins and Host Sumoylation Adenovirus type 5 early region 1B 55K oncoprotein-dependent degradation of cellular factor Daxx is required for efficient transformation of primary rodent cells A core viral protein binds host nucleosomes to sequester immune danger signals.SPOC1-mediated antiviral host cell response is antagonized early in human adenovirus type 5 infection The repression domain of the E1B 55-kilodalton protein participates in countering interferon-induced inhibition of adenovirus replication.A ubiquitin-specific protease possesses a decisive role for adenovirus replication and oncogene-mediated transformation.Cullin E3 ligases and their rewiring by viral factors Proteomic analysis of ubiquitin-like posttranslational modifications induced by the adenovirus E4-ORF3 protein.TopBP1 interacts with BLM to maintain genome stability but is dispensable for preventing BLM degradation.Protein degradation pathways regulate the functions of helicases in the DNA damage response and maintenance of genomic stability The α2 helix in the DNA ligase IV BRCT-1 domain is required for targeted degradation of ligase IV during adenovirus infection.Biophysical and functional analyses suggest that adenovirus E4-ORF3 protein requires higher-order multimerization to function against promyelocytic leukemia protein nuclear bodies The BLM helicase contributes to telomere maintenance through processing of late-replicating intermediate structures RAD51 and BRCA2 Enhance Oncolytic Adenovirus Type 5 Activity in Ovarian Cancer De novo derivation of proteomes from transcriptomes for transcript and protein identification.Infection of a Single Cell Line with Distinct Strains of Human Cytomegalovirus Can Result in Large Variations in Virion Production and Facilitate Efficient Screening of Virus Protein Function.Using the E4orf6-Based E3 Ubiquitin Ligase as a Tool To Analyze the Evolution of Adenoviruses.Viral and Cellular Components of AAV2 Replication Compartments.Adenovirus degradation of cellular proteins.Design stars: how small DNA viruses remodel the host nucleus.DNA virus replication compartments.Comparison of protein expression during wild-type, and E1B-55k-deletion, adenovirus infection using quantitative time-course proteomics.Analysis of the Cullin binding sites of the E4orf6 proteins of human adenovirus E3 ubiquitin ligases.High Efficiency CRISPR/Cas9-mediated Gene Editing in Primary Human T-cells Using Mutant Adenoviral E4orf6/E1b55k "Helper" Proteins Impact of Adenovirus E4-ORF3 Oligomerization and Protein Localization on Cellular Gene Expression.Role of E1B55K in E4orf6/E1B55K E3 ligase complexes formed by different human adenovirus serotypes.Control of human adenovirus type 5 gene expression by cellular Daxx/ATRX chromatin-associated complexes.Functional cooperation between human adenovirus type 5 early region 4, open reading frame 6 protein, and cellular homeobox protein HoxB7.Adenovirus E4orf3 targets transcriptional intermediary factor 1γ for proteasome-dependent degradation during infection.Adenovirus E4-ORF3-dependent relocalization of TIF1α and TIF1γ relies on access to the Coiled-Coil motif.Normal human cell proteins that interact with the adenovirus type 5 E1B 55kDa protein.The Human Adenovirus Type 5 E4orf6/E1B55K E3 Ubiquitin Ligase Complex Enhances E1A Functional Activity.The Human Adenovirus Type 5 E4orf6/E1B55K E3 Ubiquitin Ligase Complex Can Mimic E1A Effects on E2F.Identifying host factors associated with DNA replicated during virus infection.E1B-55K mediated regulation of RNF4 STUbL promotes HAdV gene expression.Degradation of a novel DNA damage response protein, tankyrase 1 binding protein 1 (Tab182), following adenovirus infection.The Mre11 Cellular Protein Is Modified by Conjugation of Both SUMO-1 and SUMO-2/3 during Adenovirus Infection

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The adenovirus E1b55K/E4orf6 complex induces degradation of the Bloom helicase during infection.

http://www.wikidata.org/entity/Q42583162

description

2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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2010年论文

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name

The adenovirus E1b55K/E4orf6 c ...... oom helicase during infection.

@en

The adenovirus E1b55K/E4orf6 c ...... oom helicase during infection.

@nl

type

label

The adenovirus E1b55K/E4orf6 c ...... oom helicase during infection.

@en

The adenovirus E1b55K/E4orf6 c ...... oom helicase during infection.

@nl

prefLabel

The adenovirus E1b55K/E4orf6 c ...... oom helicase during infection.

@en

The adenovirus E1b55K/E4orf6 c ...... oom helicase during infection.

@nl

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Journal of Virology

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The adenovirus E1b55K/E4orf6 c ...... oom helicase during infection.

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Colleen M Naeger

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Jan Karlseder

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Matthew D Weitzman

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

Nicole I Orazio

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P2860

Association of the Bloom syndrome protein with topoisomerase IIIalpha in somatic and meiotic cells

Nuclear structure in normal and Bloom syndrome cells

Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery.

Deletion of the E4 region of the genome produces adenovirus DNA concatemers

The DNA-damage response in human biology and disease

BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures

DNA end resection: many nucleases make light work

PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1

Human RECQ5beta helicase promotes strand exchange on synthetic DNA structures resembling a stalled replication fork

Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing.

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1887-1892

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10.1128/JVI.02134-10

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4

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85

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2010-12-01T00:00:00Z

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21123383

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