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Harald Mischak

Researcher at University of Glasgow

Publications -  490
Citations -  29671

Harald Mischak is an academic researcher from University of Glasgow. The author has contributed to research in topics: Kidney disease & Protein kinase C. The author has an hindex of 90, co-authored 445 publications receiving 27472 citations. Previous affiliations of Harald Mischak include Ludwig Maximilian University of Munich & University of Copenhagen.

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Selective inhibition of protein kinase C isozymes by the indolocarbazole Gö 6976.

TL;DR: In vitro kinase assays indicated that interference with Ca2+ or its binding site is not responsible for the differential inhibition of PKC isozymes by Gö 6976, and Kinetic analysis revealed that PKC inhibition by Gö 7076 was competitive with respect to ATP, non-competitive withrespect to the protein substrate, and mixed type with respectto phosphatidylserine.
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Protein kinase C alpha activates RAF-1 by direct phosphorylation

TL;DR: The observation that Raf-1 and PKCα cooperate in the transformation of NIH3T3 cells is consistent with such a direct interaction, and the Ser499 phosphorylation site is necessary for this synergism.
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Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP

TL;DR: RKIP represents a new class of protein-kinase-inhibitor protein that regulates the activity of the Raf/MEK/ERK module and competitively disrupts the interaction between these kinases.
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CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation.

TL;DR: It is demonstrated that CpG‐DNA induces phosphorylation of Jun N‐terminal kinase kinase 1 (JNKK1/SEK/MKK4) and subsequent activation of the stress kinases JNK1/2 and p38 in murine macrophages and dendritic cells, and that cellular uptake via endocytosis and subsequent endosomal maturation is essential for signalling.
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Overexpression of protein kinase C-delta and -epsilon in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity.

TL;DR: The patterns of mRNA and protein expression of 7 protein kinase C (PKC) isozymes in NIH 3T3 cells are determined and high expression of PKC-epsilon contributes to neoplastic transformation.