Protein Kinase C Regulates Pleckstrin by Phosphorylation of Sites Adjacent to the N-terminal Pleckstrin Homology Domain
Open Access
- 1 October 1995
- journal article
- Published by Elsevier
- Vol. 270 (40) , 23317-23321
- https://doi.org/10.1074/jbc.270.40.23317
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy.Proceedings of the National Academy of Sciences, 1995
- Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynaminCell, 1994
- Three-dimensional solution structure of the pleckstrin homology domain from dynaminCurrent Biology, 1994
- Structure of the pleckstrin homology domain from β-spectrinNature, 1994
- Solution structure of a pleckstrin-homology domainNature, 1994
- The PH domain: a common piece in the structural pathcwork of signalling proteinsTrends in Biochemical Sciences, 1993
- Pleckstrin domain homologyNature, 1993
- A putative modular domain present in diverse signaling proteinsCell, 1993
- Identification of a Ten-Amino Acid Proline-Rich SH3 Binding SiteScience, 1993
- SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling ProteinsScience, 1991