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Sökning: WFRF:(Kaiser Anette)

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1.
  • Kaiser, Niclas, 1973-, et al. (författare)
  • Depression and anxiety in the reindeer-herding Sami population of Sweden
  • 2010
  • Ingår i: International Journal of Circumpolar Health. - Oulu : International Association of Circumpolar Health Publishers. - 1239-9736 .- 2242-3982. ; 69:4, s. 383-393
  • Tidskriftsartikel (refereegranskat)abstract
    • Objectives. The objective of this study was to investigate symptoms and predicting factors of depression and anxiety among reindeer-herding Sami in Sweden. Study design. A total of 319 reindeer-herding Sami (168 men, 151 women) were compared with urban and rural reference populations comprising 1,393 persons (662 men, 731 women). Methods. A cross-sectional questionnaire study on mental health, which included the Hospital Anxiety and Depression Scale (HADS). Data were analysed with regard to population, gender, age group, education and work-related stress. Results. The Sami population disclosed higher mean values for both depression and anxiety than the reference groups, with Sami men reporting the highest rates. Work-related stress was associated with anxiety and depression in the Sami group. Conclusions. By comparing Sami men and women with reference groups of men and women living in urban and rural areas in northern Sweden, this study identified that reindeer-herding Sami men require special attention with regard to mental health problems.
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2.
  • Yang, Zhenlin, et al. (författare)
  • Structural basis of ligand binding modes at the neuropeptide Y Y-1 receptor
  • 2018
  • Ingår i: Nature. - : Springer Science and Business Media LLC. - 0028-0836 .- 1476-4687. ; 556:7702, s. 520-524
  • Tidskriftsartikel (refereegranskat)abstract
    • Neuropeptide Y (NPY) receptors belong to the G-protein-coupled receptor superfamily and have important roles in food intake, anxiety and cancer biology(1,2). The NPY-Y receptor system has emerged as one of the most complex networks with three peptide ligands (NPY, peptide YY and pancreatic polypeptide) binding to four receptors in most mammals, namely the Y-1, Y-2, Y-4 and Y-5 receptors, with different affinity and selectivity(3). NPY is the most powerful stimulant of food intake and this effect is primarily mediated by the Y-1 receptor (Y1R)(4). A number of peptides and small-molecule compounds have been characterized as Y1R antagonists and have shown clinical potential in the treatment of obesity(4), tumour(1) and bone loss(5). However, their clinical usage has been hampered by low potency and selectivity, poor brain penetration ability or lack of oral bioavailability(6). Here we report crystal structures of the human Y1R bound to the two selective antagonists UR-MK299 and BMS-193885 at 2.7 and 3.0 angstrom resolution, respectively. The structures combined with mutagenesis studies reveal the binding modes of Y1R to several structurally diverse antagonists and the determinants of ligand selectivity. The Y1R structure and molecular docking of the endogenous agonist NPY, together with nuclear magnetic resonance, photo-crosslinking and functional studies, provide insights into the binding behaviour of the agonist and for the first time, to our knowledge, determine the interaction of its N terminus with the receptor. These insights into Y1R can enable structure-based drug discovery that targets NPY receptors.
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