Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancer.

Human mutation - 1 Nov 2010

Goto Masanori, Shinmura Kazuya, Nakabeppu Yusaku, Tao Hong, Yamada Hidetaka, Tsuneyoshi Toshihiro, Sugimura Haruhiko

Abstract excerpt

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 t...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 8-Hydroxy-2'-Deoxyguanosine
Share to Adenomatous Polyposis Coli
Share to Colorectal Neoplasms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Deoxyguanosine

Share to DNA Glycosylases

Share to DNA Repair

Share to In Vitro Techniques

Share to Mutant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 20848659
DOI: 10.1002/humu.21363
PMCID: PMC3051265

Genes

MUTYH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20848659-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancer.PMID 20848659Read ↗

Functional Evaluation of Nine Missense-Type Variants of the Human DNA Glycosylase Enzyme MUTYH in the Japanese Population.Semantic proximity Read ↗

Role of MUTYH in human cancer.Semantic proximity Read ↗

Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer.Semantic proximity Read ↗

Understanding the role of the Q338H MUTYH variant in oxidative damage repair.Semantic proximity Read ↗

Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.Semantic proximity Read ↗

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

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

Loss of MUTYH function in human cells leads to accumulation of oxidative damage and genetic instability.Semantic proximity Read ↗

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

Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe.Semantic proximity Read ↗

Cancer-associated variants and a common polymorphism of MUTYH exhibit reduced repair of oxidative DNA damage using a GFP-based assay in mammalian cells.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.