All Outputs (2)

Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. (2007)
Journal Article
Lin, Y., Stevens, C., & Hupp, T. (2007). Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. Journal of Biological Chemistry, 282(23), 16792-16802. https://doi.org/10.107

DAPK-1 is a stress-activated tumor suppressor protein that plays a role in both proapoptotic or antiapoptotic signal transduction pathways. To define mechanisms of DAPK-1 protein regulation, we have determined that DAPK-1 protein has a long half-life... Read More about Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis..

A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis (2007)
Journal Article
Stevens, C., Lin, Y., Sanchez, M., Amin, E., Copson, E., White, H., …Hupp, T. (2007). A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis. Journal of Biological Chemistry, 282(18), 13791-13803. https://doi.org/10.1074/jb

p53 is activated genetically by a set of kinases that are components of the calcium calmodulin kinase superfamily, including CHK2, AMP kinase, and DAPK-1. In dissecting the mechanism of DAPK-1 control, a novel mutation (N1347S) was identified in the... Read More about A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis.