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Article

XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening.

DNA repair - 4 Feb 2007

Wu Yili, Zacal Natalie J, Rainbow Andrew J, Zhu Xu-Dong

Abstract excerpt

TRF2, a telomere-binding protein, is a crucial player in telomere length maintenance. Overexpression of TRF2 results in telomere shortening in both normal primary fibroblasts and telomerase-positive cancer cells. TRF2 is found to be associated with XPF-ERCC1, a structure-specific endonuclease involved in nucleotide excision repair, crosslink repair and DNA recombination. XPF-ERCC1 is implicated in TRF2-dependent...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17055345
DOI: 10.1016/j.dnarep.2006.09.005

Genes

ERCC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

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XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening.PMID 17055345Read ↗

Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms.Semantic proximity Read ↗

TRF2 overexpression diminishes repair of telomeric single-strand breaks and accelerates telomere shortening in human fibroblastsSemantic proximity Read ↗

Role of the TRF2 Telomeric Protein in Cancer and AgingSemantic proximity Read ↗

Function and Interactions of ERCC1-XPF in DNA Damage ResponseSemantic proximity Read ↗

The Intra- and Extra-Telomeric Role of TRF2 in the DNA Damage ResponseSemantic proximity Read ↗

Homologous recombination generates T-loop-sized deletions at human telomeres.Semantic proximity Read ↗

ZNF524 directly interacts with telomeric DNA and supports telomere integritySemantic proximity Read ↗

The structure-specific endonuclease Ercc1-Xpf is required for targeted gene replacement in embryonic stem cells.Semantic proximity Read ↗

TRF2 Protects Human Telomeres from End-to-End FusionsSemantic proximity Read ↗

Human telomeric protein TRF2 associates with genomic double-strand breaks as an early response to DNA damageSemantic proximity Read ↗

Telomere Repeat Binding Factor 2 Interacts with Base Excision Repair Proteins and Stimulates DNA Synthesis by DNA Polymerase βSemantic proximity Read ↗

The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision RepairSemantic proximity Read ↗

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