scholarly journals Demonstration of BACE ( -secretase) phosphorylation and its interaction with GGA1 in cells by fluorescence-lifetime imaging microscopy

2004 ◽  
Vol 117 (22) ◽  
pp. 5437-5445 ◽  
Author(s):  
C. A. F. von Arnim
Keyword(s):  
Fluorescence Lifetime ◽  
Fluorescence Lifetime Imaging Microscopy ◽  
Fluorescence Lifetime Imaging ◽  
Lifetime Imaging ◽  
In Cells

scholarly journals Monitoring conformational changes of proteins in cells by fluorescence lifetime imaging microscopy

2003 ◽  
Vol 373 (3) ◽  
pp. 999-999
Author(s):  
V. CALLEJA ◽  
S. M. AMEER-BEG ◽  
B. VOJNOVIC ◽  
R. WOSCHOLSKI ◽  
J. DOWNWARD ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Fluorescence Lifetime ◽  
Fluorescence Lifetime Imaging Microscopy ◽  
Fluorescence Lifetime Imaging ◽  
Lifetime Imaging ◽  
In Cells

scholarly journals Multiphoton fluorescence lifetime imaging microscopy (FLIM) and super-resolution fluorescence imaging with a supramolecular biopolymer for the controlled tagging of polysaccharides

Nanoscale ◽  
2019 ◽  
Vol 11 (19) ◽  
pp. 9498-9507 ◽  
Author(s):  
Haobo Ge ◽  
Fernando Cortezon-Tamarit ◽  
Hui-Chen Wang ◽  
Adam C. Sedgwick ◽  
Rory L. Arrowsmith ◽  
...  
Keyword(s):  
Fluorescence Imaging ◽  
Fluorescence Lifetime ◽  
Super Resolution ◽  
Fluorescence Lifetime Imaging Microscopy ◽  
Fluorescence Lifetime Imaging ◽  
Boronate Ester ◽  
Lifetime Imaging ◽  
In Cells

A new coumarin-appended boronate ester for fluorogenic imaging which binds polysaccharides in solution and in cells.

scholarly journals Binding of Small Molecules to G-quadruplex DNA in Cells Revealed by Fluorescence Lifetime Imaging Microscopy of o-BMVC Foci

Molecules ◽  
2018 ◽  
Vol 24 (1) ◽  
pp. 35 ◽  
Author(s):  
Ting-Yuan Tseng ◽  
I-Te Chu ◽  
Shang-Jyun Lin ◽  
Jie Li ◽  
Ta-Chau Chang
Keyword(s):  
Cancer Cells ◽  
Fluorescence Lifetime ◽  
Fluorescence Lifetime Imaging Microscopy ◽  
Dna Integrity ◽  
Fluorescence Lifetime Imaging ◽  
Quadruplex Dna ◽  
Lifetime Imaging ◽  
G Quadruplex ◽  
Direct Binding ◽  
In Cells

G-quadruplex (G4) structures have recently received increasing attention as a potential target for cancer research. We used time-gated fluorescence lifetime imaging microscopy (FLIM) with a G4 fluorescent probe, 3,6-bis(1-methyl-2-vinylpyridinium) carbazole diiodide (o-BMVC), to measure the number of o-BMVC foci, which may represent G4 foci, in cells as a common signature to distinguish cancer cells from normal cells. Here, the decrease in the number of o-BMVC foci in the pretreatment of cancer cells with TMPyP4, BRACO-19 and BMVC4 suggested that they directly bind to G4s in cells. In contrast, the increase in the number of o-BMVC foci in the pretreatment of cells with PDS and Hoechst 33258 (H33258) suggested that they do not inhabit the binding site of o-BMVC to G4s in cells. After the H33258 was removed, the gradual decrease of H33258-induced G4 foci may be due to DNA repair. The purpose of this work is to introduce o-BMVC foci as an indicator not only to verify the direct binding of potential G4 ligands to G4 structures but also to examine the possible effect of some DNA binding ligands on DNA integrity by monitoring the number of G4 foci in cells.

scholarly journals Photoswitching FRET to monitor protein–protein interactions

2018 ◽  
Vol 116 (3) ◽  
pp. 864-873 ◽  
Author(s):  
Kristin H. Rainey ◽  
George H. Patterson
Keyword(s):  
Fluorescence Lifetime ◽  
Protein Interactions ◽  
Fluorescent Protein ◽  
Fluorescence Lifetime Imaging Microscopy ◽  
Fluorescence Lifetime Imaging ◽  
Protein Protein Interactions ◽  
Lifetime Imaging ◽  
Powerful Approach ◽  
Fluorescent Molecules ◽  
In Cells

FRET is a powerful approach to study the interactions of fluorescent molecules, and numerous methods have been developed to measure FRET in cells. Here, we present a method based on a donor molecule’s photoswitching properties, which are slower in the presence vs. the absence of an acceptor. The technique, photoswitching FRET (psFRET), is similar to an established but underutilized method called photobleaching FRET (pbFRET), with the major difference being that the molecules are switched “off” rather than photobleached. The psFRET technique has some of the FRET imaging advantages normally attributed to fluorescence lifetime imaging microscopy (FLIM), such as monitoring only donor fluorescence. However, it can be performed on a conventional widefield microscope, requires less illumination light to photoswitch off than photobleaching, and can be photoswitched “on” again to repeat the experiment. We present data testing the validity of the psFRET approach to quantify FRET in cells and demonstrate its use in imaging protein–protein interactions and fluorescent protein-based biosensors.

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