ArticleJournal of bacteriology1999
Imbalanced base excision repair increases spontaneous mutation and alkylation sensitivity in Escherichia coli.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 68 citations in OpenAlex.
- Article
- High-Throughput Screening Platform for Nanoparticle-Mediated Alterations of DNA Repair Capacity.ACS nano · 2021Article
- Escherichia coli YcaQ is a DNA glycosylase that unhooks DNA interstrand crosslinks.Nucleic acids research · 2020Article
- The DNA repair enzyme MUTYH potentiates cytotoxicity of the alkylating agent MNNG by interacting with abasic sites.The Journal of biological chemistry · 2020Article
- Review
- Article
- Imbalanced adaptive responses associated with microsatellite instability in cholangiocarcinoma.Oncology letters · 2017Article
- Inter-individual variation in DNA repair capacity: a need for multi-pathway functional assays to promote translational DNA repair research.DNA repair · 2014Article
- N-methylpurine DNA glycosylase inhibits p53-mediated cell cycle arrest and coordinates with p53 to determine sensitivity to alkylating agents.Cell research · 2012Article
- Balancing repair and tolerance of DNA damage caused by alkylating agents.Nature reviews. Cancer · 2012Review
- Article
- Multifaceted roles of alkyltransferase and related proteins in DNA repair, DNA damage, resistance to chemotherapy, and research tools.Chemical research in toxicology · 2011Review
- Human base excision repair creates a bias toward -1 frameshift mutations.The Journal of biological chemistry · 2010Article
- Frameshift mutagenesis and microsatellite instability induced by human alkyladenine DNA glycosylase.Molecular cell · 2010Article
- Substrate binding pocket residues of human alkyladenine-DNA glycosylase critical for methylating agent survival.DNA repair · 2008Article
- Evidence of complete cellular repair of 1,N6-ethenoadenine, a mutagenic and potential damage for human cancer, revealed by a novel method.Molecular and cellular biochemistry · 2008Article
- Rev1 and Polzeta influence toxicity and mutagenicity of Me-lex, a sequence selective N3-adenine methylating agent.DNA repair · 2008Article
- Transcriptional networks in S. cerevisiae linked to an accumulation of base excision repair intermediates.PloS one · 2007Article
- Methylating agents and DNA repair responses: Methylated bases and sources of strand breaks.Chemical research in toxicology · 2006Review
- Modes of action and species-specific effects of di-(2-ethylhexyl)phthalate in the liver.Critical reviews in toxicology · 2006Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Inappropriate expression of 3-methyladenine (3MeA) DNA glycosylases has been shown to have harmful effects on microbial and mammalian cells. To understand the underlying reasons for this phenomenon, we have determined how DNA glycosylase activity and substrate specificity modulate glycosylase effects in Escherichia coli. We compared the effects of two 3MeA DNA glycosylases with very different substrate ranges, namely, the Saccharomyces cerevisiae Mag1 and the E. coli Tag glycosylases. Both glycosylases increased spontaneous mutation, decreased cell viability, and sensitized E. coli to killing by the alkylating agent methyl methanesulfonate. However, Tag had much less harmful effects than Mag1. The difference between the two enzymes' effects may be accounted for by the fact that Tag almost exclusively excises 3MeA lesions, whereas Mag1 excises a broad range of alkylated and other purines. We infer that the DNA lesions responsible for changes in spontaneous mutation, viability, and alkylation sensitivity are abasic sites and secondary lesions resulting from processing abasic sites via the base excision repair pathway.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.