The innate immune protein PKR, which is inhibited by viral proteins that mimic its natural substrate, has access to a wide spectrum of inhibitor-evading mutations that maintain natural substrate binding.

KPNB1 regulates rhythmic spatio-temporal nuclear import of the PER/CRY complex and is required for negative feedback repression in mammalian and fly clock function.

One-step Isolation and Lysis (OIL) PCR offers a robust, versatile, accessible, and high-throughput method for linking mobile DNA with bacterial hosts in natural microbial communities.

The crystal structure of Pur-alpha in complex with DNA reveals its molecular mechanisms of nucleic-acid binding and unwinding, allowing for a better understanding of its essential role in neurons.

A polarized Moody/protein kinase A pathway plays an unrecognized central role in controlling the enormous cell growth and blood–brain barrier integrity in a highly coordinated spatiotemporal manner in brain homeostasis.

A minimal subset of two to three residues in cyclic nucleotide binding (CNB) domains controls nucleoside vs. cyclic nucleotide specificity, repurposing PKA of certain pathogens for novel nucleoside signaling pathways or sensing.

C9ORF72 antisense repeat expanded RNAs activate PKR/eIF2α dependent integrated stress response and cause neuronal toxicity independent of DPR proteins.

Changes in the interactome of the Rel family of transcription factors control adaptation to the environmental stress of hyperosmolarity and determine cell fate.

Upon traumatic brain injury in Drosophila adults, a previously unknown Pvr–AP-1–Mmp1 signaling pathway is activated in astrocytes.

The resurrection of ancient ancestral intrinsically disordered proteins reveals the evolution of a protein-protein interaction in molecular detail.