Abstract
Calyculin A (1), isolated from the marine sponge Discodermia calyx, exhibits potent inhibitory activity against protein phosphatases PP1 and 2A. These enzymes are ubiquitously expressed in eukaryotes and catalyze the dephosphorylation of phosphorylated Ser/Thr residue. Considering the essential roles of PP1/2A in many aspects of cellular functions, fluorescence probe specific to these enzymes would be significant, but has not been reported so far. Therefore we launched a study to develop a fluorescence probe based on the specific inhibitor, 1.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
