ArticleHuman mutation2010
Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancer.
Article in Human mutation, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- DNA Damage Recognition by Bacterial and Human Adenine-DNA Glycosylases: Insights from Non-Canonical Substrates.Biomolecules · 2026Article
- First report of MUTYH-associated polyposis with c.1353_1355del and c.452A>G mutations in Tolima Grande region from Colombia: a case report.Frontiers in oncology · 2026Article
- Saturation mapping of MUTYH variant effects using DNA repair reporters.American journal of human genetics · 2025Article
- Comprehensive genetic analysis in biliary tract cancer: a prospective single-center experience.ESMO gastrointestinal oncology · 2025Article
- Polymorphisms in Base Excision Repair Genes and Association with Multiple Sclerosis in a Pilot Study on a Central European Population.International journal of molecular sciences · 2025Article
- Germline MUTYH mutations and high-grade gliomas: Novel evidence for a potential association.Genes, chromosomes & cancer · 2022Article
- A Case Report of CHEK2 and MUTYH Germline Mutations Associated With Cholangiocarcinoma in a Young Patient.Cureus · 2022Article
- Hereditary variants of unknown significance in African American women with breast cancer.PloS one · 2022Article
- A human MUTYH variant linking colonic polyposis to redox degradation of the [4Fe4S]Nature chemistry · 2018Article
- Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Free radical biology & medicine · 2017Review
- Type and frequency of MUTYH variants in Italian patients with suspected MAP: a retrospective multicenter study.Journal of human genetics · 2017Article
- Mutation Spectrum Induced by 8-Bromoguanine, a Base Damaged by Reactive Brominating Species, in Human Cells.Oxidative medicine and cellular longevity · 2017Article
- Article
- Functional Complementation Assay for 47 MUTYH Variants in a MutY-Disrupted Escherichia coli Strain.Human mutation · 2015Article
- Genomic era diagnosis and management of hereditary and sporadic colon cancer.World journal of clinical oncology · 2014Review
- MUTYH-associated colorectal cancer and adenomatous polyposis.Surgery today · 2014Review
- Impaired 8-hydroxyguanine repair activity of MUTYH variant p.Arg109Trp found in a Japanese patient with early-onset colorectal cancer.Oxidative medicine and cellular longevity · 2014Article
- Loss of MUTYH function in human cells leads to accumulation of oxidative damage and genetic instability.Oncogene · 2013Article
- Understanding the role of the Q338H MUTYH variant in oxidative damage repair.Nucleic acids research · 2013Article
- Base excision repair and cancer.Cancer letters · 2012Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biallelic inactivating germline mutations in the base excision repair MUTYH (MYH) gene have been shown to predispose to MUTYH-associated polyposis (MAP), which is characterized by multiple colorectal adenomas and carcinomas. In this study, we successfully prepared highly homogeneous human MUTYH type 2 recombinant proteins and compared the DNA glycosylase activity of the wild-type protein and fourteen variant-type proteins on adenine mispaired with 8-hydroxyguanine, an oxidized form of guanine. The adenine DNA glycosylase activity of the p.I195V protein, p.G368D protein, p.M255V protein, and p.Y151C protein was 66.9%, 15.2%, 10.7%, and 4.5%, respectively, of that of the wild-type protein, and the glycosylase activity of the p.R154H, p.L360P, p.P377L, p.452delE, p.R69X, and p.Q310X proteins as well as of the p.D208N negative control form was extremely severely impaired. The glycosylase activity of the p.V47E, p.R281C, p.A345V, and p.S487F proteins, on the other hand, was almost the same as that of the wild-type protein. These results should be of great value in accurately diagnosing MAP and in fully understanding the mechanism by which MUTYH repairs DNA in which adenine is mispaired with 8-hydroxyguanine.
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