Fluorescence quenching of graphene oxide combined with the site-specific cleavage of restriction endonuclease for deoxyribonucleic acid demethylase activity assay

2015 ◽  
Vol 869 ◽  
pp. 74-80 ◽  
Author(s):  
Lijuan Ji ◽  
Yingdan Qian ◽  
Ping Wu ◽  
Hui Zhang ◽  
Chenxin Cai
2014 ◽  
Vol 50 (73) ◽  
pp. 10691-10694 ◽  
Author(s):  
Lijuan Ji ◽  
Zhewei Cai ◽  
Yingdan Qian ◽  
Ping Wu ◽  
Hui Zhang ◽  
...  

A sensitive and selective approach for the DNA methyltransferase activity assay and MTase inhibitor screening is reported.


2016 ◽  
Vol 26 (1) ◽  
pp. 1-7 ◽  
Author(s):  
A.N. Kapitonov ◽  
G.N. Alexandrov ◽  
F.D. Vasileva ◽  
S.A. Smagulova ◽  
V.B. Timofeev ◽  
...  

2015 ◽  
Vol 23 (10) ◽  
pp. 878-884 ◽  
Author(s):  
Javad Gholami ◽  
Mehrdad Manteghian ◽  
Alireza Badiei ◽  
Mehran Javanbakht ◽  
Hiroshi Ueda

2003 ◽  
Vol 8 (1) ◽  
pp. 89-95 ◽  
Author(s):  
Birgit Heltweg ◽  
Manfred Jung

Histone deacetylases (HDACs) are important regulators of transcription, and their inhibitors are a promising class of anticancer agents. The methods for the determination of HDAC activity and its inhibition that are currently available suffer from various drawbacks, such as animal testing, radioactive substrates, or limited throughput. Therefore, a fast nonisotopic method for the measurement of HDAC activity is highly desirable. The authors present such an assay that relies on the fluorescent HDAC substrate developed previously in their group. After incubation of the substrate with the enzyme, a derivatization leads to efficient fluorescence quenching in the deacetylated metabolite. Thus, only the fluorescence emitted by the remaining substrate is detected, which allows for a convenient detection of HDAC activity in a homogeneous format that can be performed on multiwell plate readers. This procedure, called HDASH (histone deacetylase assay—homogeneous), should be a valuable tool in transcriptional research and especially drug discovery. ( Journal of Biomolecular Screening 2003:89-95)


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