ArticleCancer biology & therapy2009
Modulation of the activity of methyl binding domain protein 4 (MBD4/MED1) while processing iododeoxyuridine generated DNA mispairs.
Article in Cancer biology & therapy, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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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.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Review
- Solution structure and intramolecular exchange of methyl-cytosine binding domain protein 4 (MBD4) on DNA suggests a mechanism to scan for mCpG/TpG mismatches.Nucleic acids research · 2014Article
- Structural basis of the versatile DNA recognition ability of the methyl-CpG binding domain of methyl-CpG binding domain protein 4.The Journal of biological chemistry · 2013Article
- Apoptosis and DNA methylation.Cancers · 2011Article
- Article
- The mismatch repair and base excision repair pathways: an opportunity for individualized (personalized) sensitization of cancer therapy.Cancer biology & therapy · 2009Article
- Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
DNA glycosylases function to remove endogenous and exogenous base damage and thus contribute to the maintenance of genomic integrity. This function gains clinical relevance when base mispairs introduced by chemotherapy or radiosensitizing drugs become their substrate. This report describes the action of DNA glycosylases on the mispairs generated by iododeoxyuridine (IUdR)-a radiosensitizer. A non-radioactive fluorescent dye-based in vitro glycosylase assay was employed to quantitatively measure the enzymatic activities of functionally related DNA glycosylases on IUdR generated mispairs including G:IU and A:IU. Thymine DNA glycosylase (TDG) and methyl binding domain protein 4 (MBD4/MED1) are found to act on G:IU (but not A:IU) mispairs and are functionally complementary to each other. However, uracil DNA glycosylase (UDG) does not show any activity on these mispairs. The methyl binding domain of MBD4/MED1 was found to specifically inhibit the activity of MBD4/MED1 as well as the glycosylase domain, when the G:IU mispairs were located in a methylated CpG context. However, inhibition of TDG activity on methylated G:IU mispairs by the methyl binding domain was not observed.
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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.