| 1. |
- Moberg, Christina, et al.
(författare)
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De unga gör helt rätt när de stämmer staten
- 2022
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Ingår i: Aftonbladet. - 1103-9000.
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Tidskriftsartikel (populärvet., debatt m.m.)abstract
- 1 620 forskare och lärare i forskarvärlden: Vi ställer oss bakom Auroras klimatkrav
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| 2. |
- Bernander, Stig, et al.
(författare)
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Downhill progressive landslides in long natural slopes: triggering agents and landslide phases modeled with a finite difference method
- 2016
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Ingår i: Canadian geotechnical journal (Print). - : Canadian Science Publishing. - 0008-3674 .- 1208-6010. ; 53:10, s. 1565-1582
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Tidskriftsartikel (refereegranskat)abstract
- A large landslide in Tuve (Gothenburg, Sweden 1977) initiated the development of a model for slope stability analysis taking the deformation-softening of soft sensitive clays into consideration. The model studies triggering agents and five phases in progressive slope failure are identified: (1) in-situ, (2) disturbance, (3) unstable ‘dynamic’, (4) transitory (or permanent) equilibrium, and (5) ‘global’ failure. The clay resistance in these phases may differ widely; mostly due to different rates of loading. Two time dependent failure criteria are defined: (i) the triggering load condition in the disturbance Phase (2), and (ii) the transitory equilibrium in Phase (4), indicating whether minor downhill displacements or a veritable landslide catastrophe will occur. The analysis explains why downhill landslides tend to spread over vast areas of almost horizontal ground further down-slope. The model has been applied to landslides in Scandinavia and Canada. Three case studies are briefly discussed. The model is a finite difference approach, where local downhill deformations caused by normal forces is maintained compatible with deviatory shear deformations above the potential (or the established) failure surface. Software and an easy-to-use spreadsheet are introduced as well as recent developments. See also Video Abstract.
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| 3. |
- Larsson, Bengt, et al.
(författare)
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Molecular oxygen in the rho Ophiuchi cloud
- 2007
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Ingår i: Astronomy & Astrophysics. - : EDP Sciences. - 0004-6361 .- 1432-0746. ; 466:3, s. 5-
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Tidskriftsartikel (refereegranskat)abstract
- Context: Molecular oxygen, O2, has been expected historically to be an abundant component of the chemical species in molecular clouds and, as such, an important coolant of the dense interstellar medium. However, a number of attempts from both ground and from space have failed to detect O2 emission.Aims: The work described here uses heterodyne spectroscopy from space to search for molecular oxygen in the interstellar medium. Methods: The Odin satellite carries a 1.1 m sub-millimeter dish and a dedicated 119 GHz receiver for the ground state line of O2. Starting in 2002, the star forming molecular cloud core ρ Oph A was observed with Odin for 34 days during several observing runs.Results: We detect a spectral line at v_LSR =+3.5 km s-1 with Δ v_FWHM=1.5 km s-1, parameters which are also common to other species associated with ρ Oph A. This feature is identified as the O2 (NJ = 11 - 1_0) transition at 118 750.343 MHz.Conclusions: The abundance of molecular oxygen, relative to H{2} , is 5 × 10-8 averaged over the Odin beam. This abundance is consistently lower than previously reported upper limits.Based on observations with Odin, a Swedish-led satellite project funded jointly by the Swedish National Space Board (SNSB), the Canadian Space Agency (CSA), the National Technology Agency of Finland (Tekes) and Centre National d'Étude Spatiale (CNES). The Swedish Space Corporation has been the industrial prime contractor and also is operating the satellite. Appendix A is only available in electronic form at http://www.aanda.org
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| 4. |
- Åberg, Anna, et al.
(författare)
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Helicobacter pylori adapts to chronic infection and gastric disease via ph-responsive baba-mediated adherence
- 2017
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Ingår i: Cell Host and Microbe. - : Elsevier BV. - 1931-3128 .- 1934-6069. ; 21:3, s. 376-389
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Tidskriftsartikel (refereegranskat)abstract
- The BabA adhesin mediates high-affinity binding of Helicobacter pylori to the ABO blood group antigen-glycosylated gastric mucosa. Here we show that BabA is acid responsive-binding is reduced at low pH and restored by acid neutralization. Acid responsiveness differs among strains; often correlates with different intragastric regions and evolves during chronic infection and disease progression; and depends on pH sensor sequences in BabA and on pH reversible formation of high-affinity binding BabA multimers. We propose that BabA's extraordinary reversible acid responsiveness enables tight mucosal bacterial adherence while also allowing an effective escape from epithelial cells and mucus that are shed into the acidic bactericidal lumen and that bio-selection and changes in BabA binding properties through mutation and recombination with babA-related genes are selected by differences among individuals and by changes in gastric acidity over time. These processes generate diverse H. pylori subpopulations, in which BabA's adaptive evolution contributes to H. pylori persistence and overt gastric disease.
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| 5. |
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| 6. |
- Adolfsson, Dan E., 1989-, et al.
(författare)
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Intramolecular Povarov Reactions for the Synthesis of Chromenopyridine fused 2-Pyridone Polyheterocycles Binding to α-Synuclein and Amyloid-β fibrils
- 2020
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Ingår i: Journal of Organic Chemistry. - : American Chemical Society (ACS). - 0022-3263 .- 1520-6904. ; 85:21, s. 14174-14189
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- A BF3×OEt2 catalyzed intramolecular Povarov reaction was used to synthesize a library of 15 chromenopyridine fused thiazolino-2-pyridone peptidomimetics. The reaction works with a range of O-alkylated salicylaldehydes and amino functionalized thiazolino-2-pyridones, to generate polyheterocycles with diverse substitution. The synthesized compounds were screened for their ability to bind α-synuclein and amyloid β fibrils in vitro. Analogs substituted with a nitro group bind to mature amyloid fibrils, and the activity moreover depends on the positioning of this functional group.
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| 7. |
- Allard, Anna, et al.
(författare)
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Småbiotopsuppföljning i NILS år 2008
- 2009
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Rapport (övrigt vetenskapligt/konstnärligt)abstract
- Denna rapport presenterar resultat för mängden av småbiotoper vid åkermark i det svenska landskapet. Analyserna görs på uppdrag av Jordbruksverket, som underlag för bl.a. utvärderingen av miljökvalitetsmålet Ett rikt odlingslandskap. Särskilda rutiner har tagits fram för att aggregera olika variabler för att välja ut de småbiotoper som uppfyller de krav som Jordbruksverket har ställt upp, ur den befintliga databasen. Urvalet av småbiotoper är anpassat för att överensstämma med det urval av objekt som ingår i det s.k. KULT-stödet (miljöersättning till lantbrukare för skötsel av värdefulla natur- och kulturmiljöer) inom Jordbruksverkets Landsbygdsprogram. Arbetet har utförts vid institutionen för skoglig resurshushållning, Sveriges lantbruks-universitet, Umeå. Resultaten baseras på data från flygbildsinventeringen inom det nationella miljöövervakningsprogrammet NILS (Nationell Inventering av Landskapet i Sverige) vilket följer tillstånd och förändringar i det svenska landskapet och hur dessa påverkar förutsättningarna för den biologiska mångfalden. NILS finansieras av Naturvårdsverket, och ingår där i programområde Landskap. Ett viktigt syfte med programmet är att följa upp de nationella miljökvalitetsmålen för olika naturtyper och fungera som underlag för att se om genomförda policybeslut och miljövårdsåtgärder leder till önskade förbättringar
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| 8. |
- Brännström, Kristoffer, et al.
(författare)
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Aβ peptide fibrillar architectures controlled by conformational constraints of the monomer
- 2011
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Ingår i: PLOS ONE. - San Francisco, CA : Public Library of Science. - 1932-6203. ; 6:9, s. e25157-
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Tidskriftsartikel (refereegranskat)abstract
- Anomalous self-assembly of the Aβ peptide into fibrillar amyloid deposits is strongly correlated with the development of Alzheimer's disease. Aβ fibril extension follows a template guided "dock and lock" mechanism where polymerisation is catalysed by the fibrillar ends. Using surface plasmon resonance (SPR) and quenched hydrogen-deuterium exchange NMR (H/D-exchange NMR), we have analysed the fibrillar structure and polymerisation properties of both the highly aggregation prone Aβ1-40 Glu22Gly (Aβ(40Arc)) and wild type Aβ1-40 (Aβ(40WT)). The solvent protection patterns from H/D exchange experiments suggest very similar structures of the fibrillar forms. However, through cross-seeding experiments monitored by SPR, we found that the monomeric form of Aβ(40WT) is significantly impaired to acquire the fibrillar architecture of Aβ(40Arc). A detailed characterisation demonstrated that Aβ(40WT) has a restricted ability to dock and isomerise with high binding affinity onto Aβ(40Arc) fibrils. These results have general implications for the process of fibril assembly, where the rate of polymerisation, and consequently the architecture of the formed fibrils, is restricted by conformational constraints of the monomers. Interestingly, we also found that the kinetic rate of fibril formation rather than the thermodynamically lowest energy state determines the overall fibrillar structure.
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| 9. |
- Brännström, Kristoffer, et al.
(författare)
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Ca2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner
- 2013
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Ingår i: Biochemical Journal. - : Portland Press. - 0264-6021 .- 1470-8728. ; 450, s. 189-197
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Tidskriftsartikel (refereegranskat)abstract
- Identifying factors that affect the self-assembly of the amyloid-β peptide (Aβ) is of utmost importance in the quest to understand the molecular mechanisms causing Alzheimer's disease (AD). Ca2+ has previously been shown to accelerate both Aβ fibril nucleation and maturation, and a dysregulated Ca2+ homeostasis frequently correlates with development of AD. The mechanisms regarding Ca2+ binding as well as its effect on fibril kinetics are not fully understood. Using a polymerization assay we show that Ca2+ in a dynamic and reversible manner enhances both the elongation rate and fibrillar stability, where specifically the "dock and lock" phase mechanism is enhanced. Through NMR analysis we found that Ca2+ affects the fibrillar architecture. In addition, and unexpectedly, we found that Ca2+ does not bind the free Aβ monomer. This implies that Ca2+ binding requires an architecture adopted by assembled peptides, and consequently is mediated through intermolecular interactions between adjacent peptides. This gives a mechanistic explanation to the enhancing effect on fibril maturation and indicates structural similarities between prefibrillar structures and mature amyloid. Taken together we expose how Ca2+ levels affect the delicate equilibrium between the monomeric and assembled Aβ and how fluctuations in vivo may contribute to development and progression of the disease.
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| 10. |
- Brännström, Kristoffer, et al.
(författare)
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Characterization of SPINK9, a KLK5-specific inhibitor expressed in palmo-plantar epidermis
- 2012
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Ingår i: Biological chemistry (Print). - : Walter de Gruyter. - 1431-6730 .- 1437-4315. ; 393:5, s. 369-377
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Tidskriftsartikel (refereegranskat)abstract
- SPINK9, a Kazal-type serine protease inhibitor, is almost exclusively expressed in the palmo-plantar epidermis. SPINK9 selectively inhibits kallikrein-related peptidase 5 (KLK5), no other target enzyme is known at present. In this study, we defined the reactive loop to residues 48 and 49 of SPINK9 and characterized the inhibition and binding of different SPINK9 variants towards KLK5, KLK7, KLK8 and KLK14. Substitutions of single amino acids in the reactive loop had a large impact on both inhibitory efficiency and specificity. Binding studies showed that it is mainly the dissociation rate that is affected by the amino acid substitutions. The inhibitory effect of wild-type SPINK9 was clearly pH-dependent with an improved effect at a pH similar to that of the outer layers of the skin. Modeling of the enzyme-inhibitor complexes showed that the reactive loop of SPINK9 fits very well into the deep negatively charged binding pocket of KLK5. A decrease in pH protonates His48 of the wild-type protein resulting in a positively charged residue, thereby explaining the observed decreased dissociation rate. Interestingly, substitution with a positively charged amino acid at position 48 resulted in a more efficient inhibitor at higher pH.
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