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Dorota Garczarczyk

Researcher at Innsbruck Medical University

Publications -  8
Citations -  124

Dorota Garczarczyk is an academic researcher from Innsbruck Medical University. The author has contributed to research in topics: Protein kinase C & Phosphorylation. The author has an hindex of 5, co-authored 8 publications receiving 110 citations.

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Investigation of the marine compound spongistatin 1 links the inhibition of PKCα translocation to nonmitotic effects of tubulin antagonism in angiogenesis

TL;DR: It is concluded that PKCα might be an important target for the antiangiogenic effects of tubulin antagonism, and the data from the kinase array suggest that different tubulin antagonists might have individual intracellular actions.
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Signal transduction of constitutively active protein kinase C epsilon

TL;DR: Investigation of the effects of constitutively active rat PKCepsilon in HeLa cells in a doxycycline-inducible vector demonstrates that PKCEPsilon can induce distinctly different signaling from the Golgi and from the plasma membrane.
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Thienoquinolines as novel disruptors of the PKCε/RACK2 protein-protein interaction.

TL;DR: A pharmacophore model from the peptide EAVSLKPT is derived, a fragment of PKCε that inhibits the interaction ofPKCε and receptor for activated C-kinase 2 (RACK2) in vitro, leading to the discovery of a series of thienoquinolines that disrupt the interaction with RACK2 in vitro.
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Barbituric acid derivative BAS 02104951 inhibits PKCε, PKCη, PKCε/RACK2 interaction, Elk-1 phosphorylation in HeLa and PKCε and η translocation in PC3 cells following TPA-induction.

TL;DR: The small organic molecule BAS 02104951 can be used as selective inhibitor of PKCε in cells not expressing PKCη and may serve as a basis for the rational development of a selective inhibitors ofPKCε or PKC ε, or for an inhibitor of the PKCα/RACK2 interaction.
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Protein kinase Cγ in colon cancer cells: Expression, Thr514 phosphorylation and sensitivity to butyrate-mediated upregulation as related to the degree of differentiation

TL;DR: The presence of unphosphorylated PKCgamma in HT29 cells, and its complete absence in Caco2 cells demonstrates a cell type-dependent differential coupling of Thr(514)- phosphorylation with de novo synthesis of PKCGamma in colon cancer cells.