Molecular and Biochemical Characterization of the Skp2-Cks1 Binding Interface
Open Access
- 1 December 2004
- journal article
- Published by Elsevier
- Vol. 279 (49), 51362-51369
- https://doi.org/10.1074/jbc.m405944200
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Negative regulation of SCFSkp2 ubiquitin ligase by TGF-β signalingOncogene, 2003
- A Negatively Charged Amino Acid in Skp2 Is Required for Skp2-Cks1 Interaction and Ubiquitination of p27Kip1Published by Elsevier ,2003
- Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligaseBiochemical Journal, 2003
- Three Different Binding Sites of Cks1 Are Required for p27-Ubiquitin LigationJournal of Biological Chemistry, 2002
- Phosphorylation-Dependent Ubiquitination of Cyclin E by the SCF Fbw7 Ubiquitin LigaseScience, 2001
- A splice variant of Skp2 is retained in the cytoplasm and fails to direct cyclin D1 ubiquitination in the uterine cancer cell line SK-UTOncogene, 2001
- F-Box Protein Grr1 Interacts with Phosphorylated Targets via the Cationic Surface of Its Leucine-Rich RepeatMolecular and Cellular Biology, 2001
- A CDK-Independent Function of Mammalian Cks1Molecular Cell, 2001
- Transforming growth factor β-induced phosphorylation of Smad3 is required for growth inhibition and transcriptional induction in epithelial cellsProceedings of the National Academy of Sciences, 1997
- Expression of cell-cycle regulators p27Kip1 and cyclin E, alone and in combination, correlate with survival in young breast cancer patientsNature Medicine, 1997