Walter Antonio Schlapkohl

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Protein kinase C, a multigene family of phospholipid-dependent and diacylglycerol-activated Ser/Thr protein kinases, is a key component in many signal transduction pathways. The kinase activity was thought to be essential for a plethora of biological processes attributed to these enzymes. Here we show that at least one protein kinase C function, the(More)
The catalytic domain of overexpressed protein kinase C (PKC)-delta mediates phorbol 12-myristate 13-acetate (PMA)-induced differentiation or apoptosis in appropriate model cell lines. To define the portions of the catalytic domain that are critical for these isozyme-specific functions, we constructed reciprocal chimeras, PKC-delta/epsilonV5 and(More)
A recently developed strategy capable of measuring the equilibrium dissociation constant for thrombin-fibrinogen interaction has been used to explore the pH dependence of the interaction and the effects of thrombin conformational transitions. The dependence of fibrinogen binding to thrombin in the pH range 6-10 is bell-shaped and remarkably similar to that(More)
Title of Dissertation: NOVEL-TYPE PROTEIN KINASE C ISOFORMSPECIFIC FUNCTION, KINASE ACTIVITY, AND PHOSPHORYLATION STATUS ARE DISRUPTED BY V5 DOMAIN MUTATIONS Walter Antonio Schlapkohl, Doctor of Philosophy, 2005 Dissertation directed by: Professor J. Frederic Mushinski Molecular and Cell Biology Program The Protein Kinase C (PKC) family consists of at least(More)
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