High-Resolution Structure of the Pleckstrin Homology Domain of Protein Kinase B/Akt Bound to Phosphatidylinositol (3,4,5)-Trisphosphate
- 1 July 2002
- journal article
- research article
- Published by Elsevier in Current Biology
- Vol. 12 (14) , 1256-1262
- https://doi.org/10.1016/s0960-9822(02)00972-7
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Identification of ARAP3, a Novel PI3K Effector Regulating Both Arf and Rho GTPases, by Selective Capture on Phosphoinositide Affinity MatricesMolecular Cell, 2002
- The High Resolution Crystal Structure of Recombinant Crithidia fasciculata Tryparedoxin-IJournal of Biological Chemistry, 1999
- Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell–matrix and cell–cell interactionCurrent Biology, 1999
- Automated MAD and MIR structure solutionActa Crystallographica Section D-Biological Crystallography, 1999
- Akt activation by growth factors is a multiple-step process: the role of the PH domainOncogene, 1998
- Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin 1 1Edited by P. E. WrightJournal of Molecular Biology, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- X‐Linked Agammaglobulinemia and Other Immunoglobulin DeficienciesImmunological Reviews, 1994
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- WHAT IF: A molecular modeling and drug design programJournal of Molecular Graphics, 1990