Browse the toolkit beneath workflows. The mechanism branch runs mechanism -> architecture -> component, while the technique branch runs from high-level approaches down to concrete methods.
13 items matching 1 filter
Mechanism Branch
Layer 1
Mechanisms
Top-level concepts: biophysical action modes such as heterodimerization, photocleavage, or RNA binding.
Layer 2
Architectures
Arrangements that realize or deploy mechanisms, including switches, construct patterns, and delivery strategies.
Layer 3
Components
Low-level parts and sequence-defined elements used inside architectures, including protein domains and RNA elements.
Technique Branch
Layer 1
Approaches
High-level engineering practices such as computational design, directed evolution, sequence verification, and functional assay.
Layer 2
Methods
Concrete methods used to design, build, verify, or characterize engineered systems.
Showing 1-13 of 13
AKAR3EV is a previously developed genetically encoded Förster resonance energy transfer (FRET) biosensor for protein kinase A activity that comprises a CFP/YFP fluorescent protein pair. In the cited 2020 ACS Sensors study, it served as the benchmark comparator for the red-shifted Booster-PKA biosensor.
CFP-YFP FRET biosensors are genetically encoded visible-range reporter constructs used in the cited study to measure RhoA activity and Rac1-GDI binding. In that work, they were combined with a near-infrared Rac1 biosensor to enable parallel imaging of Rho GTPase signaling during optogenetic manipulation of Rac1.
Single cell FRET measurements with Rho GTPase biosensors are a quantitative cell-based assay used in primary human endothelial cells to monitor guanine nucleotide exchange factor activity toward Cdc42 and Rac1. In the cited study, the method was applied to compare the cellular activities of overexpressed endothelial GEFs.
Condensate-specific lifetimes were used to track protein-protein interactions by measuring FLIM-Förster resonance energy transfer (FRET). We used condensate FLIM-FRET to evaluate whether mRNA decapping complex subunits can form decapping-competent interactions within P-bodies.
From a variety of initial designs two have emerged as promising prototypes for further optimization: FRET (Förster Resonance Energy Transfer)-based sensors and single fluorophore sensors of the GCaMP family.
Imaging molecular interactions in living cells by FRET microscopy. FRET imaging provides information about all these molecular processes with high specificity and sensitivity via probes expressed by or introduced from the external medium into the cell, tissue or organism.
Förster or fluorescence resonance energy transfer (FRET) technology and genetically encoded FRET biosensors provide a powerful tool for visualizing signaling molecules in live cells with high spatiotemporal resolution.
Sensitive FRET imaging is an assay method used in combination with optogenetics to monitor local microtubule manipulations. The available evidence identifies it as a light-associated functional imaging approach for observing spatially localized perturbations of the microtubule system.
In this study, we probed the effects of a few key mutations on the coupled binding and folding of α-synuclein by using a combination of single-molecule (smFRET) and ensemble (far-UV CD) measurements.
Biomaterial based surface ligands are designed and developed based on theoretical simulations. The hybrid nanobiomaterials satisfy anisotropic facet-selective coating, enabling effective compartmentalization beyond non-specific staining.
Finally, we highlight the importance of emerging imaging tools like Förster resonance energy transfer imaging and optogenetics in detecting, measuring and manipulating the action of cyclic nucleotide signaling cascades.
The miRFP670-miRFP720 FRET pair is a fully near-infrared genetically encoded Förster resonance energy transfer pair used to construct biosensors. It enables multiplexed biosensor imaging that is compatible with CFP-YFP imaging channels and blue-green optogenetic tools.
Here we have devised a family of photoswitchable quantum dots (psQDs) in which the semiconductor core functions as a fluorescence donor in Förster resonance energy transfer (FRET), and multiple photochromic diheteroarylethene groups function as acceptors upon activation by ultraviolet light.