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

Correlation between Charge Transport and Base Excision Repair in the MutY-DNA Glycosylase.

The journal of physical chemistry. B - 14 Jan 2021

Teo Ruijie D, Du Xiaochen, Vera Héctor Luis Torres, Migliore Agostino, Beratan David N

Abstract excerpt

Experimental evidence suggests that DNA-mediated redox signaling between high-potential [Fe4S4] proteins is relevant to DNA replication and repair processes, and protein-mediated charge transfer (CT) between [Fe4S4] clusters and nucleic acids is a fundamental process of the signaling and repair mechanisms. We analyzed the dominant CT pathways in the base excision repair glycosylase MutY using molecular dynamics...

Read the complete abstract on PubMed

Topics

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

Share to DNA Damage
Share to DNA Glycosylases
Share to DNA Repair

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanine

Share to Mutation

Share to N-Glycosyl Hydrolases

Source

Open in PubMed Open full text

Identifiers

PMID: 33371674
DOI: 10.1021/acs.jpcb.0c08598
PMCID: PMC8444423

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Correlation between Charge Transport and Base Excision Repair in the MutY-DNA Glycosylase.PMID 33371674Read ↗

Theoretical study of DNA damage recognition via electron transfer from the [4Fe-4S] complex of MutY.Semantic proximity Read ↗

Distinctive Formation of a DNA-Protein Cross-Link during the Repair of DNA Oxidative Damage: Insights into Human Disease from MD Simulations and QM/MM Calculations.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 ↗

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 repairSemantic proximity Read ↗

Single Amino Acid Mutation Controls Hole Transfer Dynamics in DNA-Methyltransferase HhaI Complexes.Semantic proximity Read ↗

Structural Connectivity Between the Zinc Linchpin Motif, the [4Fe-4S] cluster, and the active site orchestrates DNA repair in MUTYHSemantic proximity Read ↗

Crystal structure of MutYX: a novel clusterless adenine DNA glycosylase with a distinct C-terminal domain and 8-oxoguanine recognition sphere.Semantic proximity Read ↗

Analysis of an anomalous mutant of MutM DNA glycosylase leads to new insights into the catalytic mechanism.Semantic proximity Read ↗

A human MUTYH variant linking colonic polyposis to redox degradation of the [4Fe4S]2+ cluster.Semantic proximity Read ↗

Structural Basis for Avoidance of Promutagenic DNA Repair by MutY Adenine DNA Glycosylase.Semantic proximity Read ↗

Association of Functional Variants and Protein-to-Protein Physical Interactions of Human MutY homolog linked with Familial Adenomatous Polyposis and colorectal cancer SyndromeSemantic proximity Read ↗

The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport.Semantic proximity Read ↗

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