Automated Author Profile

Lane, Karen

Current S-Index

2.3

Sum of Dataset Indices for all datasets

Average Dataset Index per Dataset

0.8

Average Dataset Index per dataset

Total Datasets

3

Total datasets for this author

Average FAIR Score

65.4%

Average FAIR Score per dataset

Total Citations

0

Total citations to the author's datasets

Total Mentions

0

Total mentions of the author's datasets

S-Index Interpretation

S-Index Over Time

Cumulative Citations Over Time

Cumulative Mentions Over Time

Datasets

ARID1A stabilises non-homologous end joining factors at DNA breaks induced by the G4 ligand pyridostatin. Sousa, Amin, et al.

No description available

Authors

  • Lane, Karen
0 Citations0 Mentions65% FAIR0.7 Dataset Index
10.17632/ys34fgz4cx.1January 2026

ARID1A stabilises non-homologous end joining factors at DNA breaks induced by the G4 ligand pyridostatin. Sousa, Amin, et al.

Raw data for Sousa, Amin, et al., 2025Abstract:ARID1A is a subunit of the BAF chromatin remodelling complex that is frequently mutated in cancer. It is challenging to predict how ARID1A loss impacts cancer therapy response because it participates in many different cellular pathways. G quadruplex (G4) binding ligands, such as pyridostatin, have shown anticancer effects, but the pathways and genetic determinants involved in the response to G4 ligands are still not fully understood. Here, we show that ARID1A deficient cells are selectively sensitive to pyridostatin when compared with isogenic controls. Sensitivity to pyridostatin was apparent in ovarian and colorectal cancer cell line models, and in vivo studies suggest that G4 ligands hold promise for treating ARID1A deficient cancers. While we find that ARID1A impacts on pyridostatin-induced transcriptional responses, we find that pyridostatin-mediated toxicity in ARID1A-deficient cells is driven by defective DNA repair of topoisomerase-induced breaks. We show that ARID1A-deficient cells are unable to efficiently accumulate non-homologous end joining proteins on chromatin following pyridostatin exposure. These data uncover a role for ARID1A in the cellular response to G4 ligands, and link remodelling to G4 ligand-induced transcriptional and DNA damage responses.

Authors

  • Lane, Karen
0 Citations0 Mentions65% FAIR1.6 Dataset Index
10.17632/ys34fgz4cxAugust 2025

ARID1A stabilises non-homologous end joining factors at DNA breaks induced by the G4 ligand pyridostatin. Sousa, Amin, et al.

Raw data for Sousa, Amin, et al., 2025Abstract:ARID1A is a subunit of the BAF chromatin remodelling complex that is frequently mutated in cancer. It is challenging to predict how ARID1A loss impacts cancer therapy response because it participates in many different cellular pathways. G quadruplex (G4) binding ligands, such as pyridostatin, have shown anticancer effects, but the pathways and genetic determinants involved in the response to G4 ligands are still not fully understood. Here, we show that ARID1A deficient cells are selectively sensitive to pyridostatin when compared with isogenic controls. Sensitivity to pyridostatin was apparent in ovarian and colorectal cancer cell line models, and in vivo studies suggest that G4 ligands hold promise for treating ARID1A deficient cancers. While we find that ARID1A impacts on pyridostatin-induced transcriptional responses, we find that pyridostatin-mediated toxicity in ARID1A-deficient cells is driven by defective DNA repair of topoisomerase-induced breaks. We show that ARID1A-deficient cells are unable to efficiently accumulate non-homologous end joining proteins on chromatin following pyridostatin exposure. These data uncover a role for ARID1A in the cellular response to G4 ligands, and link remodelling to G4 ligand-induced transcriptional and DNA damage responses.

Authors

  • Lane, Karen
0 Citations0 Mentions65% FAIR0.7 Dataset Index
10.17632/ys34fgz4cx.2August 2025