Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1-Reference-Cited by-同舟云学术

Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1

Published:2009-08-30 Issue:10 Volume:5 Page:758-764
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Hindie Valerie,Stroba Adriana,Zhang Hua,Lopez-Garcia Laura A,Idrissova Leila,Zeuzem Stefan,Hirschberg Daniel,Schaeffer Francis,Jørgensen Thomas J D,Engel Matthias,Alzari Pedro M,Biondi Ricardo M

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nchembio.208.pdf

Reference38 articles.

1. Olsen, J.V. et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635–648 (2006).

2. Johnson, L.N. & Lewis, R.J. Structural basis for control by phosphorylation. Chem. Rev. 101, 2209–2242 (2001).

3. Pawson, T. & Scott, J.D. Protein phosphorylation in signaling–50 years and counting. Trends Biochem. Sci. 30, 286–290 (2005).

4. Huse, M. & Kuriyan, J. The conformational plasticity of protein kinases. Cell 109, 275–282 (2002).

5. Pearl, L.H. & Barford, D. Regulation of protein kinases in insulin, growth factor and Wnt signalling. Curr. Opin. Struct. Biol. 12, 761–767 (2002).

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