A substrate for deubiquitinating enzymes based on time-resolved fluorescence resonance energy transfer between terbium and yellow fluorescent protein

2007 ◽  
Vol 360 (1) ◽  
pp. 138-143 ◽  
Author(s):  
Robert A. Horton ◽  
Elizabeth A. Strachan ◽  
Kurt W. Vogel ◽  
Steven M. Riddle
Biochemistry ◽  
2005 ◽  
Vol 44 (11) ◽  
pp. 4312-4321 ◽  
Author(s):  
Olivier Dalmas ◽  
Marie-Ange Do Cao ◽  
Miguel R. Lugo ◽  
Frances J. Sharom ◽  
Attilio Di Pietro ◽  
...  

2007 ◽  
Vol 5 (3) ◽  
pp. 363-372 ◽  
Author(s):  
Pierre-Eloi Imbert ◽  
Vincent Unterreiner ◽  
Daniela Siebert ◽  
Hanspeter Gubler ◽  
Christian Parker ◽  
...  

2020 ◽  
Vol 10 (10) ◽  
pp. 3508
Author(s):  
Haijun Yu ◽  
Haoxiang Li ◽  
Yao Zhou ◽  
Shengmin Zhou ◽  
Ping Wang

In this paper, a fluorescence resonance energy transfer (FRET)-based sensor for ultra-sensitive detection of H2O2 was developed by utilizing the unique enzymatic properties of peroxiredoxin (Prx) to H2O2. Cyan and yellow fluorescent protein (CFP and YFP) were fused to Prx and mutant thioredoxin (mTrx), respectively. In the presence of H2O2, Prx was oxidized into covalent homodimer through disulfide bonds, which were further reduced by mTrx to form a stable mixed disulfide bond intermediate between CFP-Prx and mTrx-YFP, inducing FRET. A linear quantification range of 10–320 nM was obtained according to the applied protein concentrations and the detection limit (LOD) was determined to be as low as 4 nM. By the assistance of glucose oxidase to transform glucose into H2O2, the CFP-Prx/mTrx-YFP system (CPmTY) was further exploited for the detection of glucose in real sample with good performance, suggesting this CPmTY protein sensor is highly practical.


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