Search

An international project, which is part funded by the EU, has established a transparent generic method for assessing and ranking restoration strategies (RESTRAT) for radioactivity contaminated sites and their close surroundings. The decision-making procedure is based on multi-attribute utility analysis, which is considered superior to conventional cost-benefit analysis because criteria can be incorporated without the need to convert them into common units of measurement. In this study the attributes considered are radiation-induced health effects, monetary costs and social factors. These may be broken down into aseries of sub-attributes and can be combined through a series of utility functions and weighting factors. A probabilistic approach is adopted to take account of the uncertainties associated with the utilityfunctions and weighting factors. Restoration techniques are described in terms which allow these attributes to be determined. The application of this approach is illustrated in a worked example for Lake Tranebarssjon in Sweden. [ABSTRACT FROM AUTHOR]

Medical education has evolved over time toward a model which integrates clinical medicine with the basic sciences. More recently, medical education has put an emphasis on outcome-based education. Other areas of health care education have had a similar emphasis which can provide models to inform a new model for medical education. The Roseman University of Health Sciences has developed and implemented a model based on underlying tenets of mastery learning since 1999. The model has been implemented in pharmacy, nursing, and dental education. It was conceived as an integration of 6 key points which reinforce each other and interrelate to support learning. The model has been modified for application to medical education in support of medical education's outcome-based emphasis and to address the educational demands of the changing environment of the practice of medicine., Competing Interests: Declaration of conflicting interests:The author(s) declared no potential conflicts of interest with respect to the research, authorship, and/or publication of this article.

Education for professional nursing practice has undergone a significant shift over the last few decades impacting nursing practice and the relationship between nurses. Enhancing professional practice and acting as a conduit for empowering nurses to be active participants in their learning and development is Practice Development. This action research project with philosophical premises of critical companionship and human flourishing aimed to develop the knowledge and skills of registered nurses in their ability to provide clinical supervision of nursing students in practice. The overall project consisted of two action research cycles in two different health facilities. Participants in both projects identified similar issues and common learning needs including; how to better understand and develop skills in reflective practice; how to provide a positive learning and enabling environment; and how to provide effective solution focused feedback. Workshop facilitators witnessed the flourishing of participants as they were enabled to negotiate their learning requirements; grow and develop in their roles over the workshop series. Participants themselves identified personal growth in skills, knowledge and confidence in being a preceptor as a result of the workshops in the study. Overall, this study has resulted in the development and capacity building of the nursing workforce clinical placement capacity through the development of clinical supervisors., (Copyright © 2017 Elsevier Ltd. All rights reserved.)

The non-homologous end joining pathway uses pre-existing proteins to repair DNA double-strand breaks induced by ionizing radiation. Here we describe manipulation of this pathway in living cells using a newly developed tool. We generated a single chain antibody variable fragment (scFv) that binds to the DNA-dependent protein kinase catalytic subunit (DNA-PKcs), a key enzyme in the pathway. In contrast to existing pharmacologic inhibitors, the scFv binds a newly defined regulatory site outside the kinase catalytic domain. Although the scFv inhibits kinase activity only modestly, it completely blocks DNA end joining in a cell-free system. Microinjection of the scFv sensitizes human cells to radiation, as measured by a reduction in efficiency of colony formation and induction of apoptosis at an otherwise sublethal dose of 1.5 Gy. The scFv blocks non-homologous end joining in situ at a step subsequent to histone gamma-H2AX focus formation but preceding gamma-H2AX dephosphorylation. Blockage occurs in cells exposed to as little as 0.1 Gy, indicating that DNA-PKcs is essential for double-strand break repair even at low radiation doses. The ability to modify the radiation response in situ in living cells provides a link between biochemical, genetic and cytologic approaches to the study of double-strand break repair intermediates.

UDP-N-acetyl-d-galactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGaNTases) catalyse the initial step of mucin-type O-glycosylation. The activity of bovine ppGaNTase-T1 isoenzyme was inhibited by diethyl pyrocarbonate (DEPC) modification. Activity was partially restored by hydroxylamine treatment, indicating that one of the reactive residues was a histidine. The transferase was protected against DEPC inactivation when UDP-GalNAc and EPO-G, a peptide pseudo-substrate PPDAAGAAPLR, were simultaneously present, while presence of EPO-G alone did not alter DEPC inactivation. However, inclusion of UDP-GalNAc alone potentiated DEPC-inhibition of the enzyme, suggesting that UDP-GalNAc binding changes the accessibility or reactivity of an essential histidine residue. Deletion of the first 56 amino acids (including one hisitidine residue) yielded a fully active secreted form of the bovine ppGaNTase-T1 enzyme. Each of the 14 remaining histidines in the enzyme were mutated to alanine, and the recombinant mutants were recovered from COS7 cells. The mutation of histidine residues His211-->Ala and His344-->Ala resulted in recombinant proteins with no detectable enzymic activity. A significant decrease in the initial rate of GalNAc transfer to the substrate was observed with mutants His125-->Ala and His341-->Ala (1% and 6% of wild-type activity respectively). Mutation of the remaining ten histidine residues yielded mutants that were indistinguishable from the wild-type enzyme. Mutagenesis and SDS/PAGE analysis of all N-glycosylation sequons revealed that positions N-95 and N-552 are occupied by N-linked sugars in COS7 cells. Ablation of either site did not perturb enzyme biosynthesis or enzyme activity.