17 research outputs found

    Exploring the EQ-5D Dimension of Pain/Discomfort in Dermatology Outpatients from a Multicentre Study in 13 European Countries

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    Pain and discomfort are important symptoms in dermatology. The aim of this cross-sectional, multicentre study was to describe the prevalence of pain/discomfort and its associations in patients with several dermatological conditions across 13 European countries. The outcome was the prevalence of pain/discomfort according to a question of the EQ-5D questionnaire. Data collected from November 2011 to February 2013 were complete for 3,509 consecutive outpatients. Moderate or extreme pain/discomfort was reported by 55.5% of patients and 31.5% of controls with no skin conditions. The highest proportions were reported by patients with hidradenitis suppurativa (92.9%), leg ulcer (81.4%), prurigo (80%) and lichen planus (75.6%). Pain/discomfort was associated with older age, low educational level, clinical severity, flare on scalp or hands, itch, depression, anxiety, low quality of life, and thoughts of suicide. It is important to enquire specifically about pain/discomfort during clinical consultations and to address it when planning a patient's care.publishedVersio

    Development of a novel yeast cell-based system for studying the aggregation of Alzheimer's disease-associated A beta peptides in vivo

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    Alzheimer's disease is the most common neurodegenerative disease, affecting -50% of humans by age 85. The disease process is associated with aggregation of the AP peptides, short 39-43 residue peptides generated through endoproteolytic cleavage of the Alzheimer's precursor protein. While the process of aggregation of purified AP peptides in vitro is beginning to be well understood, little is known about this process in vivo. In the present study, we use the yeast Saccharomyces cerevisiae as a model system for studying A beta-mediated aggregation in an organism in vivo. One of this yeast's endogenous prions, Sup35/[PSI+] loses the ability to aggregate when the prion-forming domain of this protein is deleted. We show that insertion of AP pepticle sequences in place of the original prion domain of this protein restores its ability to aggregate. However, the aggregates are qualitatively different from [PSI+] prions in their sensitivity to detergents and in their requirements on transacting factors that are normally needed for [PSI+] propagation. We conclude that we have established a useful new tool for studying the aggregation of AP peptides in an organism in vivo
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