Regulation of CK2 by phosphorylation and O-GlcNAcylation revealed by semisynthesis-Reference-Cited by-同舟云学术

Regulation of CK2 by phosphorylation and O-GlcNAcylation revealed by semisynthesis

Published:2012-01-22 Issue:3 Volume:8 Page:262-269
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Tarrant Mary Katherine,Rho Hee-Sool,Xie Zhi,Jiang Yu Lin,Gross Christopher,Culhane Jeffrey C,Yan Gai,Qian Jiang,Ichikawa Yoshitaka,Matsuoka Tatsuji,Zachara Natasha,Etzkorn Felicia A,Hart Gerald W,Jeong Jun Seop,Blackshaw Seth,Zhu Heng,Cole Philip A

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nchembio.771.pdf

Reference50 articles.

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2. Pinna, L.A. Protein kinase CK2: a challenge to canons. J. Cell Sci. 115, 3873–3878 (2002).

3. Salvi, M., Sarno, S., Cesaro, L., Nakamura, H. & Pinna, L.A. Extraordinary pleiotropy of protein kinase CK2 revealed by weblogo phosphoproteome analysis. Biochim. Biophys. Acta 1793, 847–859 (2009).

4. Niefind, K., Guerra, B., Ermakowa, I. & Issinger, O.G. Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J. 20, 5320–5331 (2001).

5. Sarno, S. et al. Cooperative modulation of protein kinase CK2 by separate domains of its regulatory beta-subunit. Biochemistry 39, 12324–12329 (2000).

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