Two Rate-Limiting Steps in the Kinetic Mechanism of the Serine/Threonine Specific Protein Kinase ERK2: A Case of Fast Phosphorylation Followed by Fast Product Release
- 30 September 2003
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 42 (42) , 12273-12286
- https://doi.org/10.1021/bi0348617
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Physiological Concentrations of Divalent Magnesium Ion Activate the Serine/Threonine Specific Protein Kinase ERK2Biochemistry, 2003
- Crystal Structures of MAP Kinase p38 Complexed to the Docking Sites on Its Nuclear Substrate MEF2A and Activator MKK3bMolecular Cell, 2002
- Specificity Determinants in MAPK Signaling to Transcription FactorsJournal of Biological Chemistry, 2002
- Evidence for Existence of a Nuclear Pore Complex-mediated, Cytosol-independent Pathway of Nuclear Translocation of ERK MAP Kinase in Permeabilized CellsJournal of Biological Chemistry, 2001
- Docking Sites on Substrate Proteins Direct Extracellular Signal-regulated Kinase to Phosphorylate Specific ResiduesJournal of Biological Chemistry, 2001
- Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactionsThe EMBO Journal, 2001
- Selective Targeting of MAPKs to the ETS Domain Transcription Factor SAP-1Journal of Biological Chemistry, 2001
- Kinetic Basis for Activation of CDK2/Cyclin A by PhosphorylationJournal of Biological Chemistry, 2001
- Crystallization and Preliminary X-ray Studies of Extracellular Signal-regulated Kinase-2/MAP Kinase with an Incorporated His-tagJournal of Molecular Biology, 1993
- The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic DomainsScience, 1988