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Protein phosphatase 1--targeted in many directions.
  • P. Cohen
  • Biology, Medicine
  • Journal of cell science
  • 15 January 2002
Understanding of the mode of action of PP1C complexes may facilitate development of drugs that target particular PP1c complexes and thereby modulate the phosphorylation state of a very limited subset of proteins. Expand
MAPKAP kinase‐2; a novel protein kinase activated by mitogen‐activated protein kinase.
  • D. Stokoe, D.G. Campbell, +4 authors P. Cohen
  • Biology, Medicine
  • The EMBO journal
  • 1 November 1992
Results indicate that MAP kinase activates at least two distinct protein kinases, suggesting that it represents a point at which the growth factor‐stimulated protein kinase cascade bifurcates. Expand
The cyanobacterial toxin microcystin binds covalently to cysteine‐273 on protein phosphatase 1
It is demonstrated that Cys273 of PP1 binds covalently to the methyl‐dehydroalanine (Mdha) residue of the toxin, which explains the failure to detect this toxin post‐mortem in suspected cases of MC poisoning. Expand
Protein phosphatases come of age.
  • P. Cohen, P. Cohen
  • Biology, Medicine
  • The Journal of biological chemistry
  • 25 December 1989
This Minireview will concentrate on recent progress that has demonstrated key roles for these enzymes in tumor suppression and in cell division and identified novel phosphatase catalytic subunits. Expand
One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis
Results show that PP1 activity is required for mitotic progression and that the other loci cannot supply sufficient activity to complement loss of expression of the PP1 87B gene. Expand
PPP1R6, a novel member of the family of glycogen‐targetting subunits of protein phosphatase 1
The PPP1R6 is associated with glycogen in muscle but is not subject to the same modes of covalent and allosteric regulation as GM and GL. Expand
The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2.
The substrate specificity of mitogen-activated protein (MAP) kinase-activated protein kinase-2 (MAPKAP kinase-2) was investigated by using synthetic peptides related to the N-terminus of glycogenExpand
Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme.
The results suggest that inhibitor-2 is critical for the correct folding of nascent PP1C polypeptides, that its function is similar to that of a molecular chaperone and that it acts as a cytosolic reservoir of PP 1C molecules which can be directed to the required subcellular locations following the synthesis of specific targetting subunits. Expand
A common variant in PPP1R3 associated with insulin resistance and type 2 diabetes.
A novel substitution at codon 883 and common variant of an "ATTTA" element in the 3'-untranslated region (UTR) of the corresponding gene (PPP1R3) may contribute to the higher prevalence of type 2 diabetes in this Native American population. Expand
A novel glycogen‐targeting subunit of protein phosphatase 1 that is regulated by insulin and shows differential tissue distribution in humans and rodents
It is shown here that the mammalian gene PPP1R3E encodes a novel glycogen‐targeting subunit of PP1 that is expressed in rodent liver that is downregulated in the livers of diabetic rodents and restored by insulin treatment. Expand