ArticleMolecular and cellular biology1998
XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 359 papers, 8 of them syntheses that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
359 citing papers in PubMed, 8 syntheses or guidelines pooled it, 901 citations in OpenAlex.
- Significant Association Between XRCC1 Expression and Its rs25487 Polymorphism and Radiotherapy-Related Cancer Prognosis.Frontiers in oncology · 2021Pooled it
- The XRCC1 Arg194Trp and Arg280His polymorphisms in head and neck cancer susceptibility: a meta-analysis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Pooled it
- Association of XRCC1 genetic polymorphism (Arg399Gln) with laryngeal cancer: a meta-analysis based on 4,031 subjects.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Pooled it
- XRCC1 Arg399Gln polymorphism confers risk of breast cancer in American population: a meta-analysis of 10846 cases and 11723 controls.PloS one · 2014Pooled it
- XRCC1 Arg399Gln, Arg194Trp, and Arg280His polymorphisms in esophageal cancer risk: a meta-analysis.Digestive diseases and sciences · 2013Pooled it
- A meta-analysis of an association between the XRCC1 polymorphisms and gliomas risk.Journal of neuro-oncology · 2013Pooled it
- DNA repair gene XRCC1 polymorphisms, smoking, and bladder cancer risk: a meta-analysis.PloS one · 2013Pooled it
- Racial and tissue-specific cancer risk associated with PARP1 (ADPRT) Val762Ala polymorphism: a meta-analysis.Molecular biology reports · 2012Pooled it
- GCN5 and TADA2B constitutively regulate XRCC1 function during DNA repair to maintain cell survival.Cell death and differentiation · 2026Article
- The Landscape of BRCA1-Associated Post-Translational Modifications.Cell biology international · 2026Review
- A Large-Scale Method to Measure the Stoichiometries of Protein Poly-ADP-Ribosylation.ACS chemical biology · 2026Article
- PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation.Nature communications · 2026Article
- Article
- Anti-trapping scaffold protein: significance in cancer cell innate immune signaling and opportunities for immunotherapy.Frontiers in immunology · 2026Review
- Nuclear poly(A)-binding protein and nucleolin utilize their RNA recognition motifs to read PAR chains.Nucleic acids research · 2025Article
- Protein-Protein Interactions in Base Excision Repair.Biomolecules · 2025Review
- Single-molecule studies of repair proteins in base excision repair.BMB reports · 2025Review
- Novel inhibitors of PARP1 and PARP14: design, synthesis, and potentiation of cisplatin efficacy in cancer.Future medicinal chemistry · 2025Article
- Genetic Navigation: A Narrative Review of XRCC1 Polymorphism Impact on Platinum-Based Chemotherapy Outcomes in NSCLC Patients.Cancer management and research · 2025Review
- PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation.EMBO reports · 2024Article
299 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
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poly(ADP-ribose) polymerase (PARP; EC 2.4.2.30) is a zinc-finger DNA-binding protein that detects and signals DNA strand breaks generated directly or indirectly by genotoxic agents. In response to these breaks, the immediate poly(ADP-ribosyl)ation of nuclear proteins involved in chromatin architecture and DNA metabolism converts DNA damage into intracellular signals that can activate DNA repair programs or cell death options. To have greater insight into the physiological function of this enzyme, we have used the two-hybrid system to find genes encoding proteins putatively interacting with PARP. We have identified a physical association between PARP and the base excision repair (BER) protein XRCC1 (X-ray repair cross-complementing 1) in the Saccharomyces cerevisiae system, which was further confirmed to exist in mammalian cells. XRCC1 interacts with PARP by its central region (amino acids 301 to 402), which contains a BRCT (BRCA1 C terminus) module, a widespread motif in DNA repair and DNA damage-responsive cell cycle checkpoint proteins. Overexpression of XRCC1 in Cos-7 or HeLa cells dramatically decreases PARP activity in vivo, reinforcing the potential protective function of PARP at DNA breaks. Given that XRCC1 is also associated with DNA ligase III via a second BRCT module and with DNA polymerase beta, our results provide strong evidence that PARP is a member of a BER multiprotein complex involved in the detection of DNA interruptions and possibly in the recruitment of XRCC1 and its partners for efficient processing of these breaks in a coordinated manner. The modular organizations of these interactors, associated with small conserved domains, may contribute to increasing the efficiency of the overall pathway.
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Registered trials
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.