A novel microscopy-based assay shows that dendritic cells encountering pathogenic stimuli form increased complexes of specific SNARE proteins, driving release of large amounts of inflammatory cytokines.
Rigorous assays of membrane fusion show that a distinct tethering step is required for lumenal compartment mixing in a manner that extends beyond simply increasing the amount of total trans-SNARE complex.
Fluorescent derivatives of a bacteriophage protein that binds double-stranded ends can trap and label genome-destabilizing double-strand DNA breaks in bacterial and human cells, and illuminate the origins of spontaneous DNA breakage in both.
Peptide and nitrate transporters have been converted into fluorescent reporters of transport activity and have been used to measure various transport properties including the dual affinity of the nitrate transceptor
Cell imaging and mathematical modelling show reciprocal cross-regulation between inflammatory signalling and cell cycle timing, which is mediated through functional interactions between NF-B and E2F proteins.