ArticleNucleic acids research2005
Dynamic relocalization of hOGG1 during the cell cycle is disrupted in cells harbouring the hOGG1-Cys326 polymorphic variant.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 89 citations in OpenAlex.
- OGG1 and MUTYH DNA Glycosylases, the Dynamic Duo Against 8-Oxoguanine DNA Lesion: Structure, Regulation, and Novel Emerging Roles.Biomolecules · 2026Review
- The OGG1 Ser326Cys polymorphism: molecular mechanisms of disease susceptibility and precision medicine applications.Clinical epigenetics · 2025Review
- OGG1S326C variant frequent in human populations facilitates inflammatory responses due to its extended interaction with DNA substrate.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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- A hybrid feature extraction scheme for efficient malonylation site prediction.Scientific reports · 2022Article
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- Focus on DNA Glycosylases-A Set of Tightly Regulated Enzymes with a High Potential as Anticancer Drug Targets.International journal of molecular sciences · 2020Review
- Significant Contribution of DNA RepairOncoTargets and therapy · 2020Article
- Shedding Light on the Interaction of Human Anti-Apoptotic Bcl-2 Protein with Ligands through Biophysical and in Silico Studies.International journal of molecular sciences · 2019Article
- Multifunctional DNA nanocage with CdTe quantum dots for fluorescence detection of human 8-oxoG DNA glycosylase 1 and doxorubicin delivery to cancer cells.Mikrochimica acta · 2019Article
- Hijacking of multiple phospholipid biosynthetic pathways and induction of membrane biogenesis by a picornaviral 3CD protein.PLoS pathogens · 2018Article
- BERing the burden of damage: Pathway crosstalk and posttranslational modification of base excision repair proteins regulate DNA damage management.DNA repair · 2017Review
- Gene-gene interactions in gastrointestinal cancer susceptibility.Oncotarget · 2016Review
- Base Excision Repair, a Pathway Regulated by Posttranslational Modifications.Molecular and cellular biology · 2016Review
- A phosphorylation-related variant ADD1-rs4963 modifies the risk of colorectal cancer.PloS one · 2015Article
- Regulatory mechanisms of RNA function: emerging roles of DNA repair enzymes.Cellular and molecular life sciences : CMLS · 2014Review
- Cellular accumulation of Cys326-OGG1 protein complexes under conditions of oxidative stress.Biochemical and biophysical research communications · 2014Article
- Polymorphisms of DNA repair genes OGG1 and XPD and the risk of age-related cataract in Egyptians.Molecular vision · 2014Article
- Transforming growth factor-β and toll-like receptor-4 polymorphisms are not associated with fibrosis in haemochromatosis.World journal of gastroenterology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Numerous lines of evidence support the role of oxidative stress in different types of cancer. A major DNA lesion, 8-oxo-7,8-dihydroguanine (8-oxoG), is formed by reactive oxygen species in the genome under physiological conditions. 8-OxoG is strongly mutagenic, generating G.C-->T.A transversions, a frequent somatic mutation in cancers. hOGG1 was cloned as a gene encoding a DNA glycosylase that specifically recognizes and removes 8-oxoG from 8-oxoG:C base pairs and suppresses G.C-->T.A transversions. In this study, we investigated the subcellular localization and expression of hOGG1 during the cell cycle. Northern blots showed cell-cycle-dependent mRNA expression of the two major hOGG1 isoforms. By using a cell line constitutively expressing hOGG1 fused to enhanced green fluorescence protein (EGFP), we observed a dynamic relocalization of EGFP-hOGG1 to the nucleoli during the S-phase of the cell cycle, and this localization was shown to be linked to transcription. A C/G change that results in an amino acid substitution from serine to cysteine in codon 326 has been reported as a genetic polymorphism and a risk allele for a variety of cancers. We investigated the cellular localization of the corresponding protein, hOGG1-Cys326, fused to EGFP and observed a dramatic effect on its localization that is explained by a change in the phosphorylation status of hOGG1.
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