Exploring the prominent performance of CX-4945 derivatives as protein kinase CK2 inhibitors by a combined computational study

2014 ◽  
Vol 10 (5) ◽  
pp. 1196-1210 ◽  
Author(s):  
Xuwen Wang ◽  
Peichen Pan ◽  
Youyong Li ◽  
Dan Li ◽  
Tingjun Hou

Protein kinase CK2, also known as casein kinase II, is related to various cellular events and is a potential target for numerous cancers.

2011 ◽  
Vol 12 (10) ◽  
pp. 7004-7021 ◽  
Author(s):  
Hongbo Liu ◽  
Xia Wang ◽  
Jian Wang ◽  
Jinghui Wang ◽  
Yan Li ◽  
...  

RSC Advances ◽  
2015 ◽  
Vol 5 (1) ◽  
pp. 462-476 ◽  
Author(s):  
Min Lv ◽  
Shuying Ma ◽  
Yueli Tian ◽  
Xiaoyun Zhang ◽  
Honglin Zhai ◽  
...  

Binding conformation of flavone inhibitors to protein kinase CK2.


MedChemComm ◽  
2016 ◽  
Vol 7 (7) ◽  
pp. 1352-1355 ◽  
Author(s):  
Zong-liang Liu ◽  
Ren-mei Zhang ◽  
Qing-guo Meng ◽  
Xiao-chen Zhang ◽  
Yuan Sun

Protein kinase CK2 (CK2) serves as an attractive anticancer target. Herein new CK2 inhibitors with a 1,3-dioxo-2,3-dihydro-1H-indene core are reported.


1996 ◽  
Vol 74 (4) ◽  
pp. 541-547 ◽  
Author(s):  
David W. Litchfield ◽  
Elzbieta Slominski ◽  
Shawn Lewenza ◽  
Michael Narvey ◽  
Denis G. Bosc ◽  
...  

Protein kinase CK2, which was formerly known as casein kinase II, is a highly conserved protein serine/threonine kinase implicated in the control of cell proliferation through its phosphorylation of regulatory nuclear proteins. The enzyme consists of catalytic (α and (or) α′) subunits and β subunits that modulate the activity of the catalytic subunits. These subunits are arranged in homotetrameric (i.e., α2β2 or α′2β2) or heterotetrameric (i.e., αα′β2) complexes. We previously demonstrated using the yeast two-hybrid system that α (or α′) subunits can interact with β subunits but not other α (or α′) subunits. By comparison, β subunits can interact with α (or α′) and with β subunits, suggesting that the protein kinase CK2 holoenzyme forms because of the ability of p subunits to dimerize, bringing two heterodimers (αβ or α′β) into a tetrameric complex. In the present study, we used the yeast two-hybrid system to examine the domains of interactions between the α and β subunits of protein kinase CK2. These studies indicate that the ability of β to interact with α resides within the carboxy-terminal domain of β. By comparison, our studies suggest that individual domains of α are not sufficient for interactions with β.Key words: protein kinase CK2, casein kinase II, yeast two-hybrid system, subunit interaction, signal transduction.


Heliyon ◽  
2017 ◽  
Vol 3 (6) ◽  
pp. e00318 ◽  
Author(s):  
Melanie Bender ◽  
Lisa Schwind ◽  
David Grundmann ◽  
Monika Martin ◽  
Markus Klotz ◽  
...  

2012 ◽  
Vol 20 (7) ◽  
pp. 2282-2289 ◽  
Author(s):  
Claas Hundsdörfer ◽  
Hans-Jörg Hemmerling ◽  
Claudia Götz ◽  
Frank Totzke ◽  
Patrick Bednarski ◽  
...  

ChemBioChem ◽  
2007 ◽  
Vol 8 (1) ◽  
pp. 129-139 ◽  
Author(s):  
Mario A. Pagano ◽  
Giorgia Poletto ◽  
Giovanni Di Maira ◽  
Giorgio Cozza ◽  
Maria Ruzzene ◽  
...  

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