Title : Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase.

Pub. Date : 1995 Mar 31

PMID : 7535768






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 ERK is activated by its upstream activator, MEK, via threonine and tyrosine phosphorylation. Threonine mitogen-activated protein kinase 1 Mus musculus
2 ERK is activated by its upstream activator, MEK, via threonine and tyrosine phosphorylation. Tyrosine mitogen-activated protein kinase 1 Mus musculus
3 Recombinant HVH2 phosphatase exhibited a high substrate specificity toward activated ERK and dephosphorylated both threonine and tyrosine residues of activated ERK1 and ERK2. Threonine mitogen-activated protein kinase 1 Mus musculus
4 Recombinant HVH2 phosphatase exhibited a high substrate specificity toward activated ERK and dephosphorylated both threonine and tyrosine residues of activated ERK1 and ERK2. Threonine mitogen-activated protein kinase 1 Mus musculus
5 Recombinant HVH2 phosphatase exhibited a high substrate specificity toward activated ERK and dephosphorylated both threonine and tyrosine residues of activated ERK1 and ERK2. Tyrosine mitogen-activated protein kinase 1 Mus musculus
6 Recombinant HVH2 phosphatase exhibited a high substrate specificity toward activated ERK and dephosphorylated both threonine and tyrosine residues of activated ERK1 and ERK2. Tyrosine mitogen-activated protein kinase 1 Mus musculus