Structural pliability adjacent to the kinase domain highlights contribution of FAK1 IDRs to cytoskeletal remodeling
Open Access
- 5 October 2016
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Vol. 1865 (1) , 43-54
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Evolution and disorderCurrent Opinion in Structural Biology, 2011
- Intrinsically disordered proteins are potential drug targetsCurrent Opinion in Chemical Biology, 2010
- Ancient origin of the integrin-mediated adhesion and signaling machineryProceedings of the National Academy of Sciences, 2010
- A Small Molecule Inhibitor, 1,2,4,5-Benzenetetraamine Tetrahydrochloride, Targeting the Y397 Site of Focal Adhesion Kinase Decreases Tumor GrowthJournal of Medicinal Chemistry, 2008
- Activation of tyrosine kinases by mutation of the gatekeeper threonineNature Structural & Molecular Biology, 2008
- Intrinsic disorder in scaffold proteins: Getting more from lessProgress in Biophysics and Molecular Biology, 2008
- Recent developments in the MAFFT multiple sequence alignment programBriefings in Bioinformatics, 2008
- The role of disorder in interaction networks: a structural analysisMolecular Systems Biology, 2008
- Structural Basis for the Autoinhibition of Focal Adhesion KinaseCell, 2007
- Focal adhesion kinase: in command and control of cell motilityNature Reviews Molecular Cell Biology, 2005