The newly developed antibody-free techniques, HepG4-seq for G-quadruplexes and HBD-seq for R-loops, robustly reveal the comprehensive maps of native G-quadruplexes and R-loops, as well as their roles in transcriptional regulation.

The DNA flanks on either side of an R-loop differ in stability, and CRISPR-Cas12 enzymes form double-strand breaks by targeting the more unstable flank with their single DNase active site.

The deposition of 5-hydroxymethylcytosine epigenetic marks in active genes promotes the annealing of the nascent RNA to the template DNA strand, forming an R-loop.

Genetic analyses in budding yeast coupled with biochemical assays have revealed an unexpected role for the Smc5/6 complex in cellular pathways responsible for the prevention of RNA formation in genomic DNA.

Reconstitution of orientation-specific R-loop-replisome collisions with purified proteins reveals the differential impact of R-loop-associated RNA:DNA hybrids and G-quadruplexes on replication fork progression.

Blocking the bacterial lipid flippase MprF by monoclonal antibodies enhance staphylococcal clearance by host defense and antibiotics providing a novel proof of concept for antivirulence approaches targeting bacterial resistance mechanisms.

Six BBS proteins form a core BBSome transport vehicle, which is sufficient for recognizing membrane proteins for transport into the ciliary compartment.

Autoantibodies from myasthenia gravis patients bind a common core region on the nicotinic acetylcholine receptor through a largely conserved mechanism.

Multimodal spectroscopy (smFRET, EPR, SAXS, and SANS) and integrative structural modeling reveal large-scale domain rearrangements in human guanylate binding protein 1 (hGBP1) that are driving forces for the formation of oligomers that enable its biological function in innate immune defense.

The anchoring properties of Ca_V β2 subunits to the plasma membrane determine the biophysical states of Ca_V2.2 channels by regulating PIP₂ coupling to the nonspecific phospholipid-binding site in the I–II loop.