The Pseudoactive Site of ILK Is Essential for Its Binding to α-Parvin and Localization to Focal Adhesions
- 1 December 2009
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 36 (5) , 819-830
- https://doi.org/10.1016/j.molcel.2009.11.028
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Spatial Coordination of Actin Polymerization and ILK–Akt2 Activity during Endothelial Cell MigrationDevelopmental Cell, 2009
- Structural Basis of Focal Adhesion Localization of LIM-only Adaptor PINCH by Integrin-linked KinaseJournal of Biological Chemistry, 2009
- Structure of the Pseudokinase VRK3 Reveals a Degraded Catalytic Site, a Highly Conserved Kinase Fold, and a Putative Regulatory Binding SitePublished by Elsevier ,2009
- The structural basis of integrin-linked kinase–PINCH interactionsProceedings of the National Academy of Sciences, 2008
- Structural Analysis of the Interactions Between Paxillin LD Motifs and α-ParvinStructure, 2008
- A helix scaffold for the assembly of active protein kinasesProceedings of the National Academy of Sciences, 2008
- The Structure of α-Parvin CH2-Paxillin LD1 Complex Reveals a Novel Modular Recognition for Focal Adhesion AssemblyJournal of Biological Chemistry, 2008
- CASK Functions as a Mg2+-Independent Neurexin KinaseCell, 2008
- Integrin-linked kinase: a cancer therapeutic target unique among its ILKNature Reviews Cancer, 2005
- Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRADThe EMBO Journal, 2003