Bret Freudenthal

The paper presents cryo-EM structures of a Blm10:13S proteasome intermediate, revealing parallel assembly pathways for the proteasome core particle involving Blm10 and Pba1/Pba2.

This study shows XRCC1 enhances DNA polymerase beta's efficiency in locating DNA damage by shifting its search strategy from 3D to 1D diffusion, improving damage recognition.

This study reveals how APE1 uses a dynamic search mechanism combining 1D and 3D diffusion to efficiently locate and repair AP-sites in DNA.

This study investigates how PARP1 binds to DNA breaks and chromatin, revealing that nucleosome unwrapping and allostery influence its affinity and binding dynamics.

This study determines the structure and dynamics of 8oxoG:C and 8oxoG:A base pairs in the nucleosome and characterizes MUTYH activity, revealing that 8oxoG:A is less processable by MUTYH.

This study shows that APE1's Asn174 residue stabilizes the AP-site through hydrogen bonding and electrostatic interactions, which are essential for catalytic activity.

The paper maps DNA-embedded ribonucleotides (rNMPs) across human cell types, revealing their non-random distribution and role as a novel epigenetic mark affecting gene expression.

This study determines the structural and kinetic mechanism of DNA Polymerase β processing 1-nt gaps in the nucleosome during DNA repair.

This study identifies factors influencing 8-oxoG-induced mutagenesis in human cells, revealing a hierarchical DNA repair network and chromatin structure effects on mutation patterns.

This study uses single-molecule fluorescence to show TDG uses multiple diffusion modes to search for DNA lesions and how its structure affects nucleosome interactions.

This study investigates the structure and function of the Fatty Acid Kinase complex in Staphylococcus aureus using modeling, biochemical, and cell-based approaches, revealing key residues and interactions essential for its activity.

This study investigates how human DNA polymerase β processes the mutagenic lesion Fapy*dG during DNA replication, showing inefficient bypass and incorporation, suggesting mutagenicity arises from bypass rather than lesion incorporation.

This study compares single-molecule DNA binding dynamics of purified OGG1 and nuclear extracts using SMADNE, revealing differences in undamaged DNA binding and increased binding lifetime for a catalytically dead variant in nuclear extracts.