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Article

Defective human MutY phosphorylation exists in colorectal cancer cell lines with wild-type MutY alleles.

The Journal of biological chemistry - 28 Nov 2003

Parker Antony R, O'Meally Robert N, Sahin Fikret, Su Gloria H, Racke Frederick K, Nelson William G, DeWeese Theodore L, Eshleman James R

Abstract excerpt

Oxidative DNA damage can generate a variety of cytotoxic DNA lesions such as 8-oxoguanine (8-oxoG), which is one of the most mutagenic bases formed from oxidation of genomic DNA because 8-oxoG can readily mispair with either cytosine or adenine. If unrepaired, further replication of A.8-oxoG mispairs results in C:G to A:T transversions, a form of genomic instability. We reported previously that repair of A.8-oxoG...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 12966098
DOI: 10.1074/jbc.M306598200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Defective human MutY phosphorylation exists in colorectal cancer cell lines with wild-type MutY alleles.PMID 12966098Read ↗

MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNASemantic proximity Read ↗

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MutY and MutY homologs (MYH) in genome maintenance.Semantic proximity Read ↗

Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA.Semantic proximity Read ↗

Precision genome editing and in-cell measurements of oxidative DNA damage repair enable functional and mechanistic characterization of cancer-associated MUTYH variants.Semantic proximity Read ↗

Characterization of mutant MUTYH proteins associated with familial colorectal cancer.Semantic proximity Read ↗

8-Hydroxyguanosine repair is defective in some microsatellite stable colorectal cancer cells.Semantic proximity Read ↗

Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposisSemantic proximity Read ↗

MUTYH mutations associated with familial adenomatous polyposis: functional characterization by a mammalian cell-based assay.Semantic proximity Read ↗

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