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- Toledano, C., et al.
(författare)
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Overview of sun photometer measurements of aerosol properties in Scandinavia and Svalbard
- 2012
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Ingår i: Atmospheric Environment. - : Elsevier BV. - 1352-2310 .- 1873-2844. ; 52, s. 18-28
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Tidskriftsartikel (refereegranskat)abstract
- An overview on the data of columnar aerosol properties measured in Northern Europe is provided. Apart from the necessary data gathered in the Arctic, the knowledge of the aerosol loading in nearby areas (e.g. sub-Arctic) is of maximum interest to achieve a correct analysis of the Arctic aerosols and transport patterns. This work evaluates data from operational sites with sun photometer measurements belonging either to national or international networks (AERONET, GAW-PFR) and programs conducted in Scandinavia and Svalbard. We enumerate a list of sites, measurement type and periods together with observed aerosol properties. An evaluation and analysis of aerosol data was carried out with a review of previous results as well. Aerosol optical depth (AOD) and Angstrom exponent (AE) are the current parameters with sufficient long-term records for a first evaluation of aerosol properties. AOD (500 nm) ranges from 0.08 to 0.10 in Arctic and sub-Arctic sites (Ny-Alesund: 0.09; Andenes: 0.10; Sodankyla: 0.08), and it is somewhat higher in more populated areas in Southern Scandinavia (AOD about 0.10-0.12 at 500 nm). On the Norwegian coast, aerosols show larger mean size (AE = 1.2 at Andenes) than in Finland, with continental climate (AE = 1.5 at Sodankyla). Columnar particle size distributions and related parameters derived from inversion of sun/sky radiances were also investigated. This work makes special emphasis in the joint and collaborative effort of the various groups from different countries involved in this study. Part of the measurements presented here were involved in the IPY projects Polar-AOD and POLARCAT.
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- Brito-Zerón, Pilar, et al.
(författare)
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Mortality risk factors in primary Sjögren syndrome : a real-world, retrospective, cohort study
- 2023
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Ingår i: eClinicalMedicine. - : Elsevier. - 2589-5370. ; 61
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Tidskriftsartikel (refereegranskat)abstract
- BackgroundWhat baseline predictors would be involved in mortality in people with primary Sjögren syndrome (SjS) remains uncertain. This study aimed to investigate the baseline characteristics collected at the time of diagnosis of SjS associated with mortality and to identify mortality risk factors for all-cause death and deaths related to systemic SjS activity measured by the ESSDAI score.MethodsIn this international, real-world, retrospective, cohort study, we retrospectively collected data from 27 countries on mortality and causes of death from the Big Data Sjögren Registry. Inclusion criteria consisted of fulfilling 2002/2016 SjS classification criteria, and exclusion criteria included chronic HCV/HIV infections and associated systemic autoimmune diseases. A statistical approach based on a directed acyclic graph was used, with all-cause and Sjögren-related mortality as primary endpoints. The key determinants that defined the disease phenotype at diagnosis (glandular, systemic, and immunological) were analysed as independent variables.FindingsBetween January 1st, 2014 and December 31, 2023, data from 11,372 patients with primary SjS (93.5% women, 78.4% classified as White, mean age at diagnosis of 51.1 years) included in the Registry were analysed. 876 (7.7%) deaths were recorded after a mean follow-up of 8.6 years (SD 7.12). Univariate analysis of prognostic factors for all-cause death identified eight Sjögren-related variables (ocular and oral tests, salivary biopsy, ESSDAI, ANA, anti-Ro, anti-La, and cryoglobulins). The multivariate CPH model adjusted for these variables and the epidemiological features showed that DAS-ESSDAI (high vs no high: HR = 1.68; 95% CI, 1.27–2.22) and cryoglobulins (positive vs negative: HR = 1.72; 95% CI, 1.22–2.42) were independent predictors of all-cause death. Of the 640 deaths with available information detailing the specific cause of death, 14% were due to systemic SjS. Univariate analysis of prognostic factors for Sjögren-cause death identified five Sjögren-related variables (oral tests, clinESSDAI, DAS-ESSDAI, ANA, and cryoglobulins). The multivariate competing risks CPH model adjusted for these variables and the epidemiological features showed that oral tests (abnormal vs normal results: HR = 1.38; 95% CI, 1.01–1.87), DAS-ESSDAI (high vs no high: HR = 1.55; 95% CI, 1.22–1.96) and cryoglobulins (positive vs negative: HR = 1.52; 95% CI, 1.16–2) were independent predictors of SjS-related death.InterpretationThe key mortality risk factors at the time of SjS diagnosis were positive cryoglobulins and a high systemic activity scored using the ESSDAI, conferring a 2-times increased risk of all-cause and SjS-related death. ESSDAI measurement and cryoglobulin testing should be considered mandatory when an individual is diagnosed with SjS.
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- Padilla, C. A., et al.
(författare)
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Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin
- 1995
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Ingår i: European Journal of Biochemistry. - : Wiley-Blackwell. - 0014-2956 .- 1432-1033. ; 227:1-2, s. 27-34
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Tidskriftsartikel (refereegranskat)abstract
- Glutaredoxin is generally a glutathione-dependent hydrogen donor for ribonucleotide reductase and also catalyses general glutathione (GSH)-disulfide-oxidoreduction reactions in the presence of NADPH and glutathione reductase. A Glutaredoxin from human placenta was purified to homogeneity, as judged by SDS/PAGE and IEF (12 kDa). Purification was monitored by the activity with hydroxyethyl disulfide as a substrate. Values of pI for glutaredoxin were obtained by IEF; the pI of the protein shifted from 7.3 in its fully reduced state to 9.0 in the oxidized state after treatment with excess hydroxyethyl disulfide. The glutaredoxin preparation showed GSH-dependent hydrogen-donor activity with recombinant mouse ribonucleotide reductase, it exhibited dehydroascorbate reductase activity as well as hydroxyethyl-disulfide-reducing activity. The amino acid sequence (residues 3-104) of glutaredoxin was determined by peptide sequencing and residues 1, 2 and 105 by cDNA sequence analysis. The glutaredoxin sequence comprised the classical active site for glutaredoxins -Cys22-Pro-Tyr-Cys25- and three additional half-cystine residues; two of these in positions 78 and 82. The sequence was similar to other known mammalian glutaredoxins (about 80% identities), with important differences such as one additional Cys residue (Cys7) and no Met residue. The sequence of human glutaredoxin was compared to that of Escherichia coli glutaredoxin with known three-dimensional structure in solution to identify conserved residues and predict a structure from alignment. In particular the GSH-binding site of glutaredoxin was conserved between all molecules. A cDNA that encodes the entire glutaredoxin gene (grx) and flanking sequences was isolated from a human spleen cDNA library. The nucleotide sequence of this cDNA (0.8 kb) was determined, including the complete grx gene.
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