RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures. - Wikidata - wikimedia - TriplyDB

RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures.

RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures.

http://www.wikidata.org/entity/Q33546272

about

The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage Base excision repair and cancer Insights into the glycosylase search for damage from single-molecule fluorescence microscopy.Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase No cancer predisposition or increased spontaneous mutation frequencies in NEIL DNA glycosylases-deficient mice Pol β associated complex and base excision repair factors in mouse fibroblasts.Effect of the multifunctional proteins RPA, YB-1, and XPC repair factor on AP site cleavage by DNA glycosylase NEIL1.Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins.New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Regulation of NEIL1 protein abundance by RAD9 is important for efficient base excision repair Oxidative genome damage and its repair: implications in aging and neurodegenerative diseases.The C-terminal Domain (CTD) of Human DNA Glycosylase NEIL1 Is Required for Forming BERosome Repair Complex with DNA Replication Proteins at the Replicating Genome: DOMINANT NEGATIVE FUNCTION OF THE CTD.Enhancement of NEIL1 protein-initiated oxidized DNA base excision repair by heterogeneous nuclear ribonucleoprotein U (hnRNP-U) via direct interaction.Coordination of DNA repair by NEIL1 and PARP-1: a possible link to aging Neil3, the final frontier for the DNA glycosylases that recognize oxidative damage.The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions Deficiency of base excision repair enzyme NEIL3 drives increased predisposition to autoimmunity.Contribution of DNA unwrapping from histone octamers to the repair of oxidatively damaged DNA in nucleosomes.Regulation of oxidized base damage repair by chromatin assembly factor 1 subunit A.DNA glycosylases search for and remove oxidized DNA bases.Functions of disordered regions in mammalian early base excision repair proteins.Oxidized base damage and single-strand break repair in mammalian genomes: role of disordered regions and posttranslational modifications in early enzymes.BERing the burden of damage: Pathway crosstalk and posttranslational modification of base excision repair proteins regulate DNA damage management.Hypersensitivity of mouse NEIL1-knockdown cells to hydrogen peroxide during S phase.Formation and processing of DNA damage substrates for the hNEIL enzymes.Pre-Replicative Repair of Oxidized Bases Maintains Fidelity in Mammalian Genomes: The Cowcatcher Role of NEIL1 DNA Glycosylase.Human DNA Glycosylase NEIL1's Interactions with Downstream Repair Proteins Is Critical for Efficient Repair of Oxidized DNA Base Damage and Enhanced Cell Survival Visualizing the Search for Radiation-damaged DNA Bases in Real Time.Human cells contain a factor that facilitates the DNA glycosylase-mediated excision of oxidized bases from occluded sites in nucleosomes.The NEIL1 G83D germline DNA glycosylase variant induces genomic instability and cellular transformation.The C-terminal tail of the NEIL1 DNA glycosylase interacts with the human mitochondrial single-stranded DNA binding protein.Inhibition of abasic site cleavage in bubble DNA by multifunctional protein YB-1.

P2860

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P2860

RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures.

http://www.wikidata.org/entity/Q33546272

description

2010 nî lūn-bûn

@nan

2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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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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P356

J.DNAREP.2010.02.014

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P1476

RPA physically interacts with ...... in primer-template structures.

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P2093

Corey A Theriot

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

Sankar Mitra

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Tapas K Hazra

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P2860

Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA

Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpoints

Functional domains of the 70-kilodalton subunit of human replication protein A

The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1

Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae

Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA

Single-stranded DNA-binding protein hSSB1 is critical for genomic stability

The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene

Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA

Post-replicative base excision repair in replication foci

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643-652

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scholarly article

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10.1016/J.DNAREP.2010.02.014

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6

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9

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Muralidhar L. Hegde

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2010-03-24T00:00:00Z

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42588955

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2883689

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