A Bipartite Mechanism for ERK2 Recognition by Its Cognate Regulators and Substrates
Open Access
- 1 August 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (32) , 29901-29912
- https://doi.org/10.1074/jbc.m303909200
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- The Specificity of Extracellular Signal-regulated Kinase 2 Dephosphorylation by Protein PhosphatasesJournal of Biological Chemistry, 2002
- Modular Structure of a Docking Surface on MAPK PhosphatasesPublished by Elsevier ,2002
- The Mechanism of Dephosphorylation of Extracellular Signal-regulated Kinase 2 by Mitogen-activated Protein Kinase Phosphatase 3Published by Elsevier ,2001
- MAP KinasesChemical Reviews, 2001
- Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactionsThe EMBO Journal, 2001
- A conserved docking motif in MAP kinases common to substrates, activators and regulatorsNature Cell Biology, 2000
- Mechanism of Mitogen-activated Protein Kinase Phosphatase-3 Activation by ERK2Published by Elsevier ,1999
- Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to HumanPhysiological Reviews, 1999
- Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase).The EMBO Journal, 1991
- Multiple components in an epidermal growth factor-stimulated protein kinase cascadeJournal of Biological Chemistry, 1991