ArticleNucleic acids research2007
Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- FB23-2 and Cisplatin Synergize to Inhibit Head and Neck Squamous Cell Carcinoma by Targeting the XPF/ERCC1 Complex.Cancer science · 2026Article
- The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair.Nucleic acids research · 2026Article
- Nano-delivery of a novel inhibitor of ERCC1-XPF for targeted sensitization of colorectal cancer to platinum-based chemotherapeutics.Drug delivery and translational research · 2025Article
- Small Molecule Antagonists of the DNA Repair ERCC1/XPA Protein-Protein Interaction.ChemMedChem · 2024Article
- A key interaction with RPA orients XPA in NER complexes.Nucleic acids research · 2020Article
- Distinct DNA repair pathways cause genomic instability at alternative DNA structures.Nature communications · 2020Article
- Function and Interactions of ERCC1-XPF in DNA Damage Response.Molecules (Basel, Switzerland) · 2018Review
- Control of structure-specific endonucleases to maintain genome stability.Nature reviews. Molecular cell biology · 2017Review
- Single-stranded DNA Binding by the Helix-Hairpin-Helix Domain of XPF Protein Contributes to the Substrate Specificity of the ERCC1-XPF Protein Complex.The Journal of biological chemistry · 2017Article
- Metal binding mediated conformational change of XPA protein:a potential cytotoxic mechanism of nickel in the nucleotide excision repair.Journal of molecular modeling · 2016Article
- Role of the XPA protein in the NER pathway: A perspective on the function of structural disorder in macromolecular assembly.Computational and structural biotechnology journal · 2016Review
- Review
- The Cerebro-oculo-facio-skeletal Syndrome Point Mutation F231L in the ERCC1 DNA Repair Protein Causes Dissociation of the ERCC1-XPF Complex.The Journal of biological chemistry · 2015Article
- Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA).Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Molecular mechanism of global genome nucleotide excision repair.Acta naturae · 2014Article
- Nucleotide excision repair in eukaryotes.Cold Spring Harbor perspectives in biology · 2013Review
- Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response.Cell research · 2013Article
- Architecture and DNA recognition elements of the Fanconi anemia FANCM-FAAP24 complex.Structure (London, England : 1993) · 2013Article
- Structural and sequence similarities of hydra xeroderma pigmentosum A protein to human homolog suggest early evolution and conservation.BioMed research international · 2013Article
- DNA repair endonuclease ERCC1-XPF as a novel therapeutic target to overcome chemoresistance in cancer therapy.Nucleic acids research · 2012Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human ERCC1/XPF is a structure-specific endonuclease involved in multiple DNA repair pathways. We present the solution structure of the non-catalytic ERCC1 central domain. Although this domain shows structural homology with the catalytically active XPF nuclease domain, functional investigation reveals a completely distinct function for the ERCC1 central domain by performing interactions with both XPA and single-stranded DNA. These interactions are non-competitive and can occur simultaneously through distinct interaction surfaces. Interestingly, the XPA binding by ERCC1 and the catalytic function of XPF are dependent on a structurally homologous region of the two proteins. Although these regions are strictly conserved in each protein family, amino acid composition and surface characteristics are distinct. We discuss the possibility that after XPF gene duplication, the redundant ERCC1 central domain acquired novel functions, thereby increasing the fidelity of eukaryotic DNA repair.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.