Quantitative FRET UPR induction assay is used to measure IRE1 and BIP association and dissociation by a variety of ER misfolded proteins and by an important BiP substrate-binding domain mutant, significantly enhancing the evidence for the allosteric UPR induction model.

VRAC activation, observed with a FRET sensor of intracellular LRRC8-domains movement during gating and by fluorometry, requires plasma membrane localization and diacylglycerol signaling, but is independent of intracellular ionic strength.

Fluorescent sensors can track the movement and distribution of the plant hormone abscisic acid in roots and leaves in Arabidopsis.

Observation by single molecule FRET of MscL, a prokaryotic mechanosensitive channel, reveals that MscL opens via the helix-tilt model and its pore reaches 2.8 nm in diameter.

The yeast Saccharomyces cerevisiae has informed our understanding of molecular biology and genetics for decades, and learning more about its natural history could fuel a new era of functional and evolutionary studies of this classic model organism.

Single-cell FRET measurements reveal large temporal activity fluctuations within this signaling pathway in Escherichia coli, caused by stochasticity of receptor methylation combined with allosteric interactions and slow rearrangements within receptor clusters.

The combined use of optical trapping and single-molecule FRET permits the study of riboswitch structure formation and conformational dynamics at the same time.

Multi-site FRET measurements of moPrP oligomerization at low pH indicate that major conformational changes take place as monomers reversibly transform into large oligomers, which subsequently disassemble reversibly into small oligomers.

A new FRET-based cAMP biosensor with nanomolar sensitivity makes it possible to measure cAMP dynamics in miniscule subcellular compartments like cilia and flagella.