The Activating Dual Phosphorylation of MAPK by MEK Is Nonprocessive-Reference-Cited by-同舟云学术

The Activating Dual Phosphorylation of MAPK by MEK Is Nonprocessive

Published:1997-05-01 Issue:20 Volume:36 Page:5929-5933
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Burack W. Richard¹,Sturgill Thomas W.¹

Affiliation:

1. Departments of Pathology, Internal Medicine, and Pharmacology and Howard Hughes Medical Institute, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi970535d

Reference15 articles.

1. A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs

2. Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7

3. Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae

4. [22] Measuring activation of kinases in mitogen-activated protein kinase regulatory network

5. Ordered phosphorylation of p42mapkby MAP kinase kinase

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