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Christopher Gerner

Researcher at University of Vienna

Publications -  232
Citations -  7198

Christopher Gerner is an academic researcher from University of Vienna. The author has contributed to research in topics: Proteome & Proteomics. The author has an hindex of 41, co-authored 204 publications receiving 5890 citations. Previous affiliations of Christopher Gerner include Medical University of Vienna & Institute of Cancer Research.

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RNase P without RNA: Identification and Functional Reconstitution of the Human Mitochondrial tRNA Processing Enzyme

TL;DR: It is demonstrated that human mitochondrial RNase P is a protein enzyme that does not require a trans-acting RNA component for catalysis, and the mitochondrial enzyme turns out to be an unexpected type of patchwork enzyme, composed of a tRNA methyltransferase, a short-chain dehydrogenase/reductase-family member, and a protein of hitherto unknown functional and evolutionary origin.
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Executioner caspase-3 and caspase-7 are functionally distinct proteases

TL;DR: The observations provide a molecular basis for the different phenotypes seen in mice lacking either caspase and indicate that these proteases occupy nonredundant roles within the cell death machinery.
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Structure–activity relationships for ruthenium and osmium anticancer agents – towards clinical development

TL;DR: Global structure-activity relationships are discussed for ruthenium and osmium metallodrugs with respect to in vitro antiproliferative/cytotoxic activity and in vivo tumor-inhibiting properties, as well as pharmacokinetics.
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Serum Amyloid A in Uremic HDL Promotes Inflammation

TL;DR: It is observed that HDL isolated from healthy individuals inhibited the production of inflammatory cytokines by peripheral monocytes stimulated with a Toll-like receptor 2 agonist, suggesting a potential link between the high levels of inflammation and cardiovascular mortality in uremia.
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The Fas-induced apoptosis analyzed by high throughput proteome analysis.

TL;DR: F Fas-induced proteome alterations were compared with those of other cell death inducers, indicating specific physiological characteristics of different cell death mechanisms, consequent to as well as independent of caspase activation.