Dronpa-Green | MBL Life Sience -ASIA-
Subdiffraction Imaging through the Selective Donut-Mode Depletion of Thermally Stable Photoswitchable Fluorophores: Numerical Analysis and Application to the Fluorescent Protein Dronpa | Journal of the American Chemical Society
A Stroboscopic Approach for Fast Photoactivation−Localization Microscopy with Dronpa Mutants | Journal of the American Chemical Society
Dronpa-Green | MBL Life Science -JAPAN-
Extending fluorescence anisotropy to large complexes using reversibly switchable proteins | Nature Biotechnology
Red fluorescent proteins: chromophore formation and cellular applications – topic of research paper in Biological sciences. Download scholarly article PDF and read for free on CyberLeninka open science hub.
Regulated Fast Nucleocytoplasmic Shuttling Observed by Reversible Protein Highlighting | Science
Sensors | Free Full-Text | Genetically Encoded Biosensors Based on Fluorescent Proteins
Ultrafast Excited-State Dynamics of the Photoswitchable Protein Dronpa | Journal of the American Chemical Society
Kaede | MBL Life Sience -ASIA-
An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein | PNAS
Ultrafast Excited-State Dynamics of the Photoswitchable Protein Dronpa | Journal of the American Chemical Society
Materials | Free Full-Text | Application of Genetically Encoded Photoconvertible Protein SAASoti for the Study of Enzyme Activity in a Single Live Cell by Fluorescence Correlation Microscopy
Frontiers | The role of host pigments in coral photobiology
RCSB PDB - 2Z6Z: Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state
First biphotochromic fluorescent protein moxSAASoti stabilized for oxidizing environment | Scientific Reports
Dronpa-Green | MBL Life Science -JAPAN-
A highly photostable and bright green fluorescent protein | Nature Biotechnology
RCSB PDB - 2Z6Y: Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state
Conversion of the Monomeric Red Fluorescent Protein into a Photoactivatable Probe: Chemistry & Biology
Low-Temperature Chromophore Isomerization Reveals the Photoswitching Mechanism of the Fluorescent Protein Padron | Journal of the American Chemical Society
Fast and Reversible Photoswitching of the Fluorescent Protein Dronpa as Evidenced by Fluorescence Correlation Spectroscopy: Biophysical Journal
A Stroboscopic Approach for Fast Photoactivation−Localization Microscopy with Dronpa Mutants | Journal of the American Chemical Society
Ultrafast Excited-State Dynamics of the Photoswitchable Protein Dronpa | Journal of the American Chemical Society
Oct. 2008 - FLUORESCENT PROTEIN - Research Front Map - ScienceWatch.com
