Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q24531459

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The OXR domain defines a conserved family of eukaryotic oxidation resistance proteins Variant base excision repair proteins: contributors to genomic instability Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1 Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA Identification of 5-formyluracil DNA glycosylase activity of human hNTH1 protein.Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity Cockayne syndrome group B protein stimulates repair of formamidopyrimidines by NEIL1 DNA glycosylase NEIL2-initiated, APE-independent repair of oxidized bases in DNA: Evidence for a repair complex in human cells Stimulation of NEIL2-mediated oxidized base excision repair via YB-1 interaction during oxidative stress Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells Processing of a complex multiply damaged DNA site by human cell extracts and purified repair proteins APE1-dependent repair of DNA single-strand breaks containing 3'-end 8-oxoguanine Structure of the uncomplexed DNA repair enzyme endonuclease VIII indicates significant interdomain flexibility.NEIL1 excises 3' end proximal oxidative DNA lesions resistant to cleavage by NTH1 and OGG1.Dimerization and opposite base-dependent catalytic impairment of polymorphic S326C OGG1 glycosylase The current state of eukaryotic DNA base damage and repair DNA glycosylases: in DNA repair and beyond New perspectives on oxidized genome damage and repair inhibition by pro-oxidant metals in neurological diseases The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage Base excision repair and cancer A structural rationale for stalling of a replicative DNA polymerase at the most common oxidative thymine lesion, thymine glycol Structural Characterization of a Viral NEIL1 Ortholog Unliganded and Bound to Abasic Site-containing DNA The cis -(5 R ,6 S )-Thymine Glycol Lesion Occupies the Wobble Position When Mismatched with Deoxyguanosine in DNA Binding of the human nucleotide excision repair proteins XPA and XPC/HR23B to the 5R-thymine glycol lesion and structure of the cis-(5R,6S) thymine glycol epimer in the 5'-GTgG-3' sequence: destabilization of two base pairs at the lesion site Solution Structure of Duplex DNA Containing a β-Carba-Fapy-dG Lesion Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNA Structural Characterization of Viral Ortholog of Human DNA Glycosylase NEIL1 Bound to Thymine Glycol or 5-Hydroxyuracil-containing DNA Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2 A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions Induction of the human oxidized base-specific DNA glycosylase NEIL1 by reactive oxygen species Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein Base excision repair The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts NEIL2 protects against oxidative DNA damage induced by sidestream smoke in human cells Bisphenol a promotes cell survival following oxidative DNA damage in mouse fibroblasts Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo

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

http://www.wikidata.org/entity/Q24531459

description

2002 nî lūn-bûn

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2002 թվականի մարտին հրատարակված գիտական հոդված

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Identification and characteriz ...... ses in oxidatively damaged DNA

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Identification and characteriz ...... ses in oxidatively damaged DNA

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Identification and characteriz ...... ses in oxidatively damaged DNA

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Identification and characteriz ...... ses in oxidatively damaged DNA

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

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Identification and characteriz ...... ses in oxidatively damaged DNA

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Barry Imhoff

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Istvan Boldogh

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Miral Dizdaroglu

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Pawel Jaruga

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Sankar Mitra

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Tadahide Izumi

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Tapas K Hazra

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Yoke W Kow

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P2860

Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals

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

Oxidants, antioxidants, and the degenerative diseases of aging

Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA

Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8

Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage

Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs

Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue

Defective transcription-coupled repair of oxidative base damage in Cockayne syndrome patients from XP group G

hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs

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3523-3528

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scholarly article

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10.1073/PNAS.062053799

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6

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99

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2002-03-01T00:00:00Z

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11460455

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11904416

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122556

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