Enzyme kinetics and distinct modulation of the protein kinase N family of kinases by lipid activators and small molecule inhibitors
Author:
Affiliation:
1. Pfizer Oncology Research Unit, Pfizer Inc., San Diego, CA 92121, U.S.A.
2. Pfizer Worldwide Medicinal Chemistry, Pfizer Inc., San Diego, CA 92121, U.S.A.
3. Pfizer Oncology Research Unit, Pfizer Inc., Pearl River, NY 10965, U.S.A.
Abstract
Publisher
Portland Press Ltd.
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Link
https://portlandpress.com/bioscirep/article-pdf/doi/10.1042/BSR20140010/475455/bsr034e097.pdf
Reference61 articles.
1. The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC;Mukai;J. Biochem.,2003
2. Regulation of the interaction between protein kinase C-related protein kinase 2 (PRK2) and its upstream kinase, 3–phosphoinositide-dependent protein kinase 1 (PDK1);Dettori;J. Biol. Chem.,2009
3. The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB;Biondi;EMBO J.,2001
4. Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif;Flynn;J. Biol. Chem.,1998
5. Characterization of the interaction between RhoA and the amino-terminal region of PKN;Shibata;FEBS Lett.,1996
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