CDKN3 is a member of the dual specificity protein phosphatase family that acts as a cyclin-dependent kinase inhibitor. CDKN3 has been shown to interact with and dephosphorylate specifically the CDK2 kinase thereby preventing it′s activation. CDKN3 has been reported to be deleted, mutated, or overexpressed in several kinds of cancers. Increased expression of CDKN3 leads to increased levels of kinase-associated phosphatase activity that inhibits the G(1)/S transition of the cell cycle by dephosphorylating the cyclin-dependent kinases.
Journal of neurochemistry, 89(5), 1252-1259 (2004-05-19)
Choline is an important methyl donor and a component of membrane phospholipids. In this study, we tested the hypothesis that choline availability can modulate cell proliferation and the methylation of genes that regulate cell cycling. In several other model systems
Biochemical and biophysical research communications, 305(2), 311-314 (2003-05-15)
The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual-specificity protein phosphatase that dephosphorylates Cdk2 on a conserved threonine residue, T160, in a cyclin dependent manner. Several aberrant KAP transcripts with characteristic deletion regions have been identified in hepatocellular
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