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- Jonsson, J, et al.
(författare)
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Measuring precarious employment in Sweden: translation, adaptation and psychometric properties of the Employment Precariousness Scale (EPRES)
- 2019
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Ingår i: BMJ open. - : BMJ. - 2044-6055. ; 9:9, s. e029577-
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Tidskriftsartikel (refereegranskat)abstract
- Precarious employment (PE) is a determinant of poor health and health inequality. However, the evidence of health consequences and mechanisms underlying the associations, are still limited due to a lack of a comprehensive multidimensional definition and measurement instrument. The Employment Precariousness Scale (EPRES) is a Spanish, multidimensional scale, developed to measure degree of PE. The aim of this study was to translate the EPRES-2010 into Swedish, adapt it to the Swedish context and to assess the psychometric properties of the Swedish EPRES.MethodEPRES was translated, adapted and implemented for data collection within the research project PRecarious EMployment in Stockholm (PREMIS). During 2016–2017, questionnaire data were collected from 483 non-standard employees in Stockholm, Sweden, sampled with web-based respondent-driven sampling. Analyses included item descriptive statistics, scale descriptive statistics and exploratory factor analysis.ResultsThe final EPRES-Se (Swedish version of the EPRES),consisted of six dimensions and 23 items. There was a high response rate to all items and response options. Global Cronbach’s alpha was 0.83. Subscales ‘vulnerability’, ‘rights’ and ‘exercise rights’ had reliability coefficients between α=0.78–0.89 and item-subscale correlations between r=0.48–0.78. ‘Temporariness’ had poor reliability (α=−0.08) and inter-item correlation (r=−0.04), while ‘disempowerment’ showed acceptable psychometric properties (α=0.5; r=0.34). Exploratory factor analysis confirmed the original EPRES factor structure.Conclusions‘Vulnerability’, ‘wages’, ‘rights’, ‘exercise rights’ and ‘disempowerment’ worked in the Swedish context; however, ‘temporariness’ would need revising before implementing the EPRES-Se in further research. Continued work and validation of EPRES-Se is encouraged. In order to enable international comparisons and multinational studies, similar studies in other European countries are also called for.
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| 3. |
- Matilla-Santander, N, et al.
(författare)
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The Relation Between Precarious Employment Arrangements and Social Precarity: Findings from the PREMIS Study in Stockholm, Sweden
- 2022
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Ingår i: International journal of health services : planning, administration, evaluation. - : SAGE Publications. - 1541-4469 .- 0020-7314. ; 52:2, s. 201-211
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Tidskriftsartikel (refereegranskat)abstract
- Precarious employment (PE) is a well-known social determinant of health and health inequalities. However, as most previous studies have focused on physical and mental well-being, less is known about the social-related outcomes (ie, social precarity) associated with precarious arrangements. This cross-sectional study aims to investigate whether PE is associated with social precarity in a working population of 401 nonstandard employed workers in Stockholm, Sweden (2016-2017). PE was assessed with the Swedish version of the Employment Precarious Scale (EPRES-Se) and analyzed in relation to social precarity related to working life (eg, task quality and job security) and living conditions (eg, restraint in social activities and financial constraints). We found positive adjusted associations between quartiles of EPRES-Se and social precarity related to working life (eg, being locked in an occupation [aPRq4:1.33 [1.10-1.61]]) and living conditions (eg, inability to participate in social activities because of work [aPRq4:1.27 [1.10-1.46]]). Our findings suggest that individuals in PE experience social precarity, stressing that PE may have negative effects on well-being. Further studies using multidimensional constructs of PE and larger samples should analyze these findings according to social and policy contexts in order to be able to inform policymakers.
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| 7. |
- Benach, J, et al.
(författare)
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Structure of bacterial 3 beta/17 beta-hydroxysteroid dehydrogenase at 1.2 angstrom resolution : A model for multiple steroid recognition
- 2002
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 41:50, s. 14659-14668
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Tidskriftsartikel (refereegranskat)abstract
- The enzyme 3beta/17beta-hydroxysteroid dehydrogenase (3beta/17beta-HSD) is a steroid-inducible component of the Gram-negative bacterium Conramonas testosteroni. It catalyzes the reversible reduction/ dehydrogenation of the oxo/beta-hydroxy groups at positions 3 and 17 of steroid compounds, including hormones and isobile acids. Crystallographic analysis at 1.2 Angstrom resolution reveals the enzyme to have nearly identical subunits that form a tetramer with 222 symmetry. This is one of the largest oligomeric structures refined at this resolution. The subunit consists of a monomer with a single-domain structure built around a seven-stranded beta-sheet flanked by six alpha-helices. The active site contains a Ser-Tyr-Lys triad, typical for short-chain dehydrogenases/reductases (SDR). Despite their highly diverse substrate specificities, SDR members show a close to identical folding pattern architectures and a common catalytic mechanism. In contrast to other SDR apostructures determined, the substrate binding loop is well-defined. Analysis of structure-activity relationships of catalytic cleft residues, docking analysis of substrates and inhibitors, and accessible surface analysis explains how 3beta/17beta-HSD accommodates steroid substrates of different conformations.
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| 12. |
- Chung, H., et al.
(författare)
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Welfare State Regimes, Gender, and Depression: A Multilevel Analysis of Middle and High Income Countries
- 2013
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Ingår i: International Journal of Environmental Research and Public Health. - : MDPI AG. - 1660-4601. ; 10:4, s. 1324-1341
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Tidskriftsartikel (refereegranskat)abstract
- Using the 2002 World Health Survey, we examine the association between welfare state regimes, gender and mental health among 26 countries classified into seven distinct regimes: Conservative, Southeast Asian, Eastern European, Latin American, Liberal, Southern/Ex-dictatorship, and Social Democratic. A two-level hierarchical model found that the odds of experiencing a brief depressive episode in the last 12 months was significantly higher for Southern/Ex- dictatorship countries than for Southeast Asian (odds ratio (OR) = 0.12, 95% confidence interval (CI) 0.05-0.27) and Eastern European (OR = 0.36, 95% CI 0.22-0.58) regimes after controlling for gender, age, education, marital status, and economic development. In adjusted interaction models, compared to Southern/Ex-dictatorship males (reference category), the odds ratios of depression were significantly lower among Southeast Asian males (OR = 0.16, 95% CI 0.08-0.34) and females (OR = 0.23, 95% CI 0.10-0.53) and Eastern European males (OR = 0.41, 95% CI 0.26-0.63) and significantly higher among females in Liberal (OR = 2.00, 95% CI 1.14-3.49) and Southern (OR = 2.42, 95% CI 1.86-3.15) regimes. Our results highlight the importance of incorporating middle-income countries into comparative welfare regime research and testing for interactions between welfare regimes and gender on mental health.
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| 14. |
- Filling, C, et al.
(författare)
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Critical residues for structure and catalysis in short-chain dehydrogenases/reductases
- 2002
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 277:28, s. 25677-25684
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Tidskriftsartikel (refereegranskat)abstract
- Short-chain dehydrogenases/reductases form a large, evolutionarily old family of NAD(P)(H)-dependent enzymes with over 60 genes found in the human genome. Despite low levels of sequence identity (often 10-30%), the three-dimensional structures display a highly similar alpha/beta folding pattern. We have analyzed the role of several conserved residues regarding folding, stability, steady-state kinetics, and coenzyme binding using bacterial 3beta/17beta-hydroxysteroid dehydrogenase and selected mutants. Structure determination of the wildtype enzyme at 1.2-Angstrom resolution by x-ray crystallography and docking analysis was used to interpret the biochemical data. Enzyme kinetic data from mutagenetic replacements emphasize the critical role of residues Thr-12, Asp-60, Asn-86, Asn-87, and Ala-88 in coenzyme binding and catalysis. The data also demonstrate essential interactions of Asn-111 with active site residues. A general role of its side chain interactions for maintenance of the active site configuration to build up a proton relay system is proposed. This extends the previously recognized catalytic triad of Ser-Tyr-Lys residues to form a tetrad of Asn-Ser-Tyr-Lys in the majority of characterized short-chain dehydrogenases/reductase enzymes.
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| 15. |
- Filling, C, et al.
(författare)
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Structural role of conserved Asn179 in the short-chain dehydrogenase/reductase scaffold
- 2001
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Ingår i: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 289:3, s. 712-717
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Tidskriftsartikel (refereegranskat)abstract
- Short-chain dehydrogenases/reductases (SDR) constitute a large family of enzymes found in all forms of life. Despite a low level of sequence identity, the three-dimensional structures determined display a nearly superimposable alpha/beta folding pattern. We identified a conserved asparagine residue located within strand betaF and analyzed its role in the short-chain dehydrogenase/reductase architecture. Mutagenetic replacement of Asn179 by Ala in bacterial 3 beta /17 beta -hydroxysteroid dehydrogenase yields a folded, but enzymatically inactive enzyme, which is significantly more resistant to denaturation by guanidinium hydrochloride. Crystallographic analysis of the wild-type enzyme at 1.2-Angstrom resolution reveals a hydrogen bonding network, including a buried and well-ordered water molecule connecting strands betaE to betaF, a common feature found in 16 of 21 known three-dimensional structures of the family. Based on these results, we hypothesize that in mammalian 11 beta -hydroxysteroid dehydrogenase the essential Asn-linked glycosylation site, which corresponds to the conserved segment, displays similar structural features and has a central role to maintain the SDR scaffold.
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| 16. |
- Giskes, K, et al.
(författare)
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Trends in smoking behaviour between 1985 and 2000 in nine European countries by education
- 2005
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Ingår i: Journal of Epidemiology and Community Health. - : BMJ. - 1470-2738 .- 0143-005X. ; 59:5, s. 395-401
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Tidskriftsartikel (refereegranskat)abstract
- Objective: To examine whether trends in smoking behaviour in Western Europe between 1985 and 2000 differed by education group. Design: Data of smoking behaviour and education level were obtained from national cross sectional surveys conducted between 1985 and 2000 (a period characterised by intense tobacco control policies) and analysed for countries combined and each country separately. Annual trends in smoking prevalence and the quantity of cigarettes consumed by smokers were summarised for each education level. Education inequalities in smoking were examined at four time points. Setting: Data were obtained from nine European countries: Norway, Sweden, Denmark, Finland, the United Kingdom, the Netherlands, Germany, Italy, and Spain. Participants: 451 386 non-institutionalised men and women 25-79 years old. Main outcome measures: Smoking status, daily quantity of cigarettes consumed by smokers. Results: Combined country analyses showed greater declines in smoking and tobacco consumption among tertiary educated men and women compared with their less educated counterparts. In country specific analyses, elementary educated British men and women, and elementary educated Italian men showed greater declines in smoking than their more educated counterparts. Among Swedish, Finnish, Danish, German, Italian, and Spanish women, greater declines were seen among more educated groups. Conclusions: Widening education inequalities in smoking related diseases may be seen in several European countries in the future. More insight into effective strategies specifically targeting the smoking behaviour of low educated groups may be gained from examining the tobacco control policies of the UK and Italy over this period.
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| 21. |
- Oppermann, U C T, et al.
(författare)
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Active site directed mutagenesis of 3 beta/17 beta-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions
- 1997
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 36:1, s. 34-40
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Tidskriftsartikel (refereegranskat)abstract
- Mutagenetic replacements uf conserved residues within the active site of the short-chain dehydrogenase/reductase (SDR) superfamily were studied using prokaryotic 3 beta/17 beta-hydroxysteroid dehydrogenase (3 beta/17 beta-HSD) from Comamonas testosteroni as a model system. The results provide novel data to establish Ser138 as a member of a catalytically important ''triad'' of residues also involving Tyr151 and Lys155. A Ser --> Ala exchange at position 138 results in an almost complete (>99.9%) loss of enzymatic activity, which is not observed with a Ser --> Thr replacement. This indicates that an essential factor for catalysis is the ability of side chain 138 to form hydrogen bond interactions. Mutations in the NAD(H) binding region, in strands beta A, beta D, and adjacent turns, reveal two additional residues, Thr12 and Asn87, which are important for correct binding of the coenzyme aad with a differential effect on the reactions catalyzed. Thus, mutation of Thr12 to Ala results in a complete loss of the 3 beta-dehydrogenase activity, whereas the 3-oxoreductase activity remains unchanged. On the other hand, a T12S substitution yields a protein with unaltered catalytic constants for both reactions, revealing that a specific hydrogen bond is critical for the dehydrogenase activity. Our interpretation of the available crystal structure of 3 alpha/20 beta-HSD from Streptomyces hydrogenans suggests a hydrogen her-id in that enzyme between the Thr12 side chain and the backbone NW of Asn87 rather than the coenzyme, indicating that this hydrogen bond to the beta D strand might determine a crucial difference between the reductive and the oxidative reaction types. Similarly, mutation of Asn87 to Ala results in an 80% reduction of K-cat/K-m in the dehydrogenase direction but also unchanged 3-oxoreductase propel ties. It appears that the binding of NAD(+) to the protein is influenced by local structural changes involving strand beta D and beta A to alpha B.
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