enzymatic phosphorylation
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2020 ◽  
Vol 11 (4) ◽  
pp. 1132-1139
Author(s):  
Dongdong Liu ◽  
Zhe Miao ◽  
Chengling Wu ◽  
Fangfei He ◽  
Peng Ren ◽  
...  

A nonapeptide grafted LCST polymer undergoes enzymatic phosphorylation to assemble, which selectively disrupts PKA overexpressing cancer cells via kinetics targeting.



ChemBioChem ◽  
2019 ◽  
Vol 20 (15) ◽  
pp. 1945-1952 ◽  
Author(s):  
Yutaro Oda ◽  
Junya Chiba ◽  
Fumihiro Kurosaki ◽  
Yusuke Yamade ◽  
Masahiko Inouye


2019 ◽  
Vol 10 (14) ◽  
pp. 3937-3942 ◽  
Author(s):  
Zuzana Vaníková ◽  
Martina Janoušková ◽  
Milada Kambová ◽  
Libor Krásný ◽  
Michal Hocek

Biomimetic switching of in vitro transcription was developed by photochemical deprotection of photocaged 5hmU or 5hmC in template DNA (ON) and by enzymatic phosphorylation (OFF).



2018 ◽  
Vol 115 (12) ◽  
pp. 2327-2335 ◽  
Author(s):  
Yimin Qiu ◽  
Erik Poppleton ◽  
Arya Mekkat ◽  
Hongtao Yu ◽  
Sourav Banerjee ◽  
...  


Author(s):  
Daniela Ubiali ◽  
Giovanna Speranza


Author(s):  
Nileeka Balasuriya ◽  
McShane McKenna ◽  
Xuguang Liu ◽  
Shawn S. C. Li ◽  
Patrick O'Donoghue

Akt1 is a proto-oncogene that is over active in most cancers. Akt1 activation requires phosphorylation at Thr308; phosphorylation at Ser473 further enhances catalytic activity. Akt1 activity is also regulated via interactions between the kinase domain and the N-terminal auto-inhibitory pleckstrin homology (PH) domain. As it was previously difficult to produce Akt1 in site-specifically phosphorylated forms, the contribution of each activating phosphorylation site to auto-inhibition was unknown. Using a combination of genetic code expansion and in vivo enzymatic phosphorylation, we produced Akt1 variants containing programmed phosphorylation to probe the interplay between Akt1 phosphorylation status and the auto-inhibitory function of the PH domain. Deletion of the PH domain increased the enzyme activity for all three phosphorylated Akt1 variants. For the doubly phosphorylated enzyme, deletion of the PH domain relieved auto-inhibition by 295-fold. We next found that phosphorylation at Ser473 provided resistance to chemical inhibition by Akti-1/2 inhibitor VIII. The Akti-1/2 inhibitor was most effective against pAkt1T308 and showed 4-fold decreased potency with Akt1 variants phosphorylated at Ser473. The data highlight the need to design more potent Akt1 inhibitors that are effective against the doubly phosphorylated and most pathogenic form of Akt1.



2018 ◽  
Vol 865 ◽  
pp. 166-172 ◽  
Author(s):  
Magdalena Białek-Pietras ◽  
Agnieszka B. Olejniczak ◽  
Edyta Paradowska ◽  
Mirosława Studzińska ◽  
Agnieszka Jabłońska ◽  
...  


Author(s):  
S. Ahmadi ◽  
S. Ahmad ◽  
H.-B. Kraatz




2017 ◽  
Vol 53 (92) ◽  
pp. 12398-12401 ◽  
Author(s):  
M. J. Moure ◽  
Y. Zhuo ◽  
G. J. Boons ◽  
J. H. Prestegard

Synthesis of perdeuterated and 13C enriched myo-inositol facilitates NMR observation.



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