Richard T. Pomerantz

This study identifies Polθ as a therapeutic target in DNMT3A-mutated leukemia by showing its essential role in DNA repair and replication fork restart, and demonstrates that its inhibition enhances standard therapies.

This study presents cryo-EM structures of Pol theta-helicase domain bound to DNA, revealing its conformational changes during microhomology-mediated end joining.

This paper introduces a method for template-independent enzymatic RNA synthesis using modified nucleotides and DNA polymerases, enabling the creation of RNA with defined sequences without traditional chemical synthesis limitations.

The paper identifies DNA repair and replication defects in early-onset renal cancer patients without known germline variants, suggesting these defects contribute to cancer development and may inform treatment strategies.

This study shows that the helicase domain of Polθ promotes alt-NHEJ by displacing RPA, leading to increased chromosomal translocations and reduced HR-mediated gene targeting.