DNA repair activity of 8-oxoguanine DNA glycosylase 1 (OGG1) in human lymphocytes is not dependent on genetic polymorphism Ser326/Cys326. (Q43679802)

25 November 2017

DNA repair activity of 8-oxoguanine DNA glycosylase 1 (OGG1) in human lymphocytes is not dependent on genetic polymorphism Ser326/Cys326. (English)

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25 November 2017

Janssen K

1

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25 November 2017

Schlink K

2

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25 November 2017

Götte W

3

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25 November 2017

Hippler B

4

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25 November 2017

Kaina B

5

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25 November 2017

Oesch F

6

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25 November 2017

language of work or name

English

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publication date

1 August 2001

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25 November 2017

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25 November 2017

486

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25 November 2017

207-216

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25 November 2017

3

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Instability and decay of the primary structure of DNA

25 November 2017

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The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)

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Mutagenesis by 8-oxoguanine: an enemy within

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8-oxoguanine (8-hydroxyguanine) DNA glycosylase and its substrate specificity

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Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization.

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Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine

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Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily

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Mmh/Ogg1 gene inactivation results in accumulation of 8-hydroxyguanine in mice

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

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Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage

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Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites

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Molecular cloning and functional expression of a human cDNA encoding the antimutator enzyme 8-hydroxyguanine-DNA glycosylase

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Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase

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8-hydroxyguanine (7,8-dihydro-8-oxoguanine) DNA glycosylase and AP lyase activities of hOGG1 protein and their substrate specificity

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Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome group B cells

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Structure and chromosome location of human OGG1.

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Mutations in OGG1, a gene involved in the repair of oxidative DNA damage, are found in human lung and kidney tumours.

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New DNA polymorphisms of human MMH/OGG1 gene: prevalence of one polymorphism among lung-adenocarcinoma patients in Japanese

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Genetic polymorphisms and alternative splicing of the hOGG1 gene, that is involved in the repair of 8-hydroxyguanine in damaged DNA.

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Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations

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Activity of O6-methylguanine DNA methyltransferase in mononuclear blood cells of formaldehyde-exposed medical students

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Synthesis of 2'-deoxy-7,8-dihydro-8-oxoguanosine and 2'-deoxy-7,8-dihydro-8-oxoadenosine and their incorporation into oligomeric DNA

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Human MMH (OGG1) type 1a protein is a major enzyme for repair of 8-hydroxyguanine lesions in human cells

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

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An endonuclease activity in human polymorphonuclear neutrophils that removes 8-hydroxyguanine residues from DNA+

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Environment and cancer: who are susceptible?

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Enhanced excision repair activity in mammalian cells after ionizing radiation

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Increased 8-hydroxyguanine levels in DNA and its repair activity in rat kidney after administration of a renal carcinogen, ferric nitrilotriacetate

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7 January 2021

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Identifiers

DOI

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25 November 2017

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