Multi-site phosphorylation of pho4 by the cyclin-CDK pho80-pho85 is semi-processive with site preference
- 9 March 2001
- journal article
- research article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 306 (5), 997-1010
- https://doi.org/10.1006/jmbi.2000.4417
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The Effects of Changing the Site of Activating Phosphorylation in CDK2 from Threonine to SerinePublished by Elsevier BV ,2000
- Mechanism of Cdk2/Cyclin E Inhibition by p27 and p27 PhosphorylationBiochemistry, 1999
- Purification, Characterization, and Kinetic Mechanism of Cyclin D1·CDK4, a Major Target for Cell Cycle RegulationJournal of Biological Chemistry, 1998
- The Activating Dual Phosphorylation of MAPK by MEK Is NonprocessiveBiochemistry, 1997
- The phosphatase system in Saccharomyces cerevisiae.Genes & Genetic Systems, 1997
- Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinasesCurrent Biology, 1995
- Use of an oriented peptide library to determine the optimal substrates of protein kinasesCurrent Biology, 1994
- Phosphate-Regulated Inactivation of the Kinase PHO80-PHO85 by the CDK Inhibitor PHO81Science, 1994
- Phosphorylation of the Transcription Factor PHO4 by a Cyclin-CDK Complex, PHO80-PHO85Science, 1994
- Ordered phosphorylation of p42mapk by MAP kinase kinaseFEBS Letters, 1992