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Characterization of the reversible phosphorylation and activation of ERK8
Iva V. Klevernic
, Margaret J. Stafford
, Nicholas Morrice
, Mark Peggie
, Simon Morton
, Philip Cohen
Research output
:
Contribution to journal
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Article
›
peer-review
55
Scopus citations
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Keyphrases
Extracellular Regulated Protein Kinases
100%
Reversible Phosphorylation
100%
Reversible Deactivation
100%
HEK293 Cells
28%
Hydrogen Peroxide
21%
Dephosphorylation
21%
Serine/threonine Protein Phosphatase
21%
ERK2
14%
Insect Cells
14%
Incubation
7%
Growth Factors
7%
Phosphorylation
7%
Autophosphorylation
7%
Protein Phosphatase 2A (PP2A)
7%
Potent Inhibitor
7%
Epidermal Growth Factor
7%
Escherichia Coli
7%
ERK1
7%
Tyrosine Residue
7%
Insulin-like
7%
Okadaic Acid
7%
Relative Rate
7%
Protein Phosphatase Inhibitors
7%
Threonine
7%
Decreased Activity
7%
Protein Tyrosine Phosphatase 1B (PTP1B)
7%
Phosphatase 2A
7%
Myelin Basic Protein
7%
Anisomycin
7%
Osmotic Shock
7%
Phosphatase Inhibitors
7%
Escherichia Coli Cells
7%
Bacteria Cell
7%
Proline-directed Kinase
7%
PPP Family
7%
Biochemistry, Genetics and Molecular Biology
Protein Kinases
100%
HEK 293 Cells
26%
Hydrogen Peroxide
20%
Dephosphorylation
20%
Protein Serine/Threonine Phosphatase
20%
Escherichia coli
13%
Enzyme
6%
Phosphoprotein Phosphatase
6%
Wild Type
6%
Insulin-Like Growth Factor 1
6%
Epidermal Growth Factor
6%
Tyrosine
6%
Autophosphorylation
6%
Phosphorylated Protein
6%
Protein Tyrosine Phosphatase
6%
Myelin Basic Protein
6%
Osmotic Stress
6%
Anisomycin
6%
Threonine
6%
Proline
6%