PARP1 plays a critical role in DNA repair and chromatin remodeling. It is involved in various DNA repair pathways, including single-strand break (SSB) repair, double-strand break (DSB) repair, and nucleotide excision repair (NER). PARP1 also modulates chromatin structure, which is essential for efficient DNA repair. The inhibition of PARP1 is being explored as a therapeutic strategy for cancers with DNA repair defects, such as ovarian, breast, and prostate cancers. This approach exploits synthetic lethality, where the loss of PARP1 function in combination with mutations in DNA repair genes leads to cell death. PARP1 is a multifunctional enzyme that catalyzes the polymerization of ADP-ribose units, leading to the formation of poly(ADP-ribose) (PAR), which facilitates DNA repair and chromatin remodeling. PARP1 interacts with various proteins involved in DNA repair and chromatin remodeling, such as XRCC1, TDP1, and ALC1. PARP1 also plays a role in replication fork stabilization and processing, and its activity is crucial for the maintenance of genomic stability. The inhibition of PARP1 can lead to increased DNA damage and genomic instability, which can be detrimental to cells. PARP1 is also involved in the regulation of transcription and the recruitment of chromatin remodeling complexes. The development of PARP inhibitors has shown promise in the treatment of cancers with DNA repair defects, and further research is needed to understand the complex mechanisms by which PARP1 regulates DNA repair and chromatin remodeling.PARP1 plays a critical role in DNA repair and chromatin remodeling. It is involved in various DNA repair pathways, including single-strand break (SSB) repair, double-strand break (DSB) repair, and nucleotide excision repair (NER). PARP1 also modulates chromatin structure, which is essential for efficient DNA repair. The inhibition of PARP1 is being explored as a therapeutic strategy for cancers with DNA repair defects, such as ovarian, breast, and prostate cancers. This approach exploits synthetic lethality, where the loss of PARP1 function in combination with mutations in DNA repair genes leads to cell death. PARP1 is a multifunctional enzyme that catalyzes the polymerization of ADP-ribose units, leading to the formation of poly(ADP-ribose) (PAR), which facilitates DNA repair and chromatin remodeling. PARP1 interacts with various proteins involved in DNA repair and chromatin remodeling, such as XRCC1, TDP1, and ALC1. PARP1 also plays a role in replication fork stabilization and processing, and its activity is crucial for the maintenance of genomic stability. The inhibition of PARP1 can lead to increased DNA damage and genomic instability, which can be detrimental to cells. PARP1 is also involved in the regulation of transcription and the recruitment of chromatin remodeling complexes. The development of PARP inhibitors has shown promise in the treatment of cancers with DNA repair defects, and further research is needed to understand the complex mechanisms by which PARP1 regulates DNA repair and chromatin remodeling.