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

Versatile protection from mutagenic DNA lesions conferred by bipartite recognition in nucleotide excision repair.

Mutation research - 1 Jan 2000

Maillard Olivier, Camenisch Ulrike, Blagoev Krastan B, Naegeli Hanspeter

Abstract excerpt

Nucleotide excision repair is a cut-and-patch pathway that eliminates potentially mutagenic DNA lesions caused by ultraviolet light, electrophilic chemicals, oxygen radicals and many other genetic insults. Unlike antigen recognition by the immune system, which employs billions of immunoglobulins and T-cell receptors, the nucleotide excision repair complex relies on just a few generic factors to detect an...

Read the complete abstract on PubMed

Topics

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

Share to Chromatin
Share to Cytoprotection
Share to DNA Damage

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Repair

Share to DNA Repair Enzymes

Share to Mutagens

Share to Protein Subunits

Share to Ultraviolet Rays

Source

Identifiers

PMID: 18321768
DOI: 10.1016/j.mrrev.2008.01.007

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Versatile protection from mutagenic DNA lesions conferred by bipartite recognition in nucleotide excision repair.PMID 18321768Read ↗

DNA repair glycosylase hNEIL1 triages damaged bases via competing interaction modes.Semantic proximity Read ↗

Mapping the sequence logic of DNA repair enzyme binding reveals mechanistic principles and evolutionary linksSemantic proximity Read ↗

A structural model for the damage-sensing complex in bacterial nucleotide excision repair.Semantic proximity Read ↗

Revealing A-T and G-C Hoogsteen base pairs in stressed protein-bound duplex DNA.Semantic proximity Read ↗

DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH.Semantic proximity Read ↗

Lesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging.Semantic proximity Read ↗

Dynamic Processing of a Common Oxidative DNA Lesion by the First Two Enzymes of the Base Excision Repair Pathway.Semantic proximity Read ↗

A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases.Semantic proximity Read ↗

A biophysical and structural analysis of DNA binding by oligomeric hSSB1 (NABP2/OBFC2B)Semantic proximity Read ↗

An active site aromatic triad in Escherichia coli DNA Pol IV coordinates cell survival and mutagenesis in different DNA damaging agents.Semantic proximity Read ↗

Removal of misincorporated ribonucleotides from prokaryotic genomes: an unexpected role for nucleotide excision repair.Semantic proximity Read ↗

UNG-RPA interaction governs the choice between high-fidelity and mutagenic uracil repairSemantic proximity Read ↗

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