ArticleChemical research in toxicology2019
Reactivity of N3-Methyl-2'-Deoxyadenosine in Nucleosome Core Particles.
Article in Chemical research in toxicology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Quantification of Intracellular DNA-Protein Cross-Links with N7-Methyl-2'-Deoxyguanosine and Their Contribution to Cytotoxicity.Chemical research in toxicology · 2024Article
- A SAM analogue-utilizing ribozyme for site-specific RNA alkylation in living cells.Nature chemistry · 2023Article
- DNA-Histone Cross-Link Formation via Hole Trapping in Nucleosome Core Particles.Journal of the American Chemical Society · 2023Article
- Local Alteration of Ionic Strength in a Nucleosome Core Particle and Its Effect onBiochemistry · 2022Article
- Histone variants H3.3 and H2A.Z/H3.3 facilitate excision of uracil from nucleosome core particles.DNA repair · 2022Article
- Human TDP1, APE1 and TREX1 repair 3'-DNA-peptide/protein cross-links arising from abasic sites in vitro.Nucleic acids research · 2022Article
- Participation of Histones in DNA Damage and Repair within Nucleosome Core Particles: Mechanism and Applications.Accounts of chemical research · 2022Article
- Targeting DNA-Protein CrosslinksFrontiers in molecular biosciences · 2022Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
N3-Methyl-2'-deoxyadenosine (MdA) is the major dA methylation product in duplex DNA. MdA blocks DNA replication and undergoes depurination at significantly higher rates than the native nucleotide from which it is derived. Recent reports on the effects of the nucleosome core particle (NCP) environment on the reactivity of N7-methyl-2'-deoxyguanosine (MdG) inspired this investigation concerning the reactivity of MdA in NCPs. NCPs containing MdA at selected positions were produced using a strategy in which the minor groove binding Me-Lex molecule serves as a sequence specific methylating agent. Hydrolysis of the glycosidic bond in MdA to form abasic sites (AP) is suppressed in a NCP. Experiments using histone variants indicate that the proximal, highly basic N-terminal tails are partially responsible for the decreased depurination rate constant. MdA also forms cross-links with histone proteins. The levels of MdA-histone DNA-protein cross-links (DPC
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