Two phosphorylation sites on 53BP1 are found to mediate interaction with TOPBP1-RAD9 and shown to be essential for assembling the G1 DNA damage checkpoint response apparatus.

53BP1 and BRCA1 antagonistically control a temporal choice of two distinct pathways to restart stalled replication forks in a DNA double stand repair-independent manner.

A key cellular stress granule protein, G3BP1, is critical for efficient norovirus infection, representing the first pan-norovirus, pro-viral factor identified to date.

The RIF1-long and short splice variants show distinct ability to protect cells from replication stress by promoting 53BP1 nuclear bodies, representing the first described functional difference between the two variants.

A single-cell assay reveals that the genetic rewiring that underlies PARP inhibitor resistance drives altered DNA double-strand break end resection pathway choice.

Tumor Protein p53 Binding Protein 1 and Ubiquitin Specific Peptidase 28 engage p53 to promote mitotic efficiency.

The LIN37-DREAM complex has a critical role in regulating DNA double-strand break end processing and suppressing aberrant homology-directed repair in quiescent cells.

OptoGranules reveal the function of G3BP1 as a stress granule scaffold and demonstrate that protracted stress granule assembly is sufficient to drive neurodegeneration and the evolution of ALS-FTD pathology.

Irradiation of normal human fibroblasts and mice in conditions mimicking standard external X-ray radiotherapy protocols highlights that noncancerous cells surrounding the planning target volume accumulate DNA single-strand breaks but almost no double-strand breaks, putting them in a pre-cancerous senescent state.

Live-cell single-molecule imaging of DNA repair factors can be used to analyze their localization to DNA lesions and dissect the hierarchy of their recruitment.