Publications by authors named "Nicolas A Sieben"

Background: Ventilator Associated Pneumonia is a common complication of invasively ventilated patients with significant and underestimated morbidity and mortality. Defining VAP cases is greatly varied as many definitions are used with varying success and sensitivity. This study evaluates VAP detection using four definitions in a regional Australian Intensive Care Unit (ICU).

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Protein phosphatase one (PP1) is a major eukaryotic serine/threonine protein phosphatase whose activity is controlled by targeting or regulatory subunits. Currently, very few plant protein phosphatase one regulatory subunits are known. Here, Arabidopsis GL2 EXPRESSION MODULATOR (GEM) was identified and confirmed as a protein phosphatase one binding partner.

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Background: End-of-life discussions often are not initiated until close to death, even in the presence of life-limiting illness or frailty. Previous research shows that doctors may not explicitly verbalize approaching end-of-life in the foreseeable future, despite shifting their focus to comfort care. This may limit patients' opportunity to receive information and plan for the future.

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Background: As doctors who provide care across the life-course, general practitioners (GPs) play a key role in initiating timely end-of-life discussions. Nonetheless, these discussions are often not initiated until close to death. Given the ageing of the population, GPs will be confronted with end-of-life care more often, and this needs to become a core skill for all GPs.

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Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and well-characterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr protein phosphatase that is targeted to the mitochondrial intermembrane space (IMS) where it interacts with the mitochondrial oxidoreductase import and assembly protein 40 (AtMIA40), forming a protein complex. Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2.

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