Variant base excision repair proteins: contributors to genomic instability - Wikidata - wikimedia - TriplyDB

Variant base excision repair proteins: contributors to genomic instability

Variant base excision repair proteins: contributors to genomic instability

http://www.wikidata.org/entity/Q21558646

about

8-Oxoguanine DNA glycosylase (OGG1) deficiency increases susceptibility to obesity and metabolic dysfunction Pathways for repairing and tolerating the spectrum of oxidative DNA lesions Base excision repair and cancer Genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase: Activity, structure, and the effect of editing Base excision repair: a critical player in many games Correlation between base-excision repair gene polymorphisms and levels of in-vitro BPDE-induced DNA adducts in cultured peripheral blood lymphocytes.Functional assessment of population and tumor-associated APE1 protein variants Characterization of chromosome stability in diploid, polyploid and hybrid yeast cells 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.Base excision repair: contribution to tumorigenesis and target in anticancer treatment paradigms Mice heterozygous for CREB binding protein are hypersensitive to γ-radiation and invariably develop myelodysplastic/myeloproliferative neoplasm Mechanisms of glycosylase induced genomic instability Saccharomyces cerevisiae Apn1 mutation affecting stable protein expression mimics catalytic activity impairment: implications for assessing DNA repair capacity in humans Regulation of DNA glycosylases and their role in limiting disease.Distinct functional consequences of MUTYH variants associated with colorectal cancer: Damaged DNA affinity, glycosylase activity and interaction with PCNA and Hus1.OGG1-DNA interactions facilitate NF-κB binding to DNA targets.Cellular roles of DNA polymerase beta.DNA demethylation pathways: Additional players and regulators.Targeting DNA repair and replication stress in the treatment of ovarian cancer.Nei-like 1 (NEIL1) excises 5-carboxylcytosine directly and stimulates TDG-mediated 5-formyl and 5-carboxylcytosine excision.Yap1: a DNA damage responder in Saccharomyces cerevisiae.Potential anti-cancer effect of curcumin in human lung squamous cell carcinoma.Radiosensitivity in patients suffering from chronic kidney disease.Genomic instability in chronic renal failure patients.The NEIL1 G83D germline DNA glycosylase variant induces genomic instability and cellular transformation.Differential role of base excision repair proteins in mediating cisplatin cytotoxicity.

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Variant base excision repair proteins: contributors to genomic instability

http://www.wikidata.org/entity/Q21558646

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին 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

@zh-hant

2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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type

label

Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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Variant base excision repair proteins: contributors to genomic instability

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J.SEMCANCER.2010.10.010

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Seminars in Cancer Biology

P1476

Variant base excision repair proteins: contributors to genomic instability

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P2093

Antonia A Nemec

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

Joann B Sweasy

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P2860

MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1

Instability and decay of the primary structure of DNA

The base excision repair enzyme MED1 mediates DNA damage response to antitumor drugs and is associated with mismatch repair system integrity

Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions

Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III

Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway

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

XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions

Identification of 5-formyluracil DNA glycosylase activity of human hNTH1 protein.

Nonenzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-L-methionine is a potentially mutagenic reaction

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320-328

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scholarly article

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10.1016/J.SEMCANCER.2010.10.010

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5

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20

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Susan S Wallace

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2010-10-16T00:00:00Z

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3254599

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