Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA. - Wikidata - wikimedia - TriplyDB

Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA.

Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA.

http://www.wikidata.org/entity/Q33310273

about

The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover The current state of eukaryotic DNA base damage and repair DNA glycosylases: in DNA repair and beyond Uracil DNA N-glycosylase promotes assembly of human centromere protein A Phosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: structural and mechanistic insights Base Excision Repair, a Pathway Regulated by Posttranslational Modifications Cullin4A and cullin4B are interchangeable for HIV Vpr and Vpx action through the CRL4 ubiquitin ligase complex Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition Base excision repair An inverse switch in DNA base excision and strand break repair contributes to melphalan resistance in multiple myeloma cells Further evidence for involvement of a noncanonical function of uracil DNA glycosylase in class switch recombination.RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures.Replication protein A: directing traffic at the intersection of replication and repair.X4 and R5 HIV-1 have distinct post-entry requirements for uracil DNA glycosylase during infection of primary cells.XRCC1 coordinates disparate responses and multiprotein repair complexes depending on the nature and context of the DNA damage Direct interaction between XRCC1 and UNG2 facilitates rapid repair of uracil in DNA by XRCC1 complexes.Refining the Neuberger model: Uracil processing by activated B cells.Identification of a novel in vivo virus-targeted phosphorylation site in interferon regulatory factor-3 (IRF3)Uracil DNA glycosylase BKRF3 contributes to Epstein-Barr virus DNA replication through physical interactions with proteins in viral DNA replication complex.Recruitment of the nuclear form of uracil DNA glycosylase into virus particles participates in the full infectivity of HIV-1.AID and somatic hypermutation.Effect of the multifunctional proteins RPA, YB-1, and XPC repair factor on AP site cleavage by DNA glycosylase NEIL1.Uracil-DNA glycosylase expression determines human lung cancer cell sensitivity to pemetrexed.Alkylation sensitivity screens reveal a conserved cross-species functionome.Mitochondrial base excision repair in mouse synaptosomes during normal aging and in a model of Alzheimer's disease Uracil in DNA and its processing by different DNA glycosylases Uracil-DNA glycosylase in base excision repair and adaptive immunity: species differences between man and mouse.Antibody cross-linking and target elution protocols used for immunoprecipitation significantly modulate signal-to noise ratio in downstream 2D-PAGE analysis Removal of uracil by uracil DNA glycosylase limits pemetrexed cytotoxicity: overriding the limit with methoxyamine to inhibit base excision repair.Ectopic restriction of DNA repair reveals that UNG2 excises AID-induced uracils predominantly or exclusively during G1 phase Uracil DNA glycosylase interacts with the p32 subunit of the replication protein A complex to modulate HIV-1 reverse transcription for optimal virus dissemination.Human single-stranded DNA binding proteins: guardians of genome stability.Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase.Uracil-DNA Glycosylase UNG Promotes Tet-mediated DNA Demethylation Competitive repair pathways in immunoglobulin gene hypermutation.Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase.Human immunodeficiency virus type 1 Vpr modulates cellular expression of UNG2 via a negative transcriptional effect.Uracil DNA Glycosylase 2 negatively regulates HIV-1 LTR transcription.The cell cycle restricts activation-induced cytidine deaminase activity to early G1.Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.

P2860

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P2860

Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA.

http://www.wikidata.org/entity/Q33310273

description

2007 nî lūn-bûn

@nan

2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

@yue

name

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

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Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

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Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

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type

label

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

@ast

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

@en

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

@nl

prefLabel

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

@ast

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

@en

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

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SJ.EMBOJ.7601958

P1433

The EMBO Journal

P1476

Cell cycle-specific UNG2 phosp ...... vity and association with RPA.

@en

P2093

Bodil Kavli

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

Kathrin Torseth

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

Lars Hagen

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

Mirta M L Sousa

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

Nina B Liabakk

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

Ole Hørning

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

Ottar Sundheim

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

P2860

Instability and decay of the primary structure of DNA

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup

Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene

Post-replicative base excision repair in replication foci

SMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repair

Regulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylase

Cell cycle regulation and in vitro hybrid arrest analysis of the major human uracil-DNA glycosylase

Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins

Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA

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51-61

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10.1038/SJ.EMBOJ.7601958

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P433

1

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27

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Hans Einar Krokan

Javier Pena-Diaz

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2007-12-13T00:00:00Z

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5768290

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18079698

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P921

phosphorylation

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2147998

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