Alternative Splicing Determines the Domain Structure of WWP1, a Nedd4 Family Protein
- 11 January 2002
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 290 (1) , 431-437
- https://doi.org/10.1006/bbrc.2001.6206
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- A New Ticket for Entry into Budding Vesicles—UbiquitinCell, 2001
- Converging on proline: the mechanism of WW domain peptide recognition.Nature Structural & Molecular Biology, 2000
- Regulation of the epithelial Na+ channel by Nedd4 and ubiquitinationKidney International, 2000
- Nedd4-like proteins: an emerging family of ubiquitin-protein ligases implicated in diverse cellular functionsTrends in Cell Biology, 1999
- Nitrogen-regulated Ubiquitination of the Gap1 Permease ofSaccharomyces cerevisiaeMolecular Biology of the Cell, 1998
- The C2 Domain of the Ubiquitin Protein Ligase Nedd4 Mediates Ca2+-dependent Plasma Membrane LocalizationJournal of Biological Chemistry, 1997
- Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npi1/rsp5 and ubiquitin-hydrolase npi2/doa4FEMS Microbiology Letters, 1997
- The C2 domain calcium‐binding motif: Structural and functional diversityProtein Science, 1996
- NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin—protein ligaseMolecular Microbiology, 1995
- A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase.Proceedings of the National Academy of Sciences, 1995