The Protein Kinase C Inhibitor Bisindolyl Maleimide 2 Binds with Reversed Orientations to Different Conformations of Protein Kinase A
Open Access
- 1 May 2004
- journal article
- Published by Elsevier
- Vol. 279 (22) , 23679-23690
- https://doi.org/10.1074/jbc.m314082200
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Mutants of Protein Kinase A that Mimic the ATP-binding Site of Protein Kinase B (AKT)Published by Elsevier ,2003
- Crystal structure of an activated Akt/Protein Kinase B ternary complex with GSK3-peptide and AMP-PNPNature Structural & Molecular Biology, 2002
- Structural aspects of protein kinase control—role of conformational flexibilityPharmacology & Therapeutics, 2002
- Evidence for an internal entropy contribution to phosphoryl transfer: a study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-dependent protein kinaseJournal of Molecular Biology, 2002
- Crystal Structure of the Potent Natural Product Inhibitor Balanol in Complex with the Catalytic Subunit of cAMP-Dependent Protein KinaseBiochemistry, 1999
- Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine 1 1Edited by I. A. WilsonJournal of Molecular Biology, 1999
- A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibilityStructure, 1997
- The glycine-rich sequence of protein kinases: a multifunctional elementTrends in Biochemical Sciences, 1994
- Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptideBiochemistry, 1993
- Potent selective inhibitors of protein kinase CFEBS Letters, 1989