The Helically Extended SH3 Domain of the T Cell Adaptor Protein ADAP is a Novel Lipid Interaction Domain
- 1 May 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 348 (4) , 1025-1035
- https://doi.org/10.1016/j.jmb.2005.02.069
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Structure of a Helically Extended SH3 Domain of the T Cell Adapter Protein ADAPStructure, 2004
- Dynamics of Phosphoinositides in Membrane Retrieval and InsertionAnnual Review of Physiology, 2003
- Imaging antigen-induced PI3K activation in T cellsNature Immunology, 2002
- Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapseNature Immunology, 2002
- Coupling of the TCR to Integrin Activation by SLAP-130/FybScience, 2001
- Conformation, Localization, and Integrin Binding of Talin Depend on Its Interaction with PhosphoinositidesJournal of Biological Chemistry, 2001
- A Deubiquitinating Enzyme UBPY Interacts with the Src Homology 3 Domain of Hrs-binding Protein via a Novel Binding Motif PX(V/I)(D/N)RXXKPJournal of Biological Chemistry, 2000
- Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteinsBiochemistry, 1993
- Identification of a Ten-Amino Acid Proline-Rich SH3 Binding SiteScience, 1993
- A novel viral oncogene with structural similarity to phospholipase CNature, 1988