parp 1 inhibitor olaparib (MedChemExpress)
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parp 1 inhibitor olaparib
Parp 1 Inhibitor Olaparib, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 97/100, based on 339 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/parp+inhibitors+olaparib/Olaparib/pmc13026560-181-7-14
Average 97 stars, based on 339 article reviews
Parp 1 Inhibitor Olaparib, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 97/100, based on 339 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/parp+inhibitors+olaparib/Olaparib/pmc13026560-181-7-14
Average 97 stars, based on 339 article reviews
parp 1 inhibitor olaparib - by Bioz Stars,
2026-09
97/100 stars
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Virus:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Infection:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Control:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Biomarker Discovery:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Knock-Out:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Western Blot:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Marker:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Migration:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Molecular Weight:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Activity Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Mutagenesis:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Plaque Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Proliferation Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Concentration Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. In Vitro:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Modification:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Purification:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Fluorescence:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Labeling:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Staining:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Mass Spectrometry:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Quantitative Proteomics:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Transformation Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Comparison:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Phospho-proteomics:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Sequencing:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Binding Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. RNA Sequencing:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Expressing:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Immunoprecipitation:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. ChIP-qPCR:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Screening Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Derivative Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Inhibition:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Microscopy:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Confocal Microscopy:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Activation Assay:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Isolation:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. Incubation:Article Title: The PARP1-EXD2 axis orchestrates R-loop resolution to safeguard genome stability. Article Snippet: R-loops, comprising an RNA–DNA hybrid and a displaced single-stranded DNA, are dynamic three-stranded nucleic acid structures that, when dysregulated, can disrupt transcription and replication, undermining genome integrity and contributing to human pathologies.. Here we identify exonuclease 3′–5′ domain-containing 2 (EXD2) as a pivotal R-loop resolvase.. We demonstrate that EXD2, through direct interaction with poly(ADP-ribose) (PAR) polymers synthesized by R-loop-bound and activated PAR polymerase 1 (PARP1), is recruited to R-loops, where it undergoes acetylation by the acetyltransferase CREB-binding protein at K416. |
![(A-B) Immunoblots showing increased protein levels of γH2A.x following siRNA-mediated depletion of ZNF423 ( n =3) compared to control ( n =3). GAPDH serves as loading control. Protein expression was normalized to total protein and quantified using ImageJ. Error bars reflect SEM. P-values represent unpaired, two-tailed t test with Welch’s correction. (C) Immunofluorescence staining for phosphorylated γH2A.x in ST88-14 cells (10x) following ZNF423 knockdown. DAPI stained nuclei are in blue, and phosphorylated γH2A.x positive cells are shown in green. Scale bars represent 240μm. (D-E) CellTiter-Glo viability assays were used to generate dose response curves for four MPNST cell lines treated with doxorubicin or ifosfamide. IC₅₀ values were calculated using nonlinear regression (log[inhibitor] vs. normalized response, variable slope model). Error bars reflect SEM. (F) Representative phase-contrast images of ST88-14 cells showing enhanced growth inhibition following combined ZNF423 knockdown and treatment with doxorubicin or ifosfamide compared to scrambled controls. Scale bars represent 360μm. (G-H) Quantification of cell viability by CellTiter-Glo assay following ZNF423 depletion in combination with doxorubicin or ifosfamide treatment ( n =6). P-values represent two-way ANOVA with Tukey’s multiple comparisons tests across groups. Error bars reflect SEM. (I) Dose-response curves for three MPNST cell lines treated with the PARP inhibitor olaparib. IC₅₀ values were calculated using nonlinear regression (log[inhibitor] vs. normalized response, variable slope model). Error bars reflect SEM. (J) Representative images showing enhanced growth inhibition following ZNF423 siRNA-mediated knockdown combined with olaparib treatment. Scale bars, 360μm. (K-M) Quantification of cell viability by CellTiter-Glo assay following combined ZNF423 depletion and PARP inhibitor treatment ( n =6). P-values represent two-way ANOVA with Tukey’s multiple comparisons tests across groups. Error bars reflect SEM. (N) Immunoblots of JH-2-002 cells showing increased γH2A.x following ZNF423 knockdown and treatment with olaparib. ****=p-value ≤0.0001, ***=p-value≤0.001, **=p-value≤0.01, *=p-value≤0.05, ns=not significant.](https://bio-rxiv-images-cdn.bioz.com/dois_ending_with_60/10__64898_slash_2026__03__03__709360/10__64898_slash_2026__03__03__709360___F4.large.jpg)