Coumarin-Based Fluorogenic Probes for No-Wash Protein Labeling

2014 ◽  
Vol 53 (50) ◽  
pp. 13785-13788 ◽  
Author(s):  
Yingche Chen ◽  
Christopher M. Clouthier ◽  
Kelvin Tsao ◽  
Miroslava Strmiskova ◽  
Hugo Lachance ◽  
...  
2019 ◽  
Vol 24 (4) ◽  
pp. 443-455 ◽  
Author(s):  
Shahi Imam Reja ◽  
Masafumi Minoshima ◽  
Yuichiro Hori ◽  
Kazuya Kikuchi

2018 ◽  
Vol 54 (76) ◽  
pp. 10758-10761 ◽  
Author(s):  
Elodie Decuypère ◽  
Margaux Riomet ◽  
Antoine Sallustrau ◽  
Sarah Bregant ◽  
Robert Thai ◽  
...  

Sydnone-coumarin compounds are interesting turn-on fluorogenic probes for protein labeling.


2014 ◽  
Vol 126 (50) ◽  
pp. 14005-14008 ◽  
Author(s):  
Yingche Chen ◽  
Christopher M. Clouthier ◽  
Kelvin Tsao ◽  
Miroslava Strmiskova ◽  
Hugo Lachance ◽  
...  

2016 ◽  
Vol 14 (38) ◽  
pp. 9158-9158
Author(s):  
B. Söveges ◽  
T. Imre ◽  
T. Szende ◽  
Á. L. Póti ◽  
G. B. Cserép ◽  
...  

Correction for ‘A systematic study of protein labeling by fluorogenic probes using cysteine targeting vinyl sulfone-cyclooctyne tags’ by B. Söveges, et al., Org. Biomol. Chem., 2016, 14, 6071–6078.


2017 ◽  
Vol 28 (10) ◽  
pp. 1911-1915 ◽  
Author(s):  
Shuang Leng ◽  
Qing-Long Qiao ◽  
Yue Gao ◽  
Lu Miao ◽  
Wu-Guo Deng ◽  
...  

2019 ◽  
Vol 55 (31) ◽  
pp. 4582-4585 ◽  
Author(s):  
Lucie Plougastel ◽  
Manas R. Pattanayak ◽  
Margaux Riomet ◽  
Sarah Bregant ◽  
Antoine Sallustrau ◽  
...  

Fluorogenic sydnone-based turn-on probes allow efficient labeling of proteins and cell imaging through a bioorthogonal strained promoted sydnone–alkyne cycloaddition reaction.


2016 ◽  
Vol 14 (25) ◽  
pp. 6071-6078 ◽  
Author(s):  
B. Söveges ◽  
T. Imre ◽  
T. Szende ◽  
Á. L. Póti ◽  
G. B. Cserép ◽  
...  

Protein labeling by cycloocytynylated vinyl sulfone linkers is fast and thiol-selective, and subsequent click reaction with fluorogenic azides generates intensive fluorescence.


2012 ◽  
Vol 134 (3) ◽  
pp. 1623-1629 ◽  
Author(s):  
Shin Mizukami ◽  
Shuji Watanabe ◽  
Yuri Akimoto ◽  
Kazuya Kikuchi

Author(s):  
Margaret Hukee

Gold labeling of two antigens (double labeling) is often done on two section surfaces separated by section thickness. Whether labeling is done on both sides of the same section or on two parallel surfaces separated by section thickness (PSSST), comparable results are dependent on an equal number of epitopes being exposed at each surface. We propose a method to study protein labeling within the same field of proteins, by examining two directly adjacent surfaces that were split during sectioning. The number of labeling sites on adjacent surfaces (AS) were compared to sites on PSSST surfaces in individual bacteria.Since each bacteria needed to be recognizable in all three section surfaces, one-hole grids were used for labeling. One-hole grids require a supporting membrane and excessive handling during labeling often ruptures the membrane. To minimize handling, a labeling chamber was designed that is inexpensive, disposable, minimizes contamination, and uses a minimal amount of solution.


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