ArticleThe EMBO journal2002
The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed, 203 citations in OpenAlex.
- CRISPR Screening Identifies SMARCAL1 and MRN as Modulators of WRN Dependency in MSI-H Colorectal Cancer.Cancer research · 2026Article
- Rad1-Rad10 uses different interfaces to interact with pathway-specific DNA repair factors.Nucleic acids research · 2026Article
- Engineering quantum dot surfaces to preserve protein-DNA interactions for single-molecule visualization.Nano convergence · 2026Article
- Nucleotide excision repair and poly(ADP-ribose) polymerase 1 cooperate in HBV cccDNA synthesis: A potential viral therapeutic target.JHEP reports : innovation in hepatology · 2026Article
- Evaluation of ERCC4 (XPF) gene rs6498486 polymorphism and its potential role in breast cancer risk among Bangladeshi women.BMC cancer · 2026Article
- The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair.Nucleic acids research · 2026Article
- Molecular basis of XPF-ERCC1 targeting to SLX4-dependent DNA repair pathways.Nature communications · 2025Article
- The Converging Roles of Nucleases and Helicases in Genome Maintenance and the Aging Process.Life (Basel, Switzerland) · 2025Review
- Role of the nucleotide excision repair endonuclease XPF in the kinetoplastid parasite Trypanosoma brucei.Scientific reports · 2025Article
- Beyond Nucleotide Excision Repair: The Importance of XPF in Base Excision Repair and Its Impact on Cancer, Inflammation, and Aging.International journal of molecular sciences · 2024Review
- Review
- Skeletal phenotypes and molecular mechanisms in aging mice.Zoological research · 2024Review
- Persistent TFIIH binding to non-excised DNA damage causes cell and developmental failure.Nature communications · 2024Article
- Article
- ERCC4: a potential regulatory factor in inflammatory bowel disease and inflammation-associated colorectal cancer.Frontiers in endocrinology · 2024Review
- A novel algorithm for the virtual screening of extensive small molecule libraries against ERCC1/XPF protein-protein interaction for the identification of resistance-bypassing potential anticancer molecules.Turkish journal of biology = Turk biyoloji dergisi · 2024Article
- Fanconi anemia DNA crosslink repair factors protect against LINE-1 retrotransposition during mouse development.Nature structural & molecular biology · 2023Article
- A disease-associated XPA allele interferes with TFIIH binding and primarily affects transcription-coupled nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- XPF activates break-induced telomere synthesis.Nature communications · 2022Article
- Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
42 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
XPF-ERCC1 is a structure-specific endonuclease involved in nucleotide excision repair, interstrand crosslink repair and homologous recombination. So far, it has not been shown experimentally which subunit of the heterodimer harbors the nuclease activity and which amino acids contribute to catalysis. We used an affinity cleavage assay and located the active site to amino acids 670-740 of XPF. Point mutations generated in this region were analyzed for their role in nuclease activity, metal coordination and DNA binding. Several acidic and basic residues turned out to be required for nuclease activity, but not DNA binding. The separation of substrate binding and catalysis by XPF-ERCC1 will be invaluable in studying the role of this protein in various DNA repair processes. Alignment of the active site region of XPF with proteins belonging to the Mus81 family and a putative archaeal RNA helicase family reveals that seven of the residues of XPF involved in nuclease activity are absolutely conserved in the three protein families, indicating that they share a common nuclease motif.
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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.