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

Physical and Functional Interaction between the XPF/ERCC1 Endonuclease and hRad52

26 Mar 2004

Abstract excerpt

The XPF/ERCC1 heterodimer is a DNA structure-specific endonuclease that participates in nucleotide excision repair and homology-dependent recombination reactions, including DNA single strand annealing and gene targeting. Here we show that XPF/ERCC1 is stably associated with hRad52, a recombinational repair protein, in human cell-free extracts and that these factors interact directly via the N-terminal domain of...

Read the complete abstract on PubMed

Topics

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

Share to CRISPR and Genetic Engineering
Share to DNA Repair Mechanisms
Share to PARP inhibition in cancer therapy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 14734547
DOI: 10.1074/jbc.m313779200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Physical and Functional Interaction between the XPF/ERCC1 Endonuclease and hRad52PMID 14734547Read ↗

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

Activity of individual ERCC1 and XPF subunits in DNA nucleotide excision repair.Semantic proximity Read ↗

Multiple DNA binding domains mediate the function of the ERCC1-XPF protein in nucleotide excision repair.Semantic proximity Read ↗

The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways.Semantic proximity Read ↗

DNA repair endonuclease ERCC1-XPF as a novel therapeutic target to overcome chemoresistance in cancer therapy.Semantic proximity Read ↗

The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition.Semantic proximity Read ↗

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

Mapping of interaction domains between human repair proteins ERCC1 and XPFSemantic proximity Read ↗

Human Rad52 Promotes XPG-Mediated R-loop Processing to Initiate Transcription-Associated Homologous Recombination RepairSemantic proximity Read ↗

Recruitment and positioning determine the specific role of the XPF-ERCC1 endonuclease in interstrand crosslink repair.Semantic proximity Read ↗

Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation.Semantic proximity Read ↗

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