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

Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.

Methods in enzymology - 1 Jan 2018

Majumdar Chandrima, Nuñez Nicole N, Raetz Alan G, Khuu Cindy, David Sheila S

Abstract excerpt

Many DNA repair enzymes, including the human adenine glycosylase MUTYH, require iron-sulfur (Fe-S) cluster cofactors for DNA damage recognition and subsequent repair. MUTYH prokaryotic and eukaryotic homologs are a family of adenine (A) glycosylases that cleave A when mispaired with the oxidatively damaged guanine lesion, 8-oxo-7,8-dihydroguanine (OG). Faulty OG:A repair has been linked to the inheritance of...

Read the complete abstract on PubMed

Topics

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

Share to DNA Glycosylases
Share to DNA Repair
Share to Drug Resistance, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Assays

Share to Escherichia coli Proteins

Share to Iron-Sulfur Proteins

Share to Mutation Rate

Share to Rifampin

Source

Open in PubMed Open full text

Identifiers

PMID: 29746250
DOI: 10.1016/bs.mie.2017.12.006
PMCID: PMC6201757

Genes

MUTYH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.PMID 29746250Read ↗

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 ↗

The Zinc Linchpin Motif in the DNA Repair Glycosylase MUTYH: Identifying the Zn2+ Ligands and Roles in Damage Recognition and Repair.Semantic proximity Read ↗

Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.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 ↗

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 ↗

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

Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repair.Semantic proximity Read ↗

Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E.coli enzymes.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 ↗

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