Scott G. Olenych

TL;DR: This work introduced a method for optically imaging intracellular proteins at nanometer spatial resolution and used this method to image specific target proteins in thin sections of lysosomes and mitochondria and in fixed whole cells to image retroviral protein Gag at the plasma membrane.

TL;DR: Two-color photoactivated localization microscopy is used to determine the ultrastructural relationship between different proteins fused to spectrally distinct photoactivatable fluorescent proteins (PA-FPs) and its potential to directly visualize molecular interactions within cellular structures at the nanometer scale is suggested.

TL;DR: Cells presented with micropatterns of cytophilic and cytophobic surfaces generated by polymer-on-polymer stamping displayed a surface-dependent cytoskeletal organization and a dramatic preference for adhesion to, and spreading on, the cytophobic surface, demonstrating the utility of polyelectrolyte films in manipulating smooth muscle cell adhesion and behavior.

TL;DR: It is demonstrated that the protein-chromophore interactions responsible for blue-shifting the absorbance and emission maxima of mTFP1 operate independently of the chromophore structure, and the two histidine residues in close proximity to the Chromophore are approximately equal determinants of theblue-shifted fluorescence emission of m TFP1.

TL;DR: Expansion of the fluorescent protein family to include optical highlighters and FRET biosensors further arms this ubiquitous class of fluorophores with biological probes capable of photoactivation, photoconversion, and detection of molecular interactions beyond the resolution limits of optical microscopy.