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« Previous AbstractA conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission    Next AbstractDifferential regulation of transcription: repression by unactivated mitogen-activated protein kinase Kss1 requires the Dig1 and Dig2 proteins »

Trends Biochem Sci


Title:A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs
Author(s):Bardwell L; Thorner J;
Address:"Department of Molecular and Cell Biology, University of California, Berkeley 94720-3202, USA. jthorner@mendel.berkeley.edu"
Journal Title:Trends Biochem Sci
Year:1996
Volume:21
Issue:10
Page Number:373 - 374
DOI:
ISSN/ISBN:0968-0004 (Print) 0968-0004 (Linking)
Abstract:
Keywords:Amino Acid Sequence Calcium-Calmodulin-Dependent Protein Kinases/*metabolism Conserved Sequence/genetics Fungal Proteins/chemistry/metabolism Mitogen-Activated Protein Kinase Kinases Molecular Sequence Data Pheromones/metabolism Phosphorylation Protein Ki;
Notes:"MedlineBardwell, L Thorner, J eng GM15871/GM/NIGMS NIH HHS/ GM21841/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England 1996/10/01 Trends Biochem Sci. 1996 Oct; 21(10):373-4"

 
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