We next performed immunogold transmission electron microscopy to visualize GRP78 expression in secretory granules.
Here, we overcome these limitations by employing CO-functionalized atomic force microscopy to visualize structures corresponding to boron-boron covalent bonds.
To further confirm these sequential steps during neutrophil extravasation in detail, we used electron microscopy to visualize each stage of the neutrophil extravasation cascade.
We combined fluorescent molecular tension sensors with super-resolution light microscopy to visualize traction forces within FAs with <100 nm spatial resolution.
To address mechanisms governing this segregation, we used two-photon microscopy to visualize migration of purified thymocyte subsets in defined microenvironments within thymic slices.
They also used fluorescence confocal microscopy to visualize the molecular diffusion and neuronal enhancement in 3-D to identify both highlighted neurons and their network.
The collaboration employed negative-staining electron microscopy to visualize the Cas9 protein bound to either guide RNA, or both RNA and target DNA.
A cross-section of the indent was studied by transmission electron microscopy to visualize the deformed microstructure.
To validate the results obtained on live cells using exogenous fusion proteins of FAK and actin filaments, we applied laser scanning confocal microscopy to visualize the endogenous FAK and actin filaments localization in fixed cells.
To validate the results obtained on live cells using exogenous fusion proteins of FAK and paxillin, we applied laser scanning confocal microscopy to visualize endogenous FAK and paxillin on fixed cells stained with the anti-FAK and anti-paxillin antibodies.
Together, in this perspective review article, we demonstrate the utilization of time-lapse FRET microscopy to visualize the signaling event via the tri-molecular protein complex formation and their biological outcomes.
